@prefix biopax:  <http://www.biopax.org/release/biopax-level3.owl#> .
@prefix cito:    <http://purl.org/spar/cito/> .
@prefix dc:      <http://purl.org/dc/elements/1.1/> .
@prefix dcterms: <http://purl.org/dc/terms/> .
@prefix foaf:    <http://xmlns.com/foaf/0.1/> .
@prefix freq:    <http://purl.org/cld/freq/> .
@prefix gpml:    <http://vocabularies.wikipathways.org/gpml#> .
@prefix obo:     <http://purl.obolibrary.org/obo/> .
@prefix owl:     <http://www.w3.org/2002/07/owl#> .
@prefix pav:     <http://purl.org/pav/> .
@prefix prov:    <http://www.w3.org/ns/prov#> .
@prefix rdf:     <http://www.w3.org/1999/02/22-rdf-syntax-ns#> .
@prefix rdfs:    <http://www.w3.org/2000/01/rdf-schema#> .
@prefix skos:    <http://www.w3.org/2004/02/skos/core#> .
@prefix void:    <http://rdfs.org/ns/void#> .
@prefix wp:      <http://vocabularies.wikipathways.org/wp#> .
@prefix wprdf:   <http://rdf.wikipathways.org/> .
@prefix xsd:     <http://www.w3.org/2001/XMLSchema#> .

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        gpml:commentText  "Serotonin treatment of these cells has been reported to inhibit forskolin-stimulated cAMP accumulation in the 5-HT 1B -expressing cells, but not the parental HeLa cells (Hamblin et al., 1992 )." .

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<https://identifiers.org/pubmed/11268>
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        gpml:commentText  "8808177 (Organ: blood vessel, CellType: neural) Stimulation of the 5-HT2A receptors by serotonin has been reported to exert an excitatory effect on neocortical neurons in rats and mice, to facilitate ischaemia-induced release of excitatory amino acids and to mediate the vasomotor constrictor component of the response of blood vessels to 5-HT. 5-HT2A receptor antagonists have, therefore, been proposed as potential protectants against the effects of cerebral ischaemia. \n\n14654098 (Organ: hippocampal, CellType: neural) High doses of 5-HT also recruited both 5-HT2 and 5-HT3 receptors, causing an increase in the rate and amplitude of sIPSCs. cOA (1 microM), in the presence of Y 25130, failed to potentiate the 5-HT2 receptor induced enhancement of sIPSCs. \n\n11157082 Since 5-HT enhances GABA release ( Liu and Alreja 1997 ), 5-HT2A receptor blockade of clozapine may directly reduce pallidal GABA release. \n\n10431683 Mirtazapine is an atypical antidepressant with alpha 2 adrenergic antagonist and serotonin 5-HT2 and 5-HT3 receptor-blocking activity. \n\n8627578 Neomycin (3 mM) inhibited maximal 5-HT-induced contraction by approximately 50% without inhibiting [3H]5-HT binding to 5-HT2A receptors. \n\n9016798 (Tissue: crypt) Superfusing 5-HT (10 microM) in the bath solution increased both K+ and Cl- currents, which were antagonized by the presence of ketanserin (1 microM), a selective 5-HT2A antagonist, in the bath solution. \n\n9272731 (Tissue: mesangia) The L-type channel blocker verapamil, however, dose-dependently (0.1-10 microM) and specifically inhibited 5-HT-elicited Ca2+ signals by interference with binding of 5-HT to 5-HT2A receptors. 5-HT-mediated Ca2+ release was reduced by 80% when protein kinase C was activated by the phorbolester TPA (0.1 microM)." .

<https://identifiers.org/pubmed/10854065>
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<https://identifiers.org/pubmed/15262987>
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<https://identifiers.org/pubmed/12584202>
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        gpml:commentText  "Prot Modification JAK2 --+> STAT3" .

<https://identifiers.org/pubmed/12181435>
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<https://identifiers.org/pubmed/9688849>
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        gpml:commentText  "12801936 (Organ: pituitar, Tissue: epithelia) ERKs are activated by the mitogen-activated protein kinase kinases, MEK1 and MEK2, which are activated by the MEK kinases, Raf-1, A-Raf, and B-Raf. \n\n10783132 (Organ: lung, Tissue: epithelia) Raf-1 and B-Raf are serine/threonine-protein kinases that selectively phosphorylate and activate MEK1 and MEK2 ( 22 ). \n\n8621389 Raf-1 and B-Raf are serine/threonine-protein kinases that selectively phosphorylate and activate MEK 1 and MEK 2( 14 , 15 , 16 , 17 ) . \n\n12351703 Next, actions of the D2 receptor on c-Raf and B-Raf, which phosphorylate MEK1/2, were examined (Fig. 10 ). \n\n8668348 We show that, consequently, B-Raf interacts with MEK-1 and MEK-2 with a better affinity than does c-Raf-1, thus strengthening the notion that B-Raf is a stronger MEK activator than c-Raf-l. \n\n15153095 (CellType: neural) In addition, MEK1/2 can be activated by B-Raf, a neuron-enriched isoform of Raf, which is in turn activated by a cAMP-responsive Ras homologue called Rap-1 [ 41 ]. \n\n9733801 (CellLineName: COS I) A , quantitative analysis of the interaction of Raf-1 and B-Raf with MEK-1 and MEK-2 in the yeast two-hybrid system. \n\n12738761 Next, actions of the D2 receptor on c-Raf and B-Raf, which phosphorylate MEK1/2, were examined (Fig. 10 )." .

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        gpml:commentText  "10969079 (Organ: brain, Tissue: spore, CellType: cardiomyocyte, CellLineName: JURKAT) Initially, MEKK1 was proposed to be an activator of MEK1/MEK2 (Lange-Carter et al. 1993 ). \n\n10226075 (Organ: trachea, CellType: myocyte) Therefore, it is unlikely that MEKK1 is a major activator of MEK1 in bovine tracheal myocytes. \n\n11278353 MEKK1 also activates ERK and JNK MAPK cascades, and Stat3 Ser-727 can be phosphorylated by multiple kinases in the MAPK cascades including MEKK1 , MEK1, and ERK/JNK. \n\n12588875 Since MEKK1 is also able to activate MEK1, the MEK1-MAPK pathway may play a role in the stimulatory effect of MEKK1. \n\n9162092 Additionally, the catalytic domain of MEKK1 activated MEK1 and MEK2 in vitro and interacted with MEK in the yeast two-hybrid system. \n\n11454875 MEKK1, in turn, targets several MEKs, including MEK1, MEK3, and MEK7 but not MEK4 ( 3 , 22 ). \n\n15491994 MEK1, activated by MEKK1, also has strong inhibitory effects on SMRT function ( solid arrows ). \n\n11698415 MEKK1, in turn, activates MEK1, MEK3, and MEK7 ( 17 , 34 ). \n\n12048245 MEKK1 activates MEK1, which in turn seems to activate the ERKs. \n\n7499206 Here we report that PD 098059 does not inhibit Raf-activated MAPKK1 but that it prevents the activation of MAPKK1 by Raf or MEK kinase in vitro at concentrations (IC50 = 2-7 microM) similar to those concentrations that inhibit dephosphorylated MAPKK1 or MAPKK1(S217E,S221E)." .

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        gpml:commentText  "10713965 PDBu-induced activation of PKC promotes the priming of secretory granules, thereby enhancing the efficacy for Ca2+ to trigger fusion/exocytosis. \n\n8429046 It appears, therefore, that the binding of Ca2+ to PKC requires a complex tertiary structure in the regulatory domain. \n\n1313322 (Tissue: articular cartilage, CellType: chondrocyte) The activity of various subspecies of protein kinase C (PKC) in chondrocytes derived from rodent costal cartilage and bovine articular cartilage has been determined and the role of PKC in GAG synthesis as well as the possible interactions of PKC with calcium- or cyclic AMP (cAMP)-dependent systems in the synthesis of GAG. \n\n10325235 (CellType: cardiomyocyte) Phorbol ester-sensitive PKC isoforms were detected at very low levels in caveolae fractions prepared from unstimulated cardiomyocytes; phorbol 12-myristate 13-acetate (PMA) (but not 4alpha-PMA, which does not activate PKC) recruited calcium-sensitive PKCalpha and novel PKCdelta and PKCepsilon to this compartment. \n\n9725212 (CellType: t cell) Since cyclosporin does not have any effect on cytosolic Ca 2+ levels and thus does not interfere with the interaction between PKC and Ca 2+ , we tested the effect of an inhibitor of intracellular Ca 2+ redistribution, TMB-8 ( 36 ), on TCR cross-linking-induced AICD. \n\n10751227 (Tissue: mesangia) DAG can directly activate classical types of PKC by interacting with its lipid-binding domain, and IP3 can indirectly activate PKC by increasing intracellular Ca2+, which interacts with the PKC Ca2+-binding domain. \n\n11342594 Synaptotagmins are transmembrane proteins with a short NH2-terminal ectodomain, a single transmembrane region, and two highly conserved, independently folding Ca2+-binding C2 domains (C2A and C2B) homologous to the C2 regulatory region of protein kinase C. \n\n7836388 At odds with the concept of calcium modulation of lipid binding, these authors considered phospholipids as modulators for the binding of calcium to PKC( 31 , 34 ) . \n\n9852158 The four inhibitors of PKC all accelerated the breakdown of the F-actin network observed after 5 min (Fig. 6 D ) and 30 min (Fig. 6 E ) in 0 Ca 2+ . \n\n9218480 These data reveal that the negative charge on the carboxyl terminus of protein kinase C contributes to the interaction of protein kinase C with Ca 2+ ." .

