SPAK kinase is a substrate and target of PKCtheta in T-cell receptor-induced AP-1 activation pathway. - Wikidata - wikimedia - TriplyDB

SPAK kinase is a substrate and target of PKCtheta in T-cell receptor-induced AP-1 activation pathway.

SPAK kinase is a substrate and target of PKCtheta in T-cell receptor-induced AP-1 activation pathway.

http://www.wikidata.org/entity/Q37259298

about

Crystal structure of domain-swapped STE20 OSR1 kinase domain Ameliorated ConA-induced hepatitis in the absence of PKC-theta Overexpression of Ste20-related proline/alanine-rich kinase exacerbates experimental colitis in mice Structural and biochemical insights into the activation mechanisms of germinal center kinase OSR1.Ste20-related proline/alanine-rich kinase (SPAK) regulated transcriptionally by hyperosmolarity is involved in intestinal barrier function.Complement regulator CD46 temporally regulates cytokine production by conventional and unconventional T cells.The SWI/SNF chromatin-remodeling complex modulates peripheral T cell activation and proliferation by controlling AP-1 expression.On the substrate recognition and negative regulation of SPAK, a kinase modulating Na+-K+-2Cl- cotransport activity Characterization of SPAK and OSR1, regulatory kinases of the Na-K-2Cl cotransporter.WNK1 regulates phosphorylation of cation-chloride-coupled cotransporters via the STE20-related kinases, SPAK and OSR1.Lipid raft targeting of hematopoietic protein tyrosine phosphatase by protein kinase C theta-mediated phosphorylation.C. elegans STK39/SPAK ortholog-mediated inhibition of ClC anion channel activity is regulated by WNK-independent ERK kinase signaling Ischemia-induced stimulation of cerebral microvascular endothelial cell Na-K-Cl cotransport involves p38 and JNK MAP kinases.Protein kinase C and beyond.Molecular physiology of SPAK and OSR1: two Ste20-related protein kinases regulating ion transport.A novel role for CD46 in wound repair MST-4 and TRAF-6 expression in the peripheral blood mononuclear cells of patients with Graves' disease and its significance.The PKCθ pathway participates in the aberrant accumulation of Fra-1 protein in invasive ER-negative breast cancer cells.A critical role for protein kinase C-theta-mediated T cell survival in cardiac allograft rejection.Protein kinase C theta (PKCtheta): a key player in T cell life and death Multigene kinase network, kidney transport, and salt in essential hypertension.Nuclear factor-kappaB is a critical mediator of Ste20-like proline-/alanine-rich kinase regulation in intestinal inflammation BCL11B enhances TCR/CD28-triggered NF-kappaB activation through up-regulation of Cot kinase gene expression in T-lymphocytes.Differential requirement of PKC-theta in the development and function of natural regulatory T cells.Ste20-related proline/alanine-rich kinase: a novel regulator of intestinal inflammation.Epigenetic silencing of Stk39 in B-cell lymphoma inhibits apoptosis from genotoxic stress.No specific subcellular localization of protein kinase C is required for cytotoxic T cell granule exocytosis.Physiology and pathophysiology of SLC12A1/2 transporters.The yin and yang of protein kinase C-theta (PKCθ): a novel drug target for selective immunosuppression.Germinal center kinases in immune regulation.Kinase regulation of Na+-K+-2Cl- cotransport in primary afferent neurons.PKC-θ function at the immunological synapse: prospects for therapeutic targeting.SPAK mediates KCC3-enhanced cervical cancer tumorigenesis.PKCdelta acts upstream of SPAK in the activation of NKCC1 by hyperosmotic stress in human airway epithelial cells.PKCα and PKCβ cooperate functionally in CD3-induced de novo IL-2 mRNA transcription.Role for protein kinase Ctheta (PKCtheta) in TCR/CD28-mediated signaling through the canonical but not the non-canonical pathway for NF-kappaB activation.Intervention of PKC-θ as an immunosuppressive regimen.PKC-theta-mediated signal delivery from the TCR/CD28 surface receptors.Volume sensitivity of cation-Cl- cotransporters is modulated by the interaction of two kinases: Ste20-related proline-alanine-rich kinase and WNK4.Human immunodeficiency virus reactivation by phorbol esters or T-cell receptor ligation requires both PKCalpha and PKCtheta.

