Activation of PRK1 by phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. A comparison with protein kinase C isotypes
about
Insulin stimulates PKCzeta -mediated phosphorylation of insulin receptor substrate-1 (IRS-1). A self-attenuated mechanism to negatively regulate the function of IRS proteinsRegulatory domain selectivity in the cell-type specific PKN-dependence of cell migrationP110delta, a novel phosphoinositide 3-kinase in leukocytesLocalization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62.The extended protein kinase C superfamilyThe PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organizationProteolytic activation of PKN by caspase-3 or related protease during apoptosisAn aPKC-exocyst complex controls paxillin phosphorylation and migration through localised JNK1 activationIsolation and characterization of a structural homologue of human PRK2 from rat liver. Distinguishing substrate and lipid activator specificitiesRho GTPase control of protein kinase C-related protein kinase activation by 3-phosphoinositide-dependent protein kinaseA 3-phosphoinositide-dependent protein kinase-1 (PDK1) docking site is required for the phosphorylation of protein kinase Czeta (PKCzeta ) and PKC-related kinase 2 by PDK1Multiple interactions of PRK1 with RhoA. Functional assignment of the Hr1 repeat motifPRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163Protein kinase C-zeta as a downstream effector of phosphatidylinositol 3-kinase during insulin stimulation in rat adipocytes. Potential role in glucose transportPhosphorylation events associated with different states of activation of a hepatic cardiolipin/protease-activated protein kinase. Structural identity to the protein kinase N-type protein kinasesHyperosmotic-induced protein kinase N 1 activation in a vesicular compartment is dependent upon Rac1 and 3-phosphoinositide-dependent kinase 1Specific binding of the Akt-1 protein kinase to phosphatidylinositol 3,4,5-trisphosphate without subsequent activationRho GTPases and their effector proteinsTofacitinib and analogs as inhibitors of the histone kinase PRK1 (PKN1).PKN binds and phosphorylates human papillomavirus E6 oncoprotein.N-Formyl peptide receptor subtypes in human neutrophils activate L-plastin phosphorylation through different signal transduction intermediates.Phosphatidylinositol 3-kinase-gamma activates Bruton's tyrosine kinase in concert with Src family kinases.Inhibition of phosphatidylinositol 3-kinase stimulates activity of the small-conductance K channel in the CCD.Site recognition and substrate screens for PKN family proteins.Akt, a target of phosphatidylinositol 3-kinase, inhibits apoptosis in a differentiating neuronal cell lineCrystal structures of PRK1 in complex with the clinical compounds lestaurtinib and tofacitinib reveal ligand induced conformational changes.Identification and cloning of centaurin-alpha. A novel phosphatidylinositol 3,4,5-trisphosphate-binding protein from rat brainJAK/STAT, Raf/MEK/ERK, PI3K/Akt and BCR-ABL in cell cycle progression and leukemogenesis.The Drosophila phosphoinositide 3-kinase Dp110 promotes cell growth.Identification of Highly Potent Protein Kinase C-Related Kinase 1 Inhibitors by Virtual Screening, Binding Free Energy Rescoring, and in vitro Testing.Inositol hexakisphosphate stimulates non-Ca2+-mediated and primes Ca2+-mediated exocytosis of insulin by activation of protein kinase CEnzyme kinetics and distinct modulation of the protein kinase N family of kinases by lipid activators and small molecule inhibitors.Protein Kinase C Epsilon Contributes to NADPH Oxidase Activation in a Pre-Eclampsia Lymphoblast Cell Model.Regulation of polarized morphogenesis by protein kinase C iota in oncogenic epithelial spheroids.Protein Kinase C-Related Kinase (PKN/PRK). Potential Key-Role for PKN1 in Protection of Hypoxic Neurons.Membrane translocation of novel protein kinase Cs is regulated by phosphorylation of the C2 domain.The protein kinase C super-family member PKN is regulated by mTOR and influences differentiation during prostate cancer progression.The insert region of RhoA is essential for Rho kinase activation and cellular transformation.Glucose-regulated glucagon secretion requires insulin receptor expression in pancreatic alpha-cells.Molecular mechanisms regulating protein kinase Czeta turnover and cellular transformation.