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        gpml:commentText  "12746452 Several upstream kinases have been implicated in the activation of the p38 MAPK and JNK 1/2 including apoptosis signaling kinase-1 which appears to activate both p38 MAPK and JNK 1/2, MKK 3/6 which activates p38 MAPK, and MKK 4/7 which activates JNK 1/2 ( 23 ). \n\n12649265 Infecting cardiomyocytes with adenoviruses that encode mutant, phosphorylation-resistant MKK6 or p38??2 MAPK inhibited interleukin-1????induced p38 MAPK activation, COX-2 gene expression, and PGE2 release. \n\n10942386 In contrast, neither dominant negative MKK6 nor SB203580, which specifically inhibit p38 MAP kinase activation, abrogated the MNNG-induced effect. \n\n12600999 ERK is activated by MEK1 and MEK2, whereas p38 kinase is activated by MKK3 and MKK6, and JNK is activated by MKK4 ( 24-28 ). \n\n12670941 Among them, MKK6 and MKK3 activate p38 MAPK. \n\n11245462 This pathway is stimulated by environmental and chemical stress as well as by exposure to cytokines, and it appears to play a role in the induction of apoptosis (10 , 11) . p38 MAPK is activated by hyperosmolarity and environmental stress and regulates pro- or anti-apoptotic effects in a stimulus and cell-type specific manner (12 , 13) . p38 MAPK is phosphorylated by either MKK3 (14) or MKK6 (15 , 16) . \n\n11732999 (CellType: chondrocyte) On the other hand, p38 MAPK is known to be a stress signal transducer, and phosphorylation of p38 MAPK in chondrocytes by EGF [ 25 ], PTH [ 41 ], and GDF-5 [ 42 ] regulates differentiation of chondrocytes. p38 MAPK is phosphorylated by MKK3, and MKK6 [ 45 ], and Atf-2 is one of the transcription factors downstream of p38 MAPK [ 31 ]. \n\n10716930 Thus, MKK3 requires a docking domain for efficient dual phosphorylation of p38alpha, but MKK6 is able to phosphorylate p38alpha on both threonine and tyrosine in the absence of a docking domain. \n\n11500363 (CellLineName: HeLa) MKK4 and MKK6 are both known to phosphorylate stress-activated protein kinase 2a (SAPK2a, also called p38)." .

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        gpml:commentText  "--------------------------------------------------------------------------------\nMedLine Reference  12690113:1232  \nSentence  MSK1 is known to be regulated by MAPK/ERK and SAPK2a/p38 and is currently the best candidate for the mediation of cytokine-induced CREB phosphorylation at Ser133 ( 37 ? 39 , 47 ).  \nJournal  J. Biol. Chem  \nJournal Reference  v278 i26 p23243 (2003)  \nJournal Link  http://www.jbc.org/cgi/content/full/278/26/23243  \nTissue  epithelia  \nOrgan  lung  \nSource  Ariadne Pathways  \n--------------------------------------------------------------------------------\nMedLine Reference  9873047:7  \nSentence  Although purified recombinant RLPK can be phosphorylated by ERK2 and p38alpha in vitro, its activity is not affected by this phosphorylation.  \nCellLineName  HeLa  \nSource  Ariadne Pathways  \n--------------------------------------------------------------------------------\nMedLine Reference  12896977:1308  \nSentence  Although the p38 MAPK can activate mitogen and stress-activated protein kinase-1 (MSK1), a major histone H3 kinase ( 67 ), SB203580 shows no effect on histone H3 acetylation at the IL-2 promoter ( Fig. 9 D ).  \nJournal  J. Biol. Chem  \nJournal Reference  v278 i42 p41034 (2003)  \nJournal Link  http://www.jbc.org/cgi/content/full/278/42/41034  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11701463:1153  \nSentence  Suppression of ERK and p38 MAPK is required to suppress the activation of MSK1.  \nJournal  ATVB  \nJournal Reference  v21 i11 p1764 (2001)  \nJournal Link  http://atvb.ahajournals.org/cgi/content/full/21/11/1764  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  12628924:1039  \nSentence  The nuclear kinase MSK1 is activated by both ERK and p38 MAPK.  \nJournal  EMBO  \nJournal Reference  v22 i6 p1313 (2003)  \nJournal Link  http://embojournal.npgjournals.com/cgi/content/full/22/6/1313  \nSource  Ariadne Pathways" .

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        gpml:commentText  "8626650 Here we report that mutations within the switch 2 domain of Ras (residues 62-69) inhibit activation of Ras by the mammalian GEFs, Sos1, and GRF/CDC25Mm. \n\n1447167 As a consequence, the CDC25Mm induces a rapid formation of the biologically active Ras.GTP complex. \n\n(Tissue: blood, CellType: b cell) Phosphorylation of RasGRP3 by PKC may be critical to modulate its association with Ras at the plasma membrane and the subsequent activation of the ERK MAPK cascade. \n\n14749369 Furthermore, we have recently demonstrated that the ability of RasGRF1 to activate Ras is regulated by the Rho family GTPase Cdc42, by a mechanism that entails the translocation of RasGRF1 to the cell particulate fraction ( 3 , 4 ). \n\n14676298 (CellType: b cell) This defective Ras activation is suppressed by the expression of RasGRP3 as a membrane-attached form, suggesting that phospholipase C-gamma2 regulates RasGRP3 localization and thereby Ras activation. \n\n11500497 Our results suggest that mUBPy may play a role in controlling degradation of CDC25 Mm , thus regulating the level of this Ras-guanine nucleotide exchange factor. \n\n15572660 (Tissue: endothelial) However, RasGRP2 is a Rap1 activator and not a Ras activator, whereas RasGRP3 is an activator of Ras and Rap1. \n\n15213298 RasGRP3 activates both Ras and Rap1 (Yamashita et al., 2000 ), and RasGRP4 activates Ras (Reuther et al., 2002 ; Yang et al., 2002 ). \n\n8717044 (CellLineName: COS-7) These results demonstrate a G-protein-coupled mechanism for Ras activation, mediated by p140 Ras-GRF. \n\n8700529 (CellLineName: CHO) Transient expression of CDC25Mm in CHO cells activates Ras." .

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        gpml:commentText  "PromoterBinding ELK1 --+> FOS" .

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        gpml:commentText  "DirectRegulation HTR2A --+> GNAQ" .

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        gpml:commentText  "Binding GNAI2 ---- HTR1E" .

<https://identifiers.org/pubmed/15156153>
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        gpml:commentText  "MedLine Reference  12414794:1133  \nSentence  MSK1 has been shown to phosphorylate CREB and to be activated by EGF , as well as ERK1/2 and p38 MAPKs ( 27 ).  \nJournal  J. Biol. Chem  \nJournal Reference  v277 i52 p50550 (2002)  \nJournal Link  http://www.jbc.org/cgi/content/full/277/52/50550  \nCellLineName  HeLa  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  12896977:1312  \nSentence  It is interesting to note that H89 is also a potent inhibitor of protein kinase A (PKA) and that both MSK1 and PKA can phosphorylate CREB.  \nJournal  J. Biol. Chem  \nJournal Reference  v278 i42 p41034 (2003)  \nJournal Link  http://www.jbc.org/cgi/content/full/278/42/41034  \nCellType  lymphocyte  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  9687510:1176  \nSentence  MSK1 phosphorylates CREB at Ser133. ( A ) Comparison of the substrate specificities of MSK1, MAPKAP-K1a and MAPKAP-K1b towards the indicated peptides and CREB.  \nJournal  EMBO  \nJournal Reference  v17 i15 p4426 (1998)  \nJournal Link  http://embojournal.npgjournals.com/cgi/content/full/17/15/4426  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11907026:1243  \nSentence  MSK-1 phosphorylates CREB in response to FGF or NGF in PC12 cells.  \nJournal  J. Biol. Chem  \nJournal Reference  v277 i21 p18710 (2002)  \nJournal Link  http://www.jbc.org/cgi/content/full/277/21/18710  \nCellLineName  PC 12  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11701463:1152  \nSentence  Activated MSK1 phosphorylates CREB at Ser133.  \nJournal  ATVB  \nJournal Reference  v21 i11 p1764 (2001)  \nJournal Link  http://atvb.ahajournals.org/cgi/content/full/21/11/1764  \nSource  Ariadne Pathways" .

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        gpml:commentText  "MedLine Reference  11238126:1108  \nSentence  MEK-1/2 activation correlated with ERK-1/2 activation in 7 of 14 AML cell lines and 2 of 5 CML cell lines.  \nJournal  Blood  \nJournal Reference  v97 i6 p1823 (2001)  \nJournal Link  http://www.bloodjournal.org/cgi/content/full/97/6/1823  \nCellLineName  AML  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  10650934:1110  \nSentence  Cells were pretreated for 30 min with 10 ÃÂ¯ÃÂ¿ÃÂ½ M PD98059, an inhibitor of MEK1 and -2, the MAPK kinases that are responsible for activation of ERK1 and -2.  \nJournal  Endocrinology  \nJournal Reference  v141 i2 p544 (2000)  \nJournal Link  http://endo.endojournals.org/cgi/content/full/141/2/544  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11108712:1201  \nSentence  Finally, because MEK1 and MEK2 activate ERK , we assayed for ERK activity in the presence of the MEK inhibitor PD 98059 (Fig. 6 D ).  \nJournal  J. Biol. Chem  \nJournal Reference  v276 i10 p7586 (2001)  \nJournal Link  http://www.jbc.org/cgi/content/full/276/10/7586  \nCellType  osteoblast  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  10747974:1181  \nSentence  PD 98059 and U0126 specifically inhibit MEK1 and MEK2, the kinases that phosphorylate ERK, but have no effect on other kinases including SAPK/JNK ( 56 , 57 ).  \nJournal  J. Biol. Chem  \nJournal Reference  v275 i21 p16064 (2000)  \nJournal Link  http://www.jbc.org/cgi/content/full/275/21/16064  \nTissue  epithelia  \nOrgan  gastric  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  12225966:1161  \nSentence  We have recently reported that inhibition of muscle MAPKK1/2 (MEK1/2) abolishes isoproterenol-stimulated NKCC activity and ERK1/2 phosphorylation ( 31 ).  \nJournal  Cell Phys  \nJournal Reference  v283 i4 pC1025 (2002)  \nJournal Link  http://ajpcell.physiology.org/cgi/content/full/283/4/C1025  \nTissue  muscle  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  12393899:1082  \nSentence  To inhibit the ERK1/2 pathway, we applied PD98059, an inhibitor of MKK1 and MKK2 ( 30 ), which are upstream kinases that phosphorylate and activate ERK1/2.  \nJournal  J. Biol. Chem  \nJournal Reference  v277 i51 p49577 (2002)  \nJournal Link  http://www.jbc.org/cgi/content/full/277/51/49577  \nTissue  cortex  \nCellType  neural  \nSource  Ariadne Pathways  \n\nMedLine Reference  12839832:1143  \nSentence  U-0126 is a selective inhibitor of the MAPK kinase MEK1/2, which directly activates ERK1/2 ( 13 , 50 ).  \nJournal  Cell Phys  \nJournal Reference  v285 i5 pC1122 (2003)  \nJournal Link  http://ajpcell.physiology.org/cgi/content/full/285/5/C1122  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  10891480:1248  \nSentence  In contrast to its effect on HA-MEK1, the kinase-inactive mutant PKCetaKR did not block MEK2E-induced HA-ERK2 activation (Fig. 5 C).  \nJournal  Mol. Cell. Biol  \nJournal Reference  v20 i15 p5392 (2000)  \nJournal Link  http://mcb.asm.org/cgi/content/full/20/15/5392  \nSource  Ariadne Pathways  \n--------------------------------------------------------------------------------\nMedLine Reference  12623839:1052  \nSentence  Mkk1 and Mkk2 phosphorylate Erk kinases in the Thr-Glu-Tyr motif; Mkk3, Mkk4, and Mkk6 phosphorylate p38 kinases in the Thr-Gly-Tyr motif, while Mkk4 and Mkk7 regulate dual phosphorylation of JNK kinases in the Thr-Pro-Tyr motif ( Table 2 ).  \nJournal  Blood  \nJournal Reference  v101 i12 p4667 (2003)  \nJournal Link  http://www.bloodjournal.org/cgi/content/full/101/12/4667  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11038347:1040  \nSentence  The specificity of MEK1/2 inhibition was achieved by using two different MEK inhibitors, and by the additional use of transdominant-negative mutants, which inhibit MEK/ERK activation.  \nJournal  J. Biol. Chem  \nJournal Reference  v275 i50 p38953 (2000)  \nJournal Link  http://www.jbc.org/cgi/content/full/275/50/38953  \nSource  Ariadne Pathways" .