P2860

Q27653598-6EEFF1AA-581F-429D-ACFE-18B9F1B9ED1E Q28480548-A9B06804-AA28-416B-905A-3BB7BA8A5BA2 Q28507355-48786580-E0CD-4D82-B924-F9D041991BB7 Q30368586-03013ACB-196D-442D-9124-66697FB7C6E3 Q33426315-A03EF47A-2E55-4EC3-A087-D7473B2EAC4B Q33570304-FED47BC3-59CB-4752-B689-A0E013F4304B Q33593861-B632FA93-85E6-484B-9A6B-AD580036816A Q34149727-DD530CDA-77E0-4415-A13C-EFAF99D944E0 Q34301998-33EFF3CE-BAF9-46E0-9737-1CB85DDDC34D Q34464530-709157EB-B38B-4428-AB50-FD48FDDECB3E Q34519767-1205BD31-61FF-434B-9B9B-6D1FB3797DFE Q34718042-7E7FD55F-FDEE-4D13-AE37-1A2D31CC0504 Q35780018-0535F334-A1DB-434D-8ACB-0C14C3CA3B42 Q35849920-7617F1B1-E648-48CD-B427-4EED3119E974 Q35900778-23CEE625-0D1B-4933-A362-7168715E6E95 Q35928410-7340DD80-F7B9-42E0-A68F-E74834857937 Q36285625-89FA84DF-2101-4D3A-A9F8-6291AA347446 Q36760840-20940455-BE25-4596-B424-AF31AFE8DE5A Q36797508-FC576D3A-17EA-474F-96AA-7C01C50F9A0A Q36838094-2A9AE33A-96CF-48B6-BF16-48741797F38D Q36862737-B56E87D7-471B-43BE-A36D-7A765CE3335D Q36891517-59E9FCEE-467F-435F-B6FA-705F9FE8CAFB Q37091336-DDB0C3B2-0DCB-4845-8745-A72704B33A08 Q37236962-6B29576D-3724-41CF-A9F5-646E47C7C4D3 Q37318058-BA9F659B-7AB4-4A77-AEED-6710E6916C18 Q37362114-260DE8BD-6D35-4794-BB69-4F99685DBB75 Q37375740-4CAFE775-379F-4CB3-B8F2-B9BF7CA6AD4C Q37424563-D1C1A38A-B04B-41C3-8019-61F6AF0F3DAB Q37520009-EAC704E2-C33E-4088-811E-82FAC9F45B42 Q37727837-F9372028-77EA-4730-B73B-388FB3DBEA3B Q37760377-D5CF8321-BF62-4D2F-9B1B-0D032B3F563A Q37898306-E85B5BFA-5464-4F89-9D99-FEDF7054A6C9 Q39013208-64900F27-8ED3-4ED8-92DF-6D7F80B7589D Q39972775-4512E143-1030-4D76-B6F8-B4274FBC44C4 Q40290918-13EE9AAE-E97C-482F-A8CE-312AB689780B Q40493934-0033D75B-7BC2-4FA9-9D93-52FEE75FA51D Q41890374-E08B18ED-A5B7-4C60-81EA-C2D5947767A6 Q42287222-5EFB01C7-66E4-4476-A133-01CDC126205E Q42479166-645FFCAE-C146-44E8-8F56-7E53F6F38FCD Q42929742-43D5CCC7-D2C4-450D-8E33-AD3219633910

P2860

SPAK kinase is a substrate and target of PKCtheta in T-cell receptor-induced AP-1 activation pathway.

http://www.wikidata.org/entity/Q37259298

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 26 February 2004

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

SPAK kinase is a substrate and ...... duced AP-1 activation pathway.

@en

SPAK kinase is a substrate and ...... duced AP-1 activation pathway.

@nl

type

label

SPAK kinase is a substrate and ...... duced AP-1 activation pathway.

@en

SPAK kinase is a substrate and ...... duced AP-1 activation pathway.

@nl

prefLabel

SPAK kinase is a substrate and ...... duced AP-1 activation pathway.

@en

SPAK kinase is a substrate and ...... duced AP-1 activation pathway.

