Activation of c-Src in cells bearing v-Crk and its suppression by Csk
about
Csk inhibition of c-Src activity requires both the SH2 and SH3 domains of SrcA novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent mannerc-Abl kinase regulates the protein binding activity of c-CrkIdentification of GIT1/Cat-1 as a substrate molecule of protein tyrosine phosphatase zeta /beta by the yeast substrate-trapping systemOverexpressed Csk tyrosine kinase is localized in focal adhesions, causes reorganization of alpha v beta 5 integrin, and interferes with HeLa cell spreadingA p130Cas tyrosine phosphorylated substrate domain decoy disrupts v-crk signalingStructural basis for the transforming activity of human cancer-related signaling adaptor protein CRKDirect binding of C-terminal region of p130Cas to SH2 and SH3 domains of Src kinaseProtein-tyrosine phosphatase alpha regulates Src family kinases and alters cell-substratum adhesionInteraction between focal adhesion kinase and Crk-associated tyrosine kinase substrate p130CasSHP-2 binds to caveolin-1 and regulates Src activity via competitive inhibition of CSK in response to H2O2 in astrocytesPhosphorylation site dynamics of early T-cell receptor signalingConsensus substrate sequence for protein-tyrosine phosphatase receptor type ZTwo regions with differential growth-modulating activity in the N-terminal domain of ras GTPase-activating protein (p120GAP) src homology and Gly-Ala-Pro-rich regionsSuppression of arthritic bone destruction by adenovirus-mediated csk gene transfer to synoviocytes and osteoclastsSyk activation by the Src-family tyrosine kinase in the B cell receptor signalingCrk adaptor protein-induced phosphorylation of Gab1 on tyrosine 307 via Src is important for organization of focal adhesions and enhanced cell migration.v-Crk activates the phosphoinositide 3-kinase/AKT pathway by utilizing focal adhesion kinase and H-Ras.The intrinsic ability of AFAP-110 to alter actin filament integrity is linked with its ability to also activate cellular tyrosine kinases.v-Crk activates the phosphoinositide 3-kinase/AKT pathway in transformation.The nonreceptor protein-tyrosine kinase CSK complexes directly with the GTPase-activating protein-associated p62 protein in cells expressing v-Src or activated c-Src.Identification and characterization of Batk, a predominantly brain-specific non-receptor protein tyrosine kinase related to Csk.Analysis of the binding of the Src homology 2 domain of Csk to tyrosine-phosphorylated proteins in the suppression and mitotic activation of c-Src.Oncogenes, Protein Tyrosine Kinases, and Signal Transduction.The SH2 domain is required for stable phosphorylation of p56lck at tyrosine 505, the negative regulatory site.Identification and characterization of a high-affinity interaction between v-Crk and tyrosine-phosphorylated paxillin in CT10-transformed fibroblastsRegulation of early events in integrin signaling by protein tyrosine phosphatase SHP-2.Stat3 activation is required for cellular transformation by v-src.Agonist-stimulated cytoskeletal reorganization and signal transduction at focal adhesions in vascular smooth muscle cells require c-Src.A single amino acid substitution in the v-Eyk intracellular domain results in activation of Stat3 and enhances cellular transformation.Transmembrane phosphoprotein Cbp senses cell adhesion signaling mediated by Src family kinase in lipid rafts.Fulvestrant-induced cell death and proteasomal degradation of estrogen receptor α protein in MCF-7 cells require the CSK c-Src tyrosine kinase.Oncogenic tyrosine kinases target Dok-1 for ubiquitin-mediated proteasomal degradation to promote cell transformationControl of lymphopoiesis by p50csk, a regulatory protein tyrosine kinase.v-src transformation of rat embryo fibroblasts. Inefficient conversion to anchorage-independent growth involves heterogeneity of primary culturesSrc-induced activation of inducible T cell kinase (ITK) requires phosphatidylinositol 3-kinase activity and the Pleckstrin homology domain of inducible T cell kinaseRegulation of the SRC family kinases by Csk.Regulation of Btk by Src family tyrosine kinases.Csk enhances insulin-stimulated dephosphorylation of focal adhesion proteins.Tyrosine kinases Lyn and Syk regulate B cell receptor-coupled Ca2+ mobilization through distinct pathways.
P2860
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P2860
Activation of c-Src in cells bearing v-Crk and its suppression by Csk
description
1992 nî lūn-bûn
@nan
1992 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Activation of c-Src in cells bearing v-Crk and its suppression by Csk
@ast
Activation of c-Src in cells bearing v-Crk and its suppression by Csk
@en
type
label
Activation of c-Src in cells bearing v-Crk and its suppression by Csk
@ast
Activation of c-Src in cells bearing v-Crk and its suppression by Csk
@en
prefLabel
Activation of c-Src in cells bearing v-Crk and its suppression by Csk
@ast
Activation of c-Src in cells bearing v-Crk and its suppression by Csk
@en
P2093
P2860
P356
P1476
Activation of c-Src in cells bearing v-Crk and its suppression by Csk
@en
P2093
P2860
P304
P356
10.1128/MCB.12.10.4706
P407
P577
1992-10-01T00:00:00Z