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<http://rdf.wikipathways.org/Pathway/WP722_r141562/GraphicalLine/e1d09>
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<https://identifiers.org/pubmed/10777559>
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<http://rdf.wikipathways.org/Pathway/WP722_r141562/Interaction/f505f/Point/88cf3bbafe1c06a7e51e7d8be6f42a66>
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<http://rdf.wikipathways.org/Pathway/WP722_r141562/Interaction/e614c>
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<https://identifiers.org/pubmed/11278353>
        rdf:type          gpml:PublicationXref ;
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<http://rdf.wikipathways.org/Pathway/WP722_r141562/Interaction/cf0c1>
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<http://rdf.wikipathways.org/Pathway/WP722_r141562/Interaction/d536c/Point/69af5a964a34b796364d4121fc80151e>
        rdf:type          gpml:Point ;
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<http://rdf.wikipathways.org/Pathway/WP722_r141562/DataNode/e6339>
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<https://identifiers.org/pubmed/14532295>
        rdf:type          gpml:PublicationXref ;
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<https://identifiers.org/pubmed/11257115>
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<https://identifiers.org/pubmed/10022874>
        rdf:type          gpml:PublicationXref ;
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<http://rdf.wikipathways.org/Pathway/WP722_r141562/Interaction/e0483/Point/9a11a5f75c0e95f15e73713b5b5ade72>
        rdf:type          gpml:Point ;
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<http://rdf.wikipathways.org/Pathway/WP722_r141562/Interaction/fe402/Anchor/f6099>
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<https://identifiers.org/pubmed/12225966>
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<http://rdf.wikipathways.org/Pathway/WP722_r141562/Interaction/d0c5c>
        rdf:type                 gpml:Interaction ;
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<https://identifiers.org/pubmed/11496823>
        rdf:type          gpml:PublicationXref ;
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<http://rdf.wikipathways.org/Pathway/WP722_r141562/Interaction/aad56/Point/8f366908d858f6ea146c643ebfcf4f3>
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<http://rdf.wikipathways.org/Pathway/WP722_r141562/Comment/ba5a7b0a044b3d1ed04373a2227188bb>
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        gpml:commentText  "ProtModification MAP3K1 --+> MAP2K1" .

<https://identifiers.org/pubmed/11032810>
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<http://rdf.wikipathways.org/Pathway/WP722_r141562/Interaction/d70a1/Point/b620cf0922c5c7c252dc318322069c03>
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<https://identifiers.org/pubmed/8808177>
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<https://identifiers.org/pubmed/8846784>
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<http://rdf.wikipathways.org/Pathway/WP722_r141562/Interaction/bfe25>
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<https://identifiers.org/pubmed/9379049>
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<https://identifiers.org/pubmed/9130707>
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<http://rdf.wikipathways.org/Pathway/WP722_r141562/Comment/c9b01c7e2a0065f4436c3f0ece8db9c3>
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<https://identifiers.org/pubmed/11916537>
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<http://rdf.wikipathways.org/Pathway/WP722_r141562/Comment/56e613175f3b684c61a4d36edcb96583>
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        gpml:commentText  "ProtModification MAPK3 --+> ELK1" .

<https://identifiers.org/pubmed/10034>
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<https://identifiers.org/pubmed/11701463>
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        gpml:database     "Pubmed" ;
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<https://identifiers.org/pubmed/11315998>
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<https://identifiers.org/pubmed/12649265>
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<https://identifiers.org/pubmed/14963045>
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<https://identifiers.org/pubmed/15064721>
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<http://rdf.wikipathways.org/Pathway/WP722_r141562/Interaction/feee8>
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<http://rdf.wikipathways.org/Pathway/WP722_r141562/Interaction/d8d3a/Point/a1b9962d2ab7d3115240a41a93e44eee>
        rdf:type          gpml:Point ;
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<http://rdf.wikipathways.org/Pathway/WP722_r141562/Comment/ef53912e6146606b184600528519f28b>
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<http://rdf.wikipathways.org/Pathway/WP722_r141562/Label/b33a4>
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        gpml:textlabel       "Small molecule" ;
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<https://identifiers.org/pubmed/11395491>
        rdf:type          gpml:PublicationXref ;
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        gpml:commentText  "10777559 Both Ras-GRF and Ras-GRP/CalDAG-GEFII activate Ras and R-Ras; therefore, these GEFs appear to have two pathways for activation of JNK . \n\n12782630 Sos and RasGRP proteins are involved in linking the activation of membrane or cytoplasmic tyrosine kinases with the stimulation of Ras GTPases ( 8 ). \n\n10807788 (CellType: t cell) Here we show that RasGRP, a Ras activator that contains calcium-binding EF hands and a DAG-binding domain, is expressed in T cells. \n\n15604236 (CellType: keratinocyte) TPA may activate PLCe through Ras activation, which is mediated by RasGRP1, a TPA-regulated Ras-specific guanine nucleotide exchange factor (GEF) expressed in keratinocytes (13) . \n\n12070163 (CellType: t cell) Activated RasGRP ( 34 , 35 ) and PKCeta ( 36 , 37 ) in turn stimulate the Ras-ERK-AP-1 and NFkappaB pathways, respectively. \n\n14532295 (CellType: keratinocyte) This result suggests that, although RasGRP1 can directly activate Ras in response to phorbol esters, PKC is still required for the downstream stimulation of the Raf/MEK/ERK pathway. \n\n17190838 (CellType: MAST) These data indicated that N-Ras is the Ras member that is activated by RasGRP1 in mast cells. \n\n11395491 (CellLineName: JURKAT) Recent studies have demonstrated that overexpression of another exchange factor for Ras, RasGRP, can enhance TCR-Ras-Erk signaling and increase interleukin-2 production in Jurkat cells ( 18 ). \n\n14970203 (CellLineName: WEHI 231) This could be due to synergy between RasGRP1-mediated Ras activation and parallel BCR-initiated signaling pathways not involving Ras activation. \n\n11120810 (CellType: t cell, CellLineName: JURKAT) RasGRP can mediate Ras activation in response to TCR cross-linking in Jurkat T cells and RasGRP overexpression enhances TCR-mediated activation of ERK ( 23 )." .

