Functional interaction between c-Src and its mitotic target, Sam 68
about
Comprehensive analysis of interactions between the Src-associated protein in mitosis of 68 kDa and the human Src-homology 3 proteomeA phosphotyrosine displacement mechanism for activation of Src by PTPalphaSik (BRK) phosphorylates Sam68 in the nucleus and negatively regulates its RNA binding abilityAssociation of human DEAD box protein DDX1 with a cleavage stimulation factor involved in 3'-end processing of pre-MRNA.Selective regulation of tumor necrosis factor-induced Erk signaling by Src family kinases and the T cell protein tyrosine phosphataseIdentification of novel SH3 domain ligands for the Src family kinase Hck. Wiskott-Aldrich syndrome protein (WASP), WASP-interacting protein (WIP), and ELMO1Interaction between Sam68 and Src family tyrosine kinases, Fyn and Lck, in T cell receptor signalingStructure-function analysis of Qk1: a lethal point mutation in mouse quaking prevents homodimerization.Sam68 enhances the cytoplasmic utilization of intron-containing RNA and is functionally regulated by the nuclear kinase Sik/BRK.Adhesion signaling by a novel mitotic substrate of src kinasesSelf-association of the single-KH-domain family members Sam68, GRP33, GLD-1, and Qk1: role of the KH domainThe interaction and colocalization of Sam68 with the splicing-associated factor YT521-B in nuclear dots is regulated by the Src family kinase p59(fyn)Characterization of Sam68-like mammalian proteins SLM-1 and SLM-2: SLM-1 is a Src substrate during mitosisSam68 exerts separable effects on cell cycle progression and apoptosisSAM68: Signal Transduction and RNA Metabolism in Human CancerArginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domainsbeta-arrestin1 interacts with the catalytic domain of the tyrosine kinase c-SRC. Role of beta-arrestin1-dependent targeting of c-SRC in receptor endocytosisEvidence for SH3 domain directed binding and phosphorylation of Sam68 by SrcR-Ras contains a proline-rich site that binds to SH3 domains and is required for integrin activation by R-RasFunctional interaction of Sam68 and heterogeneous nuclear ribonucleoprotein KUCS15A, a novel small molecule, SH3 domain-mediated protein-protein interaction blocking drugSpecificity and determinants of Sam68 RNA binding. Implications for the biological function of K homology domainsModification of the E-cadherin-catenin complex in mitotic Madin-Darby canine kidney epithelial cellsSam68 from an immortalised B-cell line associates with a subset of SH3 domainsIdentification of a mouse p21Cdc42/Rac activated kinasep68 Sam is a substrate of the insulin receptor and associates with the SH2 domains of p85 PI3KSam68 associates with the SH3 domains of Grb2 recruiting GAP to the Grb2-SOS complex in insulin receptor signalingThe quaking I-5 protein (QKI-5) has a novel nuclear localization signal and shuttles between the nucleus and the cytoplasmCooperative activation of Src family kinases by SH3 and SH2 ligands.Sam68 is tyrosine phosphorylated and recruited to signalling in peripheral blood mononuclear cells from HIV infected patients.Tr-kit promotes the formation of a multimolecular complex composed by Fyn, PLCgamma1 and Sam68.Mechanisms of HGF/Met signaling to Brk and Sam68 in breast cancer progression.Selected glimpses into the activation and function of Src kinase.Dissociation of FAK/p130(CAS)/c-Src complex during mitosis: role of mitosis-specific serine phosphorylation of FAKHuman protein Sam68 relocalization and interaction with poliovirus RNA polymerase in infected cells.A role for the GSG domain in localizing Sam68 to novel nuclear structures in cancer cell lines.Targeting the RNA-binding protein Sam68 as a treatment for cancer?Role of Sam68 in post-transcriptional gene regulation.Clinical significance of Sam68 expression in endometrial carcinoma.Cleavage of RasGAP and phosphorylation of mitogen-activated protein kinase in the course of coxsackievirus B3 replication.
P2860
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P2860
Functional interaction between c-Src and its mitotic target, Sam 68
description
1995 nî lūn-bûn
@nan
1995 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
name
Functional interaction between c-Src and its mitotic target, Sam 68
@ast
Functional interaction between c-Src and its mitotic target, Sam 68
@en
Functional interaction between c-Src and its mitotic target, Sam 68
@en-gb
Functional interaction between c-Src and its mitotic target, Sam 68
@nl
type
label
Functional interaction between c-Src and its mitotic target, Sam 68
@ast
Functional interaction between c-Src and its mitotic target, Sam 68
@en
Functional interaction between c-Src and its mitotic target, Sam 68
@en-gb
Functional interaction between c-Src and its mitotic target, Sam 68
@nl
prefLabel
Functional interaction between c-Src and its mitotic target, Sam 68
@ast
Functional interaction between c-Src and its mitotic target, Sam 68
@en
Functional interaction between c-Src and its mitotic target, Sam 68
@en-gb
Functional interaction between c-Src and its mitotic target, Sam 68
@nl
P2093
P2860
P356
P1476
Functional interaction between c-Src and its mitotic target, Sam 68
@en
P2093
P2860
P304
P356
10.1074/JBC.270.17.10120
P407
P577
1995-04-28T00:00:00Z