PTP-SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal-regulated kinases ERK1 and ERK2 by association through a kinase interaction motif.
about
Interaction of mitogen-activated protein kinases with the kinase interaction motif of the tyrosine phosphatase PTP-SL provides substrate specificity and retains ERK2 in the cytoplasmA novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphataseSite-selective dephosphorylation of the platelet-derived growth factor beta-receptor by the receptor-like protein-tyrosine phosphatase DEP-1Scaffold role of a mitogen-activated protein kinase phosphatase, SKRP1, for the JNK signaling pathwayThe protein tyrosine phosphatase HePTP regulates nuclear translocation of ERK2 and can modulate megakaryocytic differentiation of K562 cellsHaematopoietic protein tyrosine phosphatase (HePTP) phosphorylation by cAMP-dependent protein kinase in T-cells: dynamics and subcellular locationCrystal structures and inhibitor identification for PTPN5, PTPRR and PTPN7: a family of human MAPK-specific protein tyrosine phosphatasesB56-containing PP2A dephosphorylate ERK and their activity is controlled by the early gene IEX-1 and ERKConstitutive induction of p-Erk1/2 accompanied by reduced activities of protein phosphatases 1 and 2A and MKP3 due to reactive oxygen species during cellular senescenceTumor suppressor density-enhanced phosphatase-1 (DEP-1) inhibits the RAS pathway by direct dephosphorylation of ERK1/2 kinasesInvestigation of protein-tyrosine phosphatase 1B function by quantitative proteomicsPhosphorylation of the kinase interaction motif in mitogen-activated protein (MAP) kinase phosphatase-4 mediates cross-talk between protein kinase A and MAP kinase signaling pathwaysIEX-1: a new ERK substrate involved in both ERK survival activity and ERK activationIdentification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions.The human phosphatase interactome: An intricate family portraitProtein tyrosine phosphatases--from housekeeping enzymes to master regulators of signal transductionProtein phosphatases and Alzheimer's diseaseActivation and function of the MAPKs and their substrates, the MAPK-activated protein kinasesIdentification of mitogen-activated protein kinase docking sites in enzymes that metabolize phosphatidylinositols and inositol phosphates.Role of Striatal-Enriched Tyrosine Phosphatase in Neuronal FunctionMolecular Targeting of ERKs/RSK2 Signaling Axis in Cancer PreventionReciprocal allosteric regulation of p38γ and PTPN3 involves a PDZ domain-modulated complex formationA specific protein-protein interaction accounts for the in vivo substrate selectivity of Ptp3 towards the Fus3 MAP kinase.The pheromone-induced nuclear accumulation of the Fus3 MAPK in yeast depends on its phosphorylation state and on Dig1 and Dig2.Protein-tyrosine Phosphatase and Kinase Specificity in Regulation of SRC and Breast Tumor KinaseDifferential interaction of the tyrosine phosphatases PTP-SL, STEP and HePTP with the mitogen-activated protein kinases ERK1/2 and p38alpha is determined by a kinase specificity sequence and influenced by reducing agentsCharacterization of a prostate-specific tyrosine phosphatase by mutagenesis and expression in human prostate cancer cellsMEKK1 binds raf-1 and the ERK2 cascade componentsERK2 mitogen-activated protein kinase binding, phosphorylation, and regulation of the PDE4D cAMP-specific phosphodiesterases. The involvement of COOH-terminal docking sites and NH2-terminal UCR regionsThe MAP-kinase ERK2 is a specific substrate of the protein tyrosine phosphatase HePTPPhosphotyrosine-specific phosphatase PTP-SL regulates the ERK5 signaling pathwayA novel dual specificity phosphatase SKRP1 interacts with the MAPK kinase MKK7 and inactivates the JNK MAPK pathway. Implication for the precise regulation of the particular MAPK pathwayIdentification of novel point mutations in ERK2 