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        gpml:commentText  "MedLine Reference  10024371:1025  \nSentence  Induction of the SRE occurs upon formation of a ternary complex with serum response factor, p62 TCF , and the SRE. 118 ERK1/2 was shown to phosphorylate p62 TCF (also known as elk-1 or SAP-1), resulting in enhanced ternary complex formation. 119 Thus, the SRE present in the c- fos promoter may be regulated by angiotensin II??????stimulated ERK1/2 phosphorylation of p62 TCF , as shown for EGF. 119 Activation of ERK1/2 requires activation of Ras and Raf, events that are regulated by tyrosine phosphorylation.  \nJournal  J. Neurosci  \nJournal Reference  v19 i5 p1876 (1999)  \nJournal Link  http://www.blackwell-synergy.com/links/doi/10.1046/j.1471-4159.2002.01075.x/full/  \nTissue  fat  \nOrgan  liver  \nCellType  eosinophil  \nCellLineName  CWSV1  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11751459:1010  \nSentence  On bryo 1 treatment, the activity of ERK2 (p42) rapidly increased, with ERK1 (p44) protein levels remaining constant. p44/42 immunoprecipitates from lysates of bryo 1-treated cells had increased their ability to phosphorylate the transcription factor Elk-1.  \nJournal  Cell Growth and Diff  \nJournal Reference  v12 i12 p641 (2001)  \nJournal Link  http://cgd.aacrjournals.org/cgi/content/full/12/12/641  \nTissue  lymph  \nCellLineName  reh  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11782488:1286  \nSentence  It was also reported that BMK1 activation is required for neurotrophin stimulation of MEF2C in both cortical neurons and PC12 cells, distinct from ERK1/2-induced activation of Elk1 and CREB transcription factors ( 30 ).  \nJournal  J. Biol. Chem  \nJournal Reference  v277 i11 p9614 (2002)  \nJournal Link  http://www.jbc.org/cgi/content/full/277/11/9614  \nTissue  cortex  \nCellType  neural  \nCellLineName  PC 12  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11297525:1051  \nSentence  In addition, the activation of ERK1/2 correlated with increased activation of the downstream transcription factor Elk-1.  \nJournal  J. Biol. Chem  \nJournal Reference  v276 i18 p15537 (2001)  \nJournal Link  http://www.jbc.org/cgi/content/full/276/18/15537  \nTissue  marrow  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  12032150:1015  \nSentence  In the nucleus, activated ERK1/2 continuously phosphorylate Elk-1, leading to the prolonged expression of c- fos , which results in the expression of several genes such as matrix metalloproteinase (mmp)-9 ; MMP-9 activity is required for the induction of the cell motility response.  \nJournal  J. Biol. Chem  \nJournal Reference  v277 i31 p28256 (2002)  \nJournal Link  http://www.jbc.org/cgi/content/full/277/31/28256  \nOrgan  kidney  \nCellLineName  Madin Darby  \nSource  Ariadne Pathways  \n--------------------------------------------------------------------------------\nMedLine Reference  9020136:1065  \nSentence  Likewise GST-Sap, the GST fusion protein containing the C-terminal activation domain of Elk-1 was more readily phosphorylated by ERK-1 than by JNK-1 in vitro (Fig. 1 A , lower right panel ), although this difference was not as pronounced as with GST-Sap. -- Fig. 1.  \nJournal  J. Biol. Chem  \nJournal Reference  v272 i7 p4219 (1997)  \nJournal Link  http://www.jbc.org/cgi/content/full/272/7/4219  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11408617:1037  \nSentence  Once activated, ERK1/2 can phosphorylate a ternary complex factor, Elk-1, that further interacts with serum response factor and induces the transcription of c-fos through serum-responsive element (Karin, 1995 ).  \nJournal  Mol. Pharm  \nJournal Reference  v60 i1 p217 (2001)  \nJournal Link  http://molpharm.aspetjournals.org/cgi/content/full/60/1/217  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  12239223:1248  \nSentence  ERK1/2 then activates transcription factor ELK-1, whereas JNK and p38 MAPK activate ATF2 .  \nJournal  J. Biol. Chem  \nJournal Reference  v277 i50 p48755 (2002)  \nJournal Link  http://www.jbc.org/cgi/content/full/277/50/48755  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11463794:1190  \nSentence  A, phosphorylation of Elk1 by HA-ERK1 and HA-ERK1b.  \nJournal  J. Biol. Chem  \nJournal Reference  v276 i38 p35280 (2001)  \nJournal Link  http://www.jbc.org/cgi/content/full/276/38/35280  \nCellLineName  COS-7  \nSource  Ariadne Pathways  \n--------------------------------------------------------------------------------\nMedLine Reference  12498787:4  \nSentence  Since Erk1 and Erk2 regulate transcription from the Fos serum response element (SRE) by phosphorylating the ternary complex factors Elk-1 and SAP-1 ( Treisman, 1995 ), we examined the effect of integrin ligation on the Fos SRE.  \nJournal  Renal Phys  \nJournal Reference  v276 i29 p26814 (2001)  \nJournal Link  http://www.jbc.org/cgi/content/full/276/29/26814  \nSource  Ariadne Pathways" .

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        gpml:commentText  "MedLine Reference  11983682:1198  \nSentence  Hippocampal neurons were treated with UO126, an inhibitor of MEK1 and MEK2, which can activate ERK1 and ERK2.  \nJournal  J. Biol. Chem  \nJournal Reference  v277 i27 p24676 (2002)  \nJournal Link  http://www.jbc.org/cgi/content/full/277/27/24676  \nOrgan  hippocampal  \nCellType  neural  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  9927426:1014  \nSentence  Both p42 and p44MAPK are activated by dual phosphorylation on a threonine and a tyrosine residue, achieved by the dual-specificity kinase MKK1/2.  \nJournal  EMBO  \nJournal Reference  v18 i3 p664 (1999)  \nJournal Link  http://embojournal.npgjournals.com/cgi/content/full/18/3/664  \nCellType  fibroblast  \nCellLineName  PC 12  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11238126:1108  \nSentence  MEK-1/2 activation correlated with ERK-1/2 activation in 7 of 14 AML cell lines and 2 of 5 CML cell lines.  \nJournal  Blood  \nJournal Reference  v97 i6 p1823 (2001)  \nJournal Link  http://www.bloodjournal.org/cgi/content/full/97/6/1823  \nCellLineName  AML  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  10650934:1110  \nSentence  Cells were pretreated for 30 min with 10 ÃÂ¯ÃÂ¿ÃÂ½ M PD98059, an inhibitor of MEK1 and -2, the MAPK kinases that are responsible for activation of ERK1 and -2.  \nJournal  Endocrinology  \nJournal Reference  v141 i2 p544 (2000)  \nJournal Link  http://endo.endojournals.org/cgi/content/full/141/2/544  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  12584202:1152  \nSentence  Because MEK1/2 phosphorylates and activates p42/p44MAPK, the inhibitor would be expected to inhibit the phosphorylation of p42/p44MAPK and their downstream targets.  \nJournal  J. Biol. Chem  \nJournal Reference  v278 i17 p14753 (2003)  \nJournal Link  http://www.jbc.org/cgi/content/full/278/17/14753  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  12832465:1147  \nSentence  All together, these results indicated that MEK2 is not essential for cell proliferation and ERK1/ERK2 activation in response to mitogens.  \nJournal  Mol. Cell. Biol  \nJournal Reference  v23 i14 p4778 (2003)  \nJournal Link  http://mcb.asm.org/cgi/content/full/23/14/4778  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11080204:1217  \nSentence  Activated Raf phosphorylates the MAP kinase kinases MEK1 and MEK2, which subsequently activate ERK1 and ERK2.  \nJournal  J. Neurochem  \nJournal Reference  v75 i6 p2511 (2000)  \nJournal Link  http://www.blackwell-synergy.com/servlet/useragent?func=showIssues&code=jnc  \nCellType  fibroblast  \nCellLineName  PC12-E2  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  12242299:1278  \nSentence  Neither LY-294002 nor wortmannin significantly affected the phosphorylation of ERK1/2 or MKK1/2 (Fig. 9A ), indicating that ERK activation is not controlled by PI3K signaling.  \nJournal  Mol. Cell. Biol  \nJournal Reference  v22 i20 p7226 (2002)  \nJournal Link  http://mcb.asm.org/cgi/content/full/22/20/7226  \nCellLineName  HeLa  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  12730329:1047  \nSentence  Two upstream dual specificity enzyme kinases MEK1/MEK2 (MAPKKs) phosphorylate threonine and tyrosine residues of ERK1/2 and initiate an ultrasensitive downstream phosphorylation cascade ( 25 ).  \nJournal  Mol. Endocrin  \nJournal Reference  v17 i8 p1593 (2003)  \nJournal Link  http://mend.endojournals.org/cgi/content/full/17/8/1593  \nSource  Ariadne Pathways  \n--------------------------------------------------------------------------------\nMedLine Reference  12496361:1025  \nSentence  Activated Ras associates with Raf that phosphorylates and activates the mitogen-activated protein (MAP) kinase kinases MEK1 and MEK2, which in turn phosphorylate the MAP kinases ERK1 and ERK2.  \nJournal  Mol. Cancer Res  \nJournal Reference  v1 i2 p147 (2002)  \nJournal Link  http://mcr.aacrjournals.org/cgi/content/full/1/2/147  \nTissue  nerve  \nCellType  neural  \nSource  Ariadne Pathways" .

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        gpml:commentText  "9439849 (Organ: hypothalamic, Tissue: cortex) These results suggest that fluoxetine gradually increases the G-protein coupling of 5-HT2A/2C receptors without altering the levels of Gq- or G11-proteins. \n\n12721328 (Organ: hypothalamic, Tissue: cortex, CellType: neural) These fluoxetine-induced changes in 5-HT2A receptor signaling occur without changing the levels of Galphaq or RGS4 proteins." .

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        gpml:commentText  "11880369 Diacylglycerol has been shown to regulate RasGRP subcellular location and catalytic activity ( 8 , 15-17 ). \n\n15879121 Y775 and Y783 are therefore identified as the primary regulatory tyrosines for both the IP 3 -mediated Ca 2+ flux and the DAG-mediated activation of the PKC/RasGRP pathway. \n\n17492052 (CellType: platelet) We have recently identified Ca 2+ and diacylglycerol-regulated guanine nucleotide exchange factor I (CalDAG-GEFI; also referred to as RasGRP2) as crucial for ÃÂ¯ÃÂ¿ÃÂ½ÃÂ¯ÃÂ¿ÃÂ½ÃÂ©ÃÂ¯ÃÂ¿ÃÂ½ÃÂ¯ÃÂ¿ÃÂ½ÃÂ©ÃÂ©ÃÂ¯ÃÂ¿ÃÂ½ÃÂ¯ÃÂ¿ÃÂ½ÃÂ©ÃÂ¯ÃÂ¿ÃÂ½ÃÂ¯ÃÂ¿ÃÂ½ÃÂ©ÃÂ©ÃÂ© 3 integrin activation in platelets ( 15 ). \n\n11395491 (CellType: t cell) IP 3 binds receptors that regulate the release of stored Ca 2+ , whereas DAG is required to activate proteins such as protein kinase C and Ras guanyl nucleotide releasing protein (RasGRP) ( 17-19 ). \n\n15795236 (CellType: t cell) An increase in inositol ( 1 , 4 , 5 ) tris phosphate levels results in release of calcium from intracellular stores, whereas increased diacylglycerol results in stimulation of PKC and RasGRP (for review see reference 30 ). \n\n11292831 (CellLineName: PC12D) Together, these data define a novel signaling pathway for M 1 mAChR , where increases in Ca 2+ and diacylglycerol stimulate the sequential activation of CalDAG-GEFI , Rap1, and B-Raf, resulting in the activation of MEK and ERK1/2. \n\n14532295 (CellType: b cell, CellLineName: ramos) Conversely, diacylglycerol both activates RasGRP1 and causes the activation and translocation of diacylglycerol kinase, which abrogates the activation of the GRP protein ( 43 , 44 ). \n\n14557275 (CellLineName: MOCK) In this regard, it has been reported that DAG kinase zeta phosphorylates specifically localized DAG molecules, thereby controlling the activation of the DAG-activated signaling protein RasGRP and H-Ras ( 20 ). \n\n11257115 (CellLineName: Rat2) It is important then that cells regulate the DAG that activates RasGRP. \n\n11352924 (Organ: brain) DAG produced in response to these external stimuli activates PKC and the guanine nucleotide exchange factors vav and RasGRP ( 39 , 40 )." .

