Transformation-specific tyrosine phosphorylation of a novel cellular protein in chicken cells expressing oncogenic variants of the avian cellular src gene.
about
Competitive regulation of E-cadherin juxtamembrane domain degradation by p120-catenin binding and Hakai-mediated ubiquitination.The transmembrane receptor protein tyrosine phosphatase DEP1 interacts with p120(ctn)p130Cas mediates the transforming properties of the anaplastic lymphoma kinaseSMAP, an Smg GDS-associating protein having arm repeats and phosphorylated by Src tyrosine kinaseAutocrine CSF-1R activation promotes Src-dependent disruption of mammary epithelial architectureInvolvement of the tyrosine kinase fer in cell adhesionMonoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases.pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions.Molecular features of the viral and cellular Src kinases involved in interactions with the GTPase-activating protein.Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60srcPaxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase.CAS proteins in normal and pathological cell growth controlNuclear localization of the p120(ctn) Armadillo-like catenin is counteracted by a nuclear export signal and by E-cadherin expressionAn SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinaseActivation and association of Stat3 with Src in v-Src-transformed cell linesIdentification of sequences required for the efficient localization of the focal adhesion kinase, pp125FAK, to cellular focal adhesions.The tyrosine kinase substrate p120cas binds directly to E-cadherin but not to the adenomatous polyposis coli protein or alpha-cateninTyrosine phosphorylation regulates the adhesions of ras-transformed breast epitheliaA core function for p120-catenin in cadherin turnoverAssociation of p120, a tyrosine kinase substrate, with E-cadherin/catenin complexesCortactin, an 80/85-kilodalton pp60src substrate, is a filamentous actin-binding protein enriched in the cell cortexA novel role for p120 catenin in E-cadherin functionStructural basis for the autoinhibition of focal adhesion kinaseSelective uncoupling of p120(ctn) from E-cadherin disrupts strong adhesionp120(ctn) acts as an inhibitory regulator of cadherin function in colon carcinoma cellsRegulation of Endothelial Adherens Junctions by Tyrosine PhosphorylationThe molecular effect of metastasis suppressors on Src signaling and tumorigenesis: new therapeutic targetsp120(ctn) binds to the membrane-proximal region of the E-cadherin cytoplasmic domain and is involved in modulation of adhesion activityReceptor protein-tyrosine phosphatase RPTPmu binds to and dephosphorylates the catenin p120(ctn)The protein-tyrosine phosphatase SHP-1 binds to and dephosphorylates p120 cateninProtein phosphatase 2A interacts with the Src kinase substrate p130(CAS)Direct association of protein-tyrosine phosphatase PTP-PEST with paxillinModification of the E-cadherin-catenin complex in mitotic Madin-Darby canine kidney epithelial cellsp120-catenin is a binding partner and substrate for Group B Pak kinasesThe Fes protein-tyrosine kinase phosphorylates a subset of macrophage proteins that are involved in cell adhesion and cell-cell signalingMultiple stimuli induce tyrosine phosphorylation of the Crk-binding sites of paxillinProtein kinase Calpha activates c-Src and induces podosome formation via AFAP-110Tyrosine phosphorylation of p130(cas) by bombesin, lysophosphatidic acid, phorbol esters, and platelet-derived growth factor. Signaling pathways and formation of a p130(cas)-Crk complexp130Cas, a substrate associated with v-Src and v-Crk, localizes to focal adhesions and binds to focal adhesion kinaseSRC catalytic but not scaffolding function is needed for integrin-regulated tyrosine phosphorylation, cell migration, and cell spreading.
P2860
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P2860
Transformation-specific tyrosine phosphorylation of a novel cellular protein in chicken cells expressing oncogenic variants of the avian cellular src gene.
description
1989 nî lūn-bûn
@nan
1989 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Transformation-specific tyrosi ...... f the avian cellular src gene.
@ast
Transformation-specific tyrosi ...... f the avian cellular src gene.
@en
type
label
Transformation-specific tyrosi ...... f the avian cellular src gene.
@ast
Transformation-specific tyrosi ...... f the avian cellular src gene.
@en
prefLabel
Transformation-specific tyrosi ...... f the avian cellular src gene.
@ast
Transformation-specific tyrosi ...... f the avian cellular src gene.
@en
P2093
P2860
P356
P1476
Transformation-specific tyrosi ...... f the avian cellular src gene.
@en
P2093
A B Reynolds
D J Roesel
J T Parsons
S B Kanner
P2860
P304
P356
10.1128/MCB.9.2.629
P407
P577
1989-02-01T00:00:00Z