P2860
Q24291007-241880D7-E595-43C1-BE83-0AED46690B42Q24314028-C87E6D71-A9F0-4B1D-BE09-C5B0B6F756F8Q24314825-22578583-CB53-4DEC-8BCB-DA746CD695BAQ24523784-7A609651-BAA7-4C95-9140-F8B3005CDE6DQ24530820-E501DA64-8057-460A-86C7-F3FB6C006049Q24646620-5EC08CFE-E289-4B5F-A327-D9E9DBA8D3AAQ24682097-0F384343-AE92-4309-B314-678792AB3A46Q27325523-7849CF5A-E5CB-4CA0-A772-3B089CC71119Q28119092-49CD89A1-CE2B-45E7-AC9D-DA9BE444666FQ28141177-1B3F564F-3BFF-4D54-935C-D94415669DDFQ28141738-5F9A6F7B-7150-406A-9C8B-A36183A1BDC9Q28260212-862EE9B3-4D24-48B4-B209-F39A36D337D1Q28272935-34934187-0A41-4D53-BC23-9A552F6FBC4BQ28570514-8B9707D2-177A-4957-9A14-EE2F15B1DF9FQ28571582-82FBF713-2454-4D49-BC80-39B53182DD88Q28588648-A32AE2F2-72EF-4C15-80F3-EA2910D80607Q28616026-945046C4-424B-4B30-BCD3-1FCC8A44640EQ29547740-B25428D0-700C-4B7F-829C-ABDE51F3703DQ30313903-294EBF35-9155-4FC3-873E-99E513D803A8Q30870479-AC75549B-9E3B-44BB-8198-17ADD76245B4Q31011302-E2E00D96-46D5-45A8-8A08-DE0EB8DD928FQ33729893-3E6A8ABC-7C5C-42F5-8218-AB2C37BFBB53Q33761404-D620B6EA-E47A-4F0C-8225-A650FDDE787BQ33958672-6C7EE5C7-7E6F-441E-8DA1-3AA0D1059AB4Q33995467-15ECDE44-16BB-4B9C-9D19-D95E46991C4BQ34028255-13F8A9AD-BCAB-4F22-9A9A-A198FCF5DE6EQ34981771-F5A8483E-7404-4453-B576-EF124FD9585AQ35635353-34386192-AEE5-494A-8CC4-AB21AF35700FQ35915951-987E698F-3424-4869-9BE3-90D63CC55E57Q36089876-055E1564-CB26-451F-9773-E0258C233572Q36133451-CF5EC92E-5045-4A72-A224-1191763038BAQ36213543-F857C921-150E-490C-9DA3-80E2220DFB61Q37441560-C9D774F9-4A84-4065-8802-254171630401Q37537542-CE66BD7D-0E50-4DBE-92B2-5CC08113C5C2Q38213708-C08DCB6A-AE42-4C90-BC59-D72D18AC8BD9Q38306802-82772A00-6F47-4E80-8E19-340E2D834A3EQ39143807-B40EF113-9884-4A16-BF6C-9F49DD344814Q39460559-6ABDC6D9-C42A-4255-952C-35B37EBED18EQ40396199-2A2376A5-5873-4576-9BFA-6974877D9A3CQ40622798-39AF939D-42B8-4BBF-BBA9-1D98B2E5A62D
P2860
Activation of PRK1 by phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. A comparison with protein kinase C isotypes
description
1995 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 1995
@ast
im September 1995 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1995/09/22)
@sk
vědecký článek publikovaný v roce 1995
@cs
wetenschappelijk artikel (gepubliceerd op 1995/09/22)
@nl
наукова стаття, опублікована у вересні 1995
@uk
name
Activation of PRK1 by phosphat ...... with protein kinase C isotypes
@ast
Activation of PRK1 by phosphat ...... with protein kinase C isotypes
@en
Activation of PRK1 by phosphat ...... with protein kinase C isotypes
@nl
type
label
Activation of PRK1 by phosphat ...... with protein kinase C isotypes
@ast
Activation of PRK1 by phosphat ...... with protein kinase C isotypes
@en
Activation of PRK1 by phosphat ...... with protein kinase C isotypes
@nl
prefLabel
Activation of PRK1 by phosphat ...... with protein kinase C isotypes
@ast
Activation of PRK1 by phosphat ...... with protein kinase C isotypes
@en
Activation of PRK1 by phosphat ...... with protein kinase C isotypes
@nl
P2093
P2860
P356
P1476
Activation of PRK1 by phosphat ...... with protein kinase C isotypes
@en
P2093
J. A. Le Good
L. V. Dekker
P. J. Parker
R. H. Palmer
R. Woscholski
P2860
P304
22412–22416
P356
10.1074/JBC.270.38.22412
P407
P577
1995-09-22T00:00:00Z