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        gpml:commentText  "15064721 Our study further showed that the E1/4 cell-specific B-Raf activity was stimulated by PLC gamma and subsequent Rap1 activation. \n\n10854065 (CellType: spermatid) Moreover, in mouse spermatids, i.e., the haploid cytodifferentiating cells, a so far unidentified protein complex formed by endogenous Rap1/B-Raf/14-3-3 theta can be coimmunoprecipitated. \n\n11950876 Rap1, a Ras-related G protein, has been reported to activate B-Raf but to inhibit Raf-1 (Vossler et al., 1997 ). \n\n12855697 (Tissue: lymph, CellType: t cell) Recent studies indicate that Rap1 activates B-Raf by recruiting B-Raf to the membrane. \n\n15572664 By recruiting a different set of adapter proteins, TrkA causes an activation of Rap-1 that stimulates B-Raf. \n\n12446733 In contrast to Raf-1, B-Raf is activated by Rap1. \n\n12351703 Activation of G o releases Rap1-GTPase activating protein to inhibit Rap1- induced B-Raf activation ( 65 ), providing an appealing mechanism for G o-mediated D2S action. \n\n14963045 (Organ: gastric, Tissue: epithelia) Rap1 activates B-Raf and subsequently induces sustained Erk activation by a growth factor. \n\n9094716 (CellType: neural, CellLineName: PC 12) Rap1, activated by mutation or by the cAMP-dependent protein kinase PKA, is a selective activator of B-Raf and an inhibitor of Raf-1. \n\n10976102 (CellType: fibroblast, CellLineName: Swiss 3T3) Rap1 then activates B-Raf and thereby MEK and ERK ( 38 , 53-55 )." .

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        gpml:commentText  "MedLine Reference  12896977:1200  \nSentence  Multiple p38 MAPK-dependent kinases such as MAPKAP kinase 2/3 have been shown to increase CREB phosphorylation in various cell types, including T-lymphocytes ( 36 , 49 A?A?A? 51 ).  \nJournal  Mol. Endocrin  \nJournal Reference  v278 i42 p41034 (2003)  \nJournal Link  http://www.jbc.org/cgi/content/full/278/42/41034  \nTissue  egg  \nOrgan  heart  \nCellType  t cell  \nCellLineName  PC 12  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  10488088:1234  \nSentence  We now demonstrate that IGF-I induces promoter activity of the bcl-2 gene through activation of CREB via a novel signaling pathway mediated by MAPK kinase 6/p38eta MAPK/MAPKAP-K3 (Fig. 8 ).  \nJournal  J. Biol. Chem  \nJournal Reference  v274 i39 p27529 (1999)  \nJournal Link  http://www.jbc.org/cgi/content/full/274/39/27529  \nTissue  cortex  \nCellType  neural  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11328854:1137  \nSentence  Additionally, these immune complex kinase assays confirmed previous reports indicating that MAPKAPK-3 can directly phosphorylate CREB in vitro ( 12 , 26 ).  \nJournal  Mol. Endocrin  \nJournal Reference  v15 i5 p716 (2001)  \nJournal Link  http://mend.endojournals.org/cgi/content/full/15/5/716  \nTissue  egg  \nSource  Ariadne Pathways  \n--------------------------------------------------------------------------------\nMedLine Reference  10781029:1082  \nSentence  Indeed, MK2 was shown to phosphorylate the nuclear transcription factors CREB as well as SRF ( 5 , 6 ) and to modulate their transcriptional activity. 3pK is also able to phosphorylate CREB in vitro and to interact with several nuclear proteins in vivo . 2 We used a human heart cDNA library and a kinase inactive version of 3pK as a bait, because wild-type 3pK autonomously led to the transactivation of the reporter genes.  \nJournal  J. Biol. Chem  \nJournal Reference  v275 i27 p20239 (2000)  \nJournal Link  http://www.jbc.org/cgi/content/full/275/27/20239  \nOrgan  heart  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  0:10240051  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  10706690:1224  \nSentence  MAPKAP-K2, MAPKAP-K3, and PKA also phosphorylate CREB and ATF1 at Ser 133 and Ser 63 , respectively ( 2 ).  \nJournal  J. Immunol  \nJournal Reference  v164 i6 p3018 (2000)  \nJournal Link  http://www.jimmunol.org/cgi/content/full/164/6/3018  \nCellType  macrophage  \nSource  Ariadne Pathways" .

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        gpml:commentText  "MedLine Reference  10666409:1192  \nSentence  These data indicate that activation of MAPKAPK2, which is immediately downstream of p38 MAPK, is highly correlated with PCÃ¢ÂÂs protection.  \nJournal  Circulation Res  \nJournal Reference  v272 i6 p3296 (1997)  \nJournal Link  http://circres.ahajournals.org/cgi/content/full/86/2/144  \nOrgan  immunologic  \nCellType  myocyte  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  9679149:1317  \nSentence  Therefore, the data are consistent with phosphorylation of MAPKAPK2 by p38-MAPK being essential for activation.  \nJournal  J. Cell Biol  \nJournal Reference  v142 i2 p523 (1998)  \nJournal Link  http://www.jcb.org/cgi/content/full/142/2/523  \nOrgan  heart  \nCellType  myocyte  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  10993748:1166  \nSentence  Thus, unlike other MAP kinases, p38 MAP kinase activates the MAPKAP kinase 2 ( 21 ).  \nJournal  Heart Circul  \nJournal Reference  v279 i3 pH901 (2000)  \nJournal Link  http://ajpheart.physiology.org/cgi/content/full/279/3/H901  \nOrgan  heart  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  9727040:11  \nSentence  These findings demonstrate that the activation of p38 MAP kinase is involved not only in response to stress, but also in physiological signaling by gastrointestinal hormones such as CCK, where activation of Gq-coupled receptors stimulates a cascade in which p38 MAP kinase activates MAP kinase-activated protein kinase-2, resulting in Hsp 27 phosphorylation.  \nJournal  J. Cell Biol  \nJournal Reference  v142 i2 p523 (1998)  \nJournal Link  http://www.jcb.org/cgi/content/full/142/2/523  \nOrgan  gastric  \nCellType  myocyte  \nSource  Ariadne Pathways  \n--------------------------------------------------------------------------------\nMedLine Reference  14499342:1  \nSentence  MAPK-activated protein kinase-2 (MK2) is activated by p38 MAPK in human neutrophils.  \nCellType  neutrophil  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  10704466:1014  \nSentence  Therefore, these studies demonstrate that p38alpha is a major upstream activator of MAPKAP kinase 2 and a key component of the IL-1 signaling pathway.  \nJournal  J. Exp. Med  \nJournal Reference  v274 i25 p17491 (1999)  \nJournal Link  http://www.jem.org/cgi/content/full/191/5/859  \nCellType  macrophage  \nCellLineName  ES  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  9759836:1135  \nSentence  Both MAPKAPK-2 and its recently identified homologue, MAPKAPK-3, are phosphorylated and activated by p38 MAPK in vivo ( 43 , 59 ).  \nJournal  J. Immunol  \nJournal Reference  v161 i7 p3225 (1998)  \nJournal Link  http://www.jimmunol.org/cgi/content/full/161/7/3225  \nCellType  b cell  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  10066767:1186  \nSentence  Although p38-alpha phosphorylated MAPKAP kinase-2 significantly but not GST-c-Jun (Fig. 6 A ), p38-delta phosphorylated GST-c-Jun but not MAPKAP kinase-2 (Fig. 6 B ).  \nJournal  J. Biol. Chem  \nJournal Reference  v274 i11 p7095 (1999)  \nJournal Link  http://www.jbc.org/cgi/content/full/274/11/7095  \nCellLineName  293T  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11490018:1219  \nSentence  MAPKAPK2, which was originally designated HSP25/27 kinase, is phosphorylated and activated by p38 MAPK ( 8 , 9 , 10 ).  \nJournal  J. Immunol  \nJournal Reference  v167 i4 p2298 (2001)  \nJournal Link  http://www.jimmunol.org/cgi/content/full/167/4/2298  \nCellType  MAST  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11859076:1323  \nSentence  SRF can be phosphorylated by pp90 rsk , a known effector of ERKs, CaM kinases II and IV, and the MAPKAP-2 (MK2), which is regulated by p38 MAPK ( 10 ).  \nJournal  J. Biol. Chem  \nJournal Reference  v277 i18 p15376 (2002)  \nJournal Link  http://www.jbc.org/cgi/content/full/277/18/15376  \nCellType  t cell  \nSource  Ariadne Pathways" .