that selectively disrupt binding to MEK1Striatal-enriched protein tyrosine phosphatase expression and activity in Huntington's disease: a STEP in the resistance to excitotoxicityThe TriTryp phosphatome: analysis of the protein phosphatase catalytic domainsThe expression of the phosphotyrosine phosphatase DEP-1/PTPeta dictates the responsivity of glioma cells to somatostatin inhibition of cell proliferationExtracellular signal-regulated kinase activated by epidermal growth factor and cell adhesion interacts with and phosphorylates vinexinERK2 shows a restrictive and locally selective mechanism of recognition by its tyrosine phosphatase inactivators not shared by its activator MEK1Neuroprotective role of a brain-enriched tyrosine phosphatase, STEP, in focal cerebral ischemiaSegregation and crosstalk of D1 receptor-mediated activation of ERK in striatal medium spiny neurons upon acute administration of psychostimulants
P2860
Q22010423-5FCE66E0-24CB-4A67-9298-AE7BE8757CC9Q22010940-FDF830A9-543C-4878-8669-74D40AF5FA52Q22254150-745C3FA7-B038-4496-A7EB-9923F628DCBDQ24294660-08C48340-FBAC-4070-8ED9-ADBD9EE3248BQ24294952-2DF50552-F5CB-4FF3-9224-B9A51ED0A19FQ24299601-4FBD4DAB-768F-4115-AEF7-55B45C5E797FQ24302258-8093A338-865E-4891-8E5F-CB0265B738ECQ24303557-A820F9B6-1E1B-450E-B939-139A253B221FQ24306834-80424B58-0665-455D-B932-95F26FFBF9DDQ24316361-5C84975F-2B57-499A-AB9A-5675D720E10EQ24318475-7CE104E1-907A-484E-BFB1-B1819BCAD7B6Q24337592-1DB4ABB2-D28F-4A3F-874E-44931EF5A1C6Q24534869-C5C2512A-A20C-4C98-BE5F-ACDEB7AA7AD4Q24536356-F582071D-3708-448A-BE21-AB19BA975C17Q24604530-CDAB7AE4-FC32-49A4-B736-EF7597C1196EQ24622527-80F030A2-8B15-4C4B-824D-B2D6927F365BQ24632495-F08809A9-D94D-4BED-9429-2C8615EACB31Q24632768-E3E3D538-EDE1-4D58-AFBF-8B253F4697A3Q25255706-6B936148-AF34-4ACE-A0DB-2C2B67AFF1E4Q26748710-A1F57FE1-4EA0-4D1D-A198-A62A4B9E77F3Q26782527-F47441D0-73E4-4E71-8EC0-13881B02FBDCQ27695708-CC9ED6B5-4F27-4533-8BEF-52BE8F5472E8Q27934447-77AD1238-5F5A-4EA7-BBB0-64114D852E34Q27935754-0A8BF0B2-136B-4749-A3C9-BD28CEADA655Q28116384-5513A147-5419-4D59-9C84-EF30ACA4541AQ28116921-DC4CC774-0BD7-4747-A3E5-62AADA3D59BBQ28118863-A1F4E87A-C903-4A48-88FE-4E9FFBF141CEQ28145204-42D1C8A9-0889-4615-AA27-6009EA56BD02Q28145238-4A5D4971-45A8-4EBF-91EB-070DAB484BDFQ28145888-B4DC03BA-7C4D-47B1-8BF2-F11E251BCA49Q28202064-67BB5D8F-9EC0-4757-AFE4-763838A5E5CAQ28215085-CCA74A25-568B-406B-8662-B96FB530DCE2Q28217158-3EBEA1D7-32BA-4319-BCA6-8EB68D1A3853Q28239309-92B73AFF-9464-4E48-8758-16513248B8C6Q28258708-617BC774-BF79-4508-B533-FAE7270B137EQ28259893-0D0E1954-7915-4B25-8160-F381BDCF26C1Q28265686-D2B71F5A-9E50-4197-A2C4-527F6067C111Q28271104-2B7A73AB-A1AF-4CDE-B65B-63A78F7CE2A9Q28301445-4BEAA10C-82E2-41C4-910D-E74D0F106058Q28395155-9057AFDD-97A5-43D6-B578-183B979BA024
P2860
PTP-SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal-regulated kinases ERK1 and ERK2 by association through a kinase interaction motif.
description
1998 nî lūn-bûn
@nan
1998 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
name
PTP-SL and STEP protein tyrosi ...... ugh a kinase interaction motif
@nl
PTP-SL and STEP protein tyrosi ...... gh a kinase interaction motif.
@ast
PTP-SL and STEP protein tyrosi ...... gh a kinase interaction motif.
@en
type
label
PTP-SL and STEP protein tyrosi ...... ugh a kinase interaction motif
@nl
PTP-SL and STEP protein tyrosi ...... gh a kinase interaction motif.
@ast
PTP-SL and STEP protein tyrosi ...... gh a kinase interaction motif.
@en
prefLabel
PTP-SL and STEP protein tyrosi ...... ugh a kinase interaction motif
@nl
PTP-SL and STEP protein tyrosi ...... gh a kinase interaction motif.
@ast
PTP-SL and STEP protein tyrosi ...... gh a kinase interaction motif.
@en
P2860
P3181
P356
P1433
P1476
PTP-SL and STEP protein tyrosi ...... ugh a kinase interaction motif
@en
P2093
P2860
P304
P3181
P356
10.1093/EMBOJ/17.24.7337
P407
P577
1998-12-01T00:00:00Z