A role for Sam68 in cell cycle progression antagonized by a spliced variant within the KH domain
about
Comprehensive analysis of interactions between the Src-associated protein in mitosis of 68 kDa and the human Src-homology 3 proteomeSik (BRK) phosphorylates Sam68 in the nucleus and negatively regulates its RNA binding abilityMCG10, a novel p53 target gene that encodes a KH domain RNA-binding protein, is capable of inducing apoptosis and cell cycle arrest in G(2)-MStress-induced nuclear bodies are sites of