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        gpml:commentText  "--------------------------------------------------------------------------------\nMedLine Reference  10428835:1222  \nSentence  PD98059 is a specific inhibitor for MKK1 and -2 ( 56 ), upstream kinases that phosphorylate and activate ERK ( 15 , 57 ).  \nJournal  J. Biol. Chem  \nJournal Reference  v274 i32 p22569 (1999)  \nJournal Link  http://www.jbc.org/cgi/content/full/274/32/22569  \nTissue  cortex  \nCellType  neural  \nCellLineName  DIV  \nSource  Ariadne Pathways  \n--------------------------------------------------------------------------------\nMedLine Reference  12529254:1190  \nSentence  The present study provides direct evidence that the P2X7-R can mediate ERK1/2 activation through a cellular pathway that is dependent on intracellular and extracellular Ca2+, Pyk2, c-Src, PI 3-K, and MEK1/2.  \nJournal  Cell Phys  \nJournal Reference  v284 i2 pC571 (2003)  \nJournal Link  http://ajpcell.physiology.org/cgi/content/full/284/2/C571  \nCellType  macrophage  \nSource  Ariadne Pathways  \n--------------------------------------------------------------------------------\nMedLine Reference  10827000:1180  \nSentence  MEK1 activity was assayed in muscle protein by measuring the ability of MEK1 immune complexes to phosphorylate a recombinant kinase-inactive MAPK (p42MAPK).  \nJournal  Endocrin. Metabol  \nJournal Reference  v278 i6 pE992 (2000)  \nJournal Link  http://ajpendo.physiology.org/cgi/content/full/278/6/E992  \nTissue  muscle  \nSource  Ariadne Pathways  \n--------------------------------------------------------------------------------\nMedLine Reference  12746434:1159  \nSentence  These activation kinetic data are consistent with the fact that ERK1/2 is specifically activated by MEK1/2.  \nJournal  J. Biol. Chem  \nJournal Reference  v278 i31 p29000 (2003)  \nJournal Link  http://www.jbc.org/cgi/content/full/278/31/29000  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  9207092:1125  \nSentence  Control experiments demonstrated that ERK2 and p38alpha were activated by their cognate MAP kinase kinases, MKK1 and MKK6 (data not shown).  \nJournal  PNAS  \nJournal Reference  v94 i14 p7337 (1997)  \nJournal Link  http://www.pnas.org/cgi/content/full/94/14/7337  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  10636870:1150  \nSentence  MEK1/2 inhibition prevents H 2 O 2 -mediated activation of ERK1/2 to a greater extent than activation of p90RSK.  \nJournal  J. Biol. Chem  \nJournal Reference  v275 i3 p1739 (2000)  \nJournal Link  http://www.jbc.org/cgi/content/full/275/3/1739  \nCellLineName  JURKAT  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11303030:1103  \nSentence  The closely related mammalian kinases, ERK1 and ERK2 (also called p44 and p42), are activated by the MEK1/2 kinases in response to mitogenic signals.  \nJournal  J. Biol. Chem  \nJournal Reference  v276 i24 p20805 (2001)  \nJournal Link  http://www.jbc.org/cgi/content/full/276/24/20805  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11571230:1117  \nSentence  Assessment of VES-induced differentiation after blockage of ERK1/2 activation by MEK1 using the chemical inhibitor PD 98059.  \nJournal  Cell Growth and Diff  \nJournal Reference  v12 i9 p471 (2001)  \nJournal Link  http://cgd.aacrjournals.org/cgi/content/full/12/9/471  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  12226077:1214  \nSentence  Expression of dominant negative MEK1 significantly attenuates the bFGF-induced phosphorylation of ERK1/2 (Fig. 3 C , lane 4 on the bottom panel ).  \nJournal  J. Biol. Chem  \nJournal Reference  v277 i46 p44417 (2002)  \nJournal Link  http://www.jbc.org/cgi/content/full/277/46/44417  \nSource  Ariadne Pathways  \n--------------------------------------------------------------------------------\nMedLine Reference  12960148:1141  \nSentence  Furthermore, S100A1-mediated activation of ERK 1/2 could be prevented by preincubation with PD98095 (2-10 ÃÂ¯ÃÂ¿ÃÂ½ M ) ( Fig. 6 B ), a specific inhibitor of MEK1 ( 26 , 27 ).  \nJournal  J. Biol. Chem  \nJournal Reference  v278 i48 p48404 (2003)  \nJournal Link  http://www.jbc.org/cgi/content/full/278/48/48404  \nSource  Ariadne Pathways" .

<http://rdf.wikipathways.org/Pathway/WP722_r141562/Comment/bd546c20f3b14608309b514e86cf5625>
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        gpml:commentText  "MedLine Reference  11245588:10383  \nSentence  The three MAP kinase pathways regulate AP-1 activity both by increasing the transcription of the jun and fos genes and by phosphorylation of newly synthesized AP-1 transcription complexes. c-Fos gene transcription is activated by the cooperative interaction of Elk-1 with the serum response factor (SRF).  \nJournal  Cell Phys  \nJournal Reference  v280 i4 pC719  \nJournal Link  http://ajpcell.physiology.org/cgi/content/full/280/4/C719  \n\n--------------------------------------------------------------------------------\nMedLine Reference  12600988:10161  \nSentence  First, it has been concluded from many transfection (permanent and transient) experiments that the serum response factor-ELK1 complex, likely also including the nearby AP-1 proteins, is required for the optimal transcriptional response to growth factors and to phorbol esters (TPA ).  \nJournal  J. Biol. Chem  \nJournal Reference  v278 i18 p15794  \nJournal Link  http://www.jbc.org/cgi/content/full/278/18/15794  \n\n--------------------------------------------------------------------------------\nMedLine Reference  10477597:10028  \nSentence  Also, they phosphorylate Elk1, which interacts with the serum response factor and participates in c- fos activation (reviewed in Refs. 18 and 19 ).  \nJournal  J. Immunol  \nJournal Reference  v163 i6 p3279  \nJournal Link  http://www.jimmunol.org/cgi/content/full/163/6/3279  \n\n--------------------------------------------------------------------------------\nMedLine Reference  131101359:11268  \nSentence  D. (1994) The transcription factors Elk-1 and serum response factor interact by direct protein-protein contacts mediated by a short region of Elk-1.  \nJournal  J. Neurochem  \nJournal Reference  v77 i1 p25  \nJournal Link  http://www.blackwell-synergy.com/doi/full/10.1046/j.1471-4159.2001.00232.x  \n\n--------------------------------------------------------------------------------\nMedLine Reference  131104515:11133  \nSentence  We have designed and expressed a dominant-negative mutant of Elk-1 that binds to DNA and serum response factor but lacks the phosphorylation-dependent transcriptional activation domain.  \nJournal  J. Neurochem  \nJournal Reference  v97 i1 p8  \nJournal Link  http://www.blackwell-synergy.com/doi/full/10.1111/j.1471-4159.2006.03749.x  \n\n--------------------------------------------------------------------------------\nMedLine Reference  162101848:11031  \nSentence  One possibility is that the sequence-specificity of DNA recognition by Sd is augmented by the coactivator; this could be achieved, for example, if Vg itself contacts some bases or if it alters the stability of Sdthat confer added DNA-binding specificity on a complex by contacting the DNA, as in the interactions of SAP1 and ELK-1 with serum response factor [ 14 ].  \nJournal  Current Biology  \nJournal Reference  v9 i7 p7  \nJournal Link  http://www.current-biology.com/content/article/fulltext?uid=PIIS0960982299801547  \nOrgan  wing  \n\n--------------------------------------------------------------------------------\nMedLine Reference  9755064:10025  \nSentence  Activated Elk-1 interacts with the serum response factor (SRF) to mediate transcription through serum response elements (SREs) and adjacent Ets motif sequences contained within the 5&apos;-flanking region of several genes (reviewed in Ref. 24 ), including the immediate-early gene (IEG) Egr-1 ( 59 ).  \nJournal  Cell Phys  \nJournal Reference  v275 i4 pC1104  \nJournal Link  http://ajpcell.physiology.org/cgi/content/full/275/4/C1104  \nTissue  serum  \n\n--------------------------------------------------------------------------------\nMedLine Reference  10196167:10161  \nSentence  Elk-1 forms a ternary complex with serum response factor and the serum response element (SRE ) that is present in many genes ( 35 ).  \nJournal  J. Biol. Chem  \nJournal Reference  v274 i16 p10897  \nJournal Link  http://www.jbc.org/cgi/content/full/274/16/10897  \nTissue  serum  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11053438:10182  \nSentence  Activation of Transcription Factor Elk1 during Thapsigargin-induced pip92 Expression-- Previous studies have shown that serum response element (SRE ) present in the pip92 promoter can interact with recombinant serum response factor (SRF ) and Elk1 proteins forming a tertiary complex ( 16 , 25 ).  \nJournal  J. Biol. Chem  \nJournal Reference  v276 i3 p2132  \nJournal Link  http://www.jbc.org/cgi/content/full/276/3/2132  \nTissue  serum  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11839761:10228  \nSentence  When phosphorylated by ERK2, Elk-1 forms a complex with the serum response factor and binds the serum response promoter element to enhance transcription from the c- fos promoter.  \nJournal  J. Biol. Chem  \nJournal Reference  v277 i16 p13889  \nJournal Link  http://www.jbc.org/cgi/content/full/277/16/13889  \nTissue  serum" .

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        gpml:commentText  "--------------------------------------------------------------------------------\nMedLine Reference  11454682:1161  \nSentence  Activated ERK1/2 phosphorylated Elk-1, which involves in the induction of the growth-related genes, suggesting that stimulative effects of low-dose irradiation were mediated by ERK1/2 activation.  \nJournal  Cancer Res  \nJournal Reference  v61 i14 p5396 (2001)  \nJournal Link  http://cancerres.aacrjournals.org/cgi/content/full/61/14/5396  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  10444401:1223  \nSentence  Once in the nucleus, ERK can phosphorylate and activate transcription factors such as TCF/ELK-1, resulting in c-Fos production and AP-1 complex formation ( 13 , 15 ).  \nJournal  Cell Phys  \nJournal Reference  v277 i2 pC253 (1999)  \nJournal Link  http://ajpcell.physiology.org/cgi/content/full/277/2/C253  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11090049:1273  \nSentence  Therefore, it has been proposed that Elk1-dependent gene activation can occur independently of SRE/SRF if it can bind to the promoter efficiently. 50 This proposition is supported by the finding that the phosphorylation of Elk1 by ERK2 increases its ability to bind to DNA without interacting with SRF 54 , 55 and by the fact that Elk1 binding is facilitated in transfection experiments with a reporter gene containing multiple high-affinity Elk1 binding sites 40 , 56 or phosphorylation in its C-terminus. 55 , 57 Even though the 9E3/cCAF promoter does not contain an SRE, Elk1 binds to the Elk1 elements and activates transcription, suggesting that thrombin-induced Elk1 activation does not require cooperation with SRF.  \nJournal  Blood  \nJournal Reference  v96 i12 p3696 (2000)  \nJournal Link  http://www.bloodjournal.org/cgi/content/full/96/12/3696  \nTissue  smooth muscle  \nOrgan  umbilical vein  \nCellType  fibroblast  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11812784:1038  \nSentence  Activated ERK1/2 phosphorylated Elk-1, which involves in the induction of the growth-related genes, suggesting that stimulative effects of low-dose irradiation were mediated by ERK1/2 activation.  \nJournal  EBM  \nJournal Reference  v277 i15 p12532 (2002)  \nJournal Link  http://www.blackwell-synergy.com/links/doi/10.1046/j.1471-4159.2002.01075.x/full/  \nTissue  stroma  \nOrgan  renal  \nCellType  b cell  \nCellLineName  JEG3  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  10463587:1029  \nSentence  MAP kinase (MAPK/ERK) phosphorylates Elk-1, which is part of the ternary complex factor that binds to the serum response element in the fos promotor; JNK phosphorylates c-Jun, Elk-1, and ATF-2; and p38 kinase phosphorylates both ternary-complex-factor /Elk-1 and ATF-2.  \nJournal  Cancer Res  \nJournal Reference  v59 i16 p3935 (1999)  \nJournal Link  http://cancerres.aacrjournals.org/cgi/content/full/59/16/3935  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11520792:1024  \nSentence  TCFs, such as Elk-1, Sap-1, and Fli-1, are targets of the MAPK pathway. 36 , 37 Our data indicated that phosphorylation of Elk-1 by the MEK-ERK1/2 pathway induces Egr-1 expression in LPS-stimulated monocytes and subsequent TF gene expression.  \nJournal  Blood  \nJournal Reference  v98 i5 p1429 (2001)  \nJournal Link  http://www.bloodjournal.org/cgi/content/full/98/5/1429  \nCellType  monocyte  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  12495932:1207  \nSentence  In summary, this study has demonstrated, in a rat in vivo model, that both serpentine and amphibole asbestos fibers induced protracted phosphorylation of intrapulmonary ERK proteins and upregulated Elk-1 phosphorylation by ERK.  \nJournal  AJRCMB  \nJournal Reference  v28 i1 p51 (2003)  \nJournal Link  http://ajrcmb.atsjournals.org/cgi/content/full/28/1/51  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------" .