@nl

P1433

Q37259298-C0AC068D-C012-4B03-8720-57ECB495954E

P1476

Q37259298-2387FE2B-9683-43DF-B200-F6CCA84A8119

P2093

Q37259298-0919B2D0-5ECE-4D60-B4FD-8231D736353E

Q37259298-0FB5887F-FEF4-4DD7-9FA3-B55DEE63BABB

Q37259298-57CE8C4F-DE50-432E-A0B0-FB1569B05C78

Q37259298-B97E1A2F-FFCC-496A-897C-732EBE2106B1

Q37259298-C4E9AE2D-C6E7-4724-9BF2-D46D953563E5

Q37259298-D05499B0-FFA9-4D7E-8722-9C4A11820368

P2860

Q37259298-02C0399B-FBBE-46EF-9507-D129629609F1

Q37259298-07F9FFA5-2CBD-4C3C-94BE-D8BF9362BCF1

Q37259298-0AC2D3F8-FEA0-40CE-904B-7E05562D63A2

Q37259298-34965276-647B-44AF-AD31-24C8CD0B599D

Q37259298-389C8541-C736-402A-8320-389E9A304319

Q37259298-3BF6DEF6-ACF8-42DA-93C4-4AFF600AABB3

Q37259298-3D2462C8-C6FC-4F18-89EF-0B67E48D76F6

Q37259298-3E5CCCBC-8839-44AD-88CD-2AAEC0D747CE

Q37259298-4A719575-07D4-423D-B744-B20F243C8DB1

Q37259298-57A76DFC-6036-4064-B13B-769266A27744

P304

Q37259298-CC8F281D-F7A4-41C6-8376-EBFEC4E85E6D

P31

Q37259298-EC49FB43-4376-4EBC-B60B-571C47127561

P356

Q37259298-13D6479A-4F77-4605-8435-8AE6A7F20F0D

P407

Q37259298-0D23E496-0175-416E-AD05-F611A13A2706

P433

Q37259298-B269D339-FA13-44F9-978C-FA3360A60E90

P478

Q37259298-A99BFBE4-3C01-4424-9000-3A0681F04BA4

P577

Q37259298-41472882-F0FA-4F8E-8620-6F10B554157E

P5875

Q37259298-8B422D98-D530-4188-B034-3C8689DC17BC

P698

Q37259298-E6233E68-4F0B-41E6-9CB9-BD5686580257

P932

Q37259298-AA974A38-9304-461A-8B20-2D41AA668752

P356

SJ.EMBOJ.7600125

P1433

The EMBO Journal

P1476

SPAK kinase is a substrate and ...... duced AP-1 activation pathway.

@en

P2093

Amnon Altman

http://www.w3.org/2001/XMLSchema#string

Binggang Sun

http://www.w3.org/2001/XMLSchema#string

Hiroki Tabata

http://www.w3.org/2001/XMLSchema#string

Junru Hu

http://www.w3.org/2001/XMLSchema#string

Randi Vita

http://www.w3.org/2001/XMLSchema#string

Yingqiu Li

http://www.w3.org/2001/XMLSchema#string

P2860

Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-kappaB pathways by PICOT, a novel protein kinase C-interacting protein with a thioredoxin homology domain

SPAK, a STE20/SPS1-related kinase that activates the p38 pathway

CARMA1 is a critical lipid raft-associated regulator of TCR-induced NF-kappa B activation

Serine phosphorylation of Cbl induced by phorbol ester enhances its association with 14-3-3 proteins in T cells via a novel serine-rich 14-3-3-binding motif

CARD11 mediates factor-specific activation of NF-kappaB by the T cell receptor complex.

A requirement for CARMA1 in TCR-induced NF-kappa B activation

Three-dimensional segregation of supramolecular activation clusters in T cells

c-Jun can recruit JNK to phosphorylate dimerization partners via specific docking interactions

Selective modulation of protein kinase C-theta during T-cell activation

JNK is required for effector T-cell function but not for T-cell activation

P304

1112-1122

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1038/SJ.EMBOJ.7600125

http://www.w3.org/2001/XMLSchema#string

P407

P433

5

http://www.w3.org/2001/XMLSchema#string

P478

23

http://www.w3.org/2001/XMLSchema#string

P577

2004-02-26T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

8068699

http://www.w3.org/2001/XMLSchema#string

P698

14988727

http://www.w3.org/2001/XMLSchema#string

P932

380980

http://www.w3.org/2001/XMLSchema#string