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        gpml:commentText  "inositol 1,4,5-triphosphate receptor 1" .

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        gpml:commentText  "MedLine Reference  10625698:1034  \nSentence  Activated MAPK interacts with a number of downstream targets, including the p90 ribosomal S6 kinase (p90 Rsk ) ( 19 ) and MAPK-activated protein kinase-2 (MAPKAP-K2 ) ( 20 , 21 ), which are activated by ERK1/2 and p38 MAPK , respectively.  \nJournal  J. Biol. Chem  \nJournal Reference  v275 i2 p1457 (2000)  \nJournal Link  http://www.jbc.org/cgi/content/full/275/2/1457  \nOrgan  ventricle  \nCellType  myocyte  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  8846784:6  \nSentence  In contrast, full-length GST-MAPKAP kinase-2 was phosphorylated at Thr25 (and not activated) by p42 MAPK, suggesting a role for the N-terminal domain in specifying activation by RK in vivo.  \nCellLineName  KB  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  14499342:7  \nSentence  ERK phosphorylated MK2 in vitro and activated MK2 in f-methionyl-leucyl-phenylalanine (FMLP)-stimulated neutrophils.  \nCellType  neutrophil  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  8900202:1138  \nSentence  MBP is an efficient substrate for ERK1 and ERK2, whereas GST-cJun (1-169) includes the activating phosphorylation sites Ser-63 and Ser-73, which have been shown to be phosphorylated by SAPK/JNK but not by ERK1, ERK2, or p38 HOG1 ( 3 ). 2 Similarly, hsp27 is an efficient substrate for MAPKAPK2, which in turn is predominantly activated by p38 HOG1, although MAPKAPK2 can also be phosphorylated in vitro by ERK1 and ERK2 ( 29 , 30 ). -- Fig. 2.  \nJournal  J. Biol. Chem  \nJournal Reference  v271 i43 p27107 (1996)  \nJournal Link  http://www.jbc.org/cgi/content/full/271/43/27107  \nCellLineName  Pam 212  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  8798679:1021  \nSentence  Although p42 MAPK can also phosphorylate and activate MAPKAP kinase-2 in vitro , the MAPK pathway is not activated by these stresses; conversely, activation of the MAPK pathway is not associated with activation of MAPKAP kinase-2 ( 9 , 11 ).  \nJournal  J. Biol. Chem  \nJournal Reference  v271 i40 p24313 (1996)  \nJournal Link  http://www.jbc.org/cgi/content/full/271/40/24313  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  10022874:1302  \nSentence  The MAP kinase-activated protein kinases, Rsk and MAPKAPK-2, are similarly phosphorylated in their T loops by ERK and p38, respectively ( 2 , 8 ).  \nJournal  Mol. Cell. Biol  \nJournal Reference  v19 i3 p1871 (1999)  \nJournal Link  http://mcb.asm.org/cgi/content/full/19/3/1871  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  12649327:1050  \nSentence  Both ERK and p38 can phosphorylate CREB via several downstream kinases including MSK1 for ERK and p38, p90RSK for ERK, and MAPKAPK2 for p38 ( 12 , 14 , 26 ).  \nJournal  Mol. Endocrin  \nJournal Reference  v17 i6 p1131 (2003)  \nJournal Link  http://mend.endojournals.org/cgi/content/full/17/6/1131  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  14688255:1134  \nSentence  This co-expression system was used previously in our laboratory to activate GST-RSK CTD ( 21 ), and ERK2 has been reported to activate MK2 ( 26 ).  \nJournal  J. Biol. Chem  \nJournal Reference  v279 i11 p10176 (2004)  \nJournal Link  http://www.jbc.org/cgi/content/full/279/11/10176  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  8995385:1254  \nSentence  First, LY294002, which inhibited Erk-1 and 2 but not p38, failed to inhibit MAPKAPK-2.  \nJournal  J. Biol. Chem  \nJournal Reference  v272 i2 p937 (1997)  \nJournal Link  http://www.jbc.org/cgi/content/full/272/2/937  \nCellType  leukocyte  \nSource  Ariadne Pathways  \n--------------------------------------------------------------------------------\nMedLine Reference  11463795:1195  \nSentence  With respect to alternative non-PLD/PA mechanisms whereby ERK could conceivably activate PKC-eta/ , it has been reported that ERK-activated MAPK-activated kinase-2 ( 34 , 35 ) and MSK-1 ( 36 ) can act like PDK-1 and/or PDK-2 and phosphorylate PKB on serine 308 and threonine 473 residues.  \nJournal  J. Biol. Chem  \nJournal Reference  v276 i38 p35537 (2001)  \nJournal Link  http://www.jbc.org/cgi/content/full/276/38/35537  \nTissue  skeletal muscle  \nCellType  adipocyte  \nSource  Ariadne Pathways" .

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<https://identifiers.org/pubmed/9346921>
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<https://identifiers.org/pubmed/11907026>
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<http://rdf.wikipathways.org/Pathway/WP722_r141562/Comment/b4f7ff326f88d952100e71de40f1b6fc>
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<https://identifiers.org/pubmed/1038>
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<https://identifiers.org/pubmed/9808624>
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<https://identifiers.org/pubmed/11120810>
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<https://identifiers.org/pubmed/8429046>
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<https://identifiers.org/pubmed/9422727>
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        gpml:commentText  "5-hydroxytryptamine (serotonin) receptor 2A" .

<http://rdf.wikipathways.org/Pathway/WP722_r141562/Interaction/db29d/Point/c1cc9446085c4cae045f26cf77525212>
        rdf:type          gpml:Point ;
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<http://rdf.wikipathways.org/Pathway/WP722_r141562/Comment/5aab980b4129f36d739ee245235f969b>
        rdf:type          gpml:Comment ;
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        gpml:commentText  "MedLine Reference  12842874:1221  \nSentence  Several other kinases such as CKII, MAPK, PKC, and CaMK are known to phosphorylate CREB and thereby activate CREB-dependent transcription ( 25 , 26 , 29 , 30 , 49 , 56 - 59 ).  \nJournal  J. Biol. Chem  \nJournal Reference  v278 i40 p38860 (2003)  \nJournal Link  http://www.jbc.org/cgi/content/full/278/40/38860  \nCellType  b cell  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  10931853:1209  \nSentence  However, others have suggested that calcium/calmodulin-dependent kinases, Ras/mitogen-activated protein kinase, and protein kinase C can phosphorylate CREB at Ser 133 ( 47-49 ).  \nJournal  J. Biol. Chem  \nJournal Reference  v275 i43 p33365 (2000)  \nJournal Link  http://www.jbc.org/cgi/content/full/275/43/33365  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11416000:1287  \nSentence  CRE- binding protein (CREB) has been reported to be phosphorylated by MAP kinase-activated protein kinase, possibly through p70S6K, as well as cAMP kinase ( 35 , 36 ).  \nJournal  Endocrinology  \nJournal Reference  v142 i7 p2811 (2001)  \nJournal Link  http://endo.endojournals.org/cgi/content/full/142/7/2811  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  10098484:1177  \nSentence  However, the MEK inhibitor PD98059 was not able to modulate phosphorylation of CREB at a dose that fully inhibited the phosphorylation of MAP kinase (Fig. 6b ).  \nJournal  Endocrinology  \nJournal Reference  v140 i4 p1525 (1999)  \nJournal Link  http://endo.endojournals.org/cgi/content/full/140/4/1525  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  10951185:1095  \nSentence  This could occur via RSK2, a protein kinase activated by MAP kinases/ERKs, that phosphorylates CREB on its activator site serine 133 [ 43 ].  \nJournal  Eur. J. Biochem  \nJournal Reference  v267 i17 p5280.html) (2000)  \nJournal Link  http://www.ejbiochem.org/cgi/content/full/267/17/5280.h  \nCellType  dendritic  \nSource  Ariadne Pathways" .

<https://identifiers.org/pubmed/7559496>
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        gpml:commentText  "DirectRegulation RASGRF1 --+> Ras" .

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        gpml:commentText  "ProtModification MAP2K6 --+> MAPK14," .

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<https://identifiers.org/pubmed/1273>
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        gpml:commentText  "MedLine Reference  8887554:4  \nSentence  We show that MAPKAP kinase-2 phosphorylates CREB at Ser133 in vitro, that the FGF- or stress-induced activation of MAPKAP kinase-2 and phosphorylation of CREB and ATF-1 are prevented by similar concentrations of the specific p38 MAP kinase inhibitor SB 203580, and that MAPKAP kinase-2 is the only detectable SB 203580-sensitive CREB kinase in SK-N-MC cell extracts.  \nCellLineName  sk-n-mc  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  10487749:1189  \nSentence  MK2 phosphorylates the nuclear transcription factors CREB (Tan et al. , 1996 ; Iordanov et al. , 1997 ), ATF-1 (Tan et al. , 1996 ) and SRF (Heidenreich et al. , 1999 ), indicating a role in transcriptional regulation.  \nJournal  EMBO  \nJournal Reference  v18 i18 p4969 (1999)  \nJournal Link  http://embojournal.npgjournals.com/cgi/content/full/18/18/4969  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  9422727:1245  \nSentence  Although it has been shown that MAPKAPK-2 phosphorylates CREB at Ser-133 in vitro ( 73 ), we did not observe an increase in phosphorylation of CREB by MAPKAPK-2 activated by OA HS.  \nJournal  J. Biol. Chem  \nJournal Reference  v273 i2 p749 (1998)  \nJournal Link  http://www.jbc.org/cgi/content/full/273/2/749  \nCellLineName  9L  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  9139689:1033  \nSentence  One of the downstream targets of p38 is the MAPKAP kinase-2, which can activate the transcription factors CREB and ATF-1 ( 18 ) and phosphorylate heat-shock protein hsp27 ( 19 , 20 ).  \nJournal  J. Biol. Chem  \nJournal Reference  v272 i19 p12422 (1997)  \nJournal Link  http://www.jbc.org/cgi/content/full/272/19/12422  \nCellType  pre B  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11123233:1259  \nSentence  Furthermore, activation of MAPKAP kinase 2 results in activation of the transcriptional factor CREB ( 44 ) as well as HSP27 in human cells and HSP25 in bovine and murine cells ( 4 , 17 ).  \nJournal  Heart Circul  \nJournal Reference  v280 i1 pH189 (2001)  \nJournal Link  http://ajpheart.physiology.org/cgi/content/full/280/1/H189  \nCellLineName  P0  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11907026:1240  \nSentence  In contrast to EGF or NGF , fibroblast growth factor (FGF )-induced CREB phosphorylation is mediated by MAPKAP kinase-2 ( 14 ) that lies immediately downstream from p38MAPK.  \nJournal  J. Biol. Chem  \nJournal Reference  v277 i21 p18710 (2002)  \nJournal Link  http://www.jbc.org/cgi/content/full/277/21/18710  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  12810757:1144  \nSentence  Therefore, p90rsk2 and MAPKAP kinase-2 might be responsible for phosphorylation of CREB downstream from ERK and p38 MAPK, respectively.  \nJournal  Hypertension  \nJournal Reference  v42 i2 p177 (2003)  \nJournal Link  http://hyper.ahajournals.org/cgi/content/full/42/2/177  \nCellType  macrophage  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  9759836:1029  \nSentence  In addition, MAPKAPK-2, a downstream target for p38 MAPK, phosphorylates CREB in response to FGF and arsenite ( 33 ).  \nJournal  J. Immunol  \nJournal Reference  v161 i7 p3225 (1998)  \nJournal Link  http://www.jimmunol.org/cgi/content/full/161/7/3225  \nCellType  myocyte  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11278709:1233  \nSentence  PKA , PKC , CaM kinase, CK2 , MAPKAP kinase-2, p60 S6K , and p90 RSK have been reported to phosphorylate CREB .  \nJournal  J. Biol. Chem  \nJournal Reference  v276 i17 p13858 (2001)  \nJournal Link  http://www.jbc.org/cgi/content/full/276/17/13858  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11006268:1158  \nSentence  It has been reported that MAPKAP kinase-2 phosphorylates CREB in response to fibroblast growth factor in neuroblastoma cells ( 45 ).  \nJournal  J. Biol. Chem  \nJournal Reference  v275 i51 p40539 (2000)  \nJournal Link  http://www.jbc.org/cgi/content/full/275/51/40539  \nSource  Ariadne Pathways" .

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        gpml:commentText  "11292831 (Organ: brain, CellLineName: PC12D) We next showed in coimmunoprecipitation experiments that CalDAG-GEFI forms a complex with Rap1 and B-Raf following exposure to carbachol or calcium ionophore and the DAG analogue OAG (Fig. 8 ). \n\n9789079 (CellLineName: 293T) Expression of CalDAG-GEFI activates Rap1A and inhibits Ras-dependent activation of the Erk/MAP kinase cascade in 293T cells. \n\n14702343 (CellLineName: JURKAT) Our results have demonstrated that forced expression of CalDAG-GEFI activated endogenous Rap1 and augmented adhesion to ICAM-1 in response to TCR stimulation. \n\n10835426 (CellLineName: 293T) As reported previously ( 15 , 16 ), CalDAG-GEFI activated Rap1 and, to a lesser extent, R-Ras, and CalDAG-GEFII activated both Ha-Ras and R-Ras" .

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        gpml:commentText  "--------------------------------------------------------------------------------\nMedLine Reference  9927426:1014  \nSentence  Both p42 and p44MAPK are activated by dual phosphorylation on a threonine and a tyrosine residue, achieved by the dual-specificity kinase MKK1/2.  \nJournal  EMBO  \nJournal Reference  v18 i3 p664 (1999)  \nJournal Link  http://embojournal.npgjournals.com/cgi/content/full/18/3/664  \nCellType  fibroblast  \nCellLineName  PC 12  \nSource  Ariadne Pathways  \n--------------------------------------------------------------------------------\nMedLine Reference  12393899:1257  \nSentence  Furthermore, expression of a constitutively active MKK1, which directly activated ERK1/2, suppressed cortical neuron apoptosis induced by expression of recombinant wild-type GSK3eta or the GSK3eta(S9A) mutant.  \nJournal  J. Biol. Chem  \nJournal Reference  v277 i51 p49577 (2002)  \nJournal Link  http://www.jbc.org/cgi/content/full/277/51/49577  \nTissue  cortex  \nSource  Ariadne Pathways  \n--------------------------------------------------------------------------------\nMedLine Reference  10958792:5  \nSentence  In the ovarian carcinoma cell line A2780, inhibition of ERK1/2 activation with the mitogen-activated protein kinase/ERK kinase 1 (MEK1) inhibitor PD98059 resulted in decreased p53 protein half-life and diminished accumulation of p53 protein during exposure to cisplatin.  \nCellLineName  A2780  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  9159118:3  \nSentence  Inhibiting activation of ERK1 and ERK2 with the MEK1/2 inhibitor PD98059 has no effect on insulin secretion, indicating that ERK activity is not necessary for secretion under these conditions.  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11673351:5  \nCellType  cardiomyocyte  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  10711350:4  \nSentence  PD98059, a specific inhibitor of MEK-1 which phosphorylates p44/p42 MAP kinase, strongly suppressed both the thapsigargin (30 nM)- and TPA (30 nM)-induced histamine production, whereas SB203580, a specific inhibitor of p38 MAP kinase, inhibited them only partially. 6.  \nCellType  macrophage  \nCellLineName  RAW264.7  \nSource  Ariadne Pathways  \n\n--------------------------------------------------------------------------------\nMedLine Reference  11496823:2  \nSentence  PD98059, a specific inhibitor of MEK-1 which phosphorylates p44/p42 MAP kinase, strongly suppressed the thapsigargin-induced histamine production, the increase in HDC mRNA level and 74-kDa HDC protein expression.  \nCellType  macrophage  \nCellLineName  RAW264.7  \nSource  Ariadne Pathways  \n--------------------------------------------------------------------------------\nMedLine Reference  9235901:1031  \nSentence  In the mammalian Erk1/2 pathway, the proximal kinases Raf-1 and B-Raf phosphorylate and activate the dual function threonine/tyrosine kinases MAP/Erk kinases 1 and 2, which in turn phosphorylate Erk1/2.  \nJournal  J. Biol. Chem  \nJournal Reference  v272 i31 p19125 (1997)  \nJournal Link  http://www.jbc.org/cgi/content/full/272/31/19125  \nOrgan  heart  \nCellType  myocyte  \nCellLineName  AR  \nSource  Ariadne Pathways" .

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        dcterms:isPartOf     <http://rdf.wikipathways.org/Pathway/WP722_r141562> ;
        gpml:align           "Center" ;
        gpml:centerX         "505.98333333333335"^^xsd:double ;
        gpml:centerY         "643.6499999999988"^^xsd:double ;
        gpml:color           "0" ;
        gpml:fillColor       "ffffff" ;
        gpml:fontDecoration  "Normal" ;
        gpml:fontName        "Arial" ;
        gpml:fontSize        "12.0"^^xsd:double ;
        gpml:fontStrikethru  "Normal" ;
        gpml:fontStyle       "Normal" ;
        gpml:fontWeight      "Normal" ;
        gpml:graphId         "f0d8b" ;
        gpml:hasComment      <http://rdf.wikipathways.org/Pathway/WP722_r141562/Comment/69ad5ca35e2c54e517d1cc7983e89506> ;
        gpml:height          "25.0"^^xsd:double ;
        gpml:lineStyle       "Solid" ;
        gpml:lineThickness   "1.0"^^xsd:double ;
        gpml:shapeType       "Rectangle" ;
        gpml:textlabel       "MAP2K6" ;
        gpml:type            "GeneProduct" ;
        gpml:valign          "Middle" ;
        gpml:width           "60.0"^^xsd:double ;
        gpml:xrefDataSource  "Entrez Gene" ;
        gpml:xrefId          "5608" ;
        gpml:zorder          "32889"^^xsd:long .

<http://rdf.wikipathways.org/Pathway/WP722_r141562/Comment/a5a998e78c855919a67e1fd8ae7d7de7>
        rdf:type          gpml:Comment ;
        dcterms:isPartOf  <http://rdf.wikipathways.org/Pathway/WP722_r141562/Interaction/c6702> ;
        gpml:commentText  "Binding GNAI3 ---- HTR1E" .

<https://identifiers.org/pubmed/12649327>
        rdf:type          gpml:PublicationXref ;
        dcterms:isPartOf  <http://rdf.wikipathways.org/Pathway/WP722_r141562/Interaction/f644b> ;
        gpml:database     "Pubmed" ;
        gpml:id           "12649327" .

<https://identifiers.org/pubmed/15155836>
        rdf:type          gpml:PublicationXref ;
        dcterms:isPartOf  <http://rdf.wikipathways.org/Pathway/WP722_r141562/Interaction/ffa2d> ;
        gpml:database     "Pubmed" ;
        gpml:id           "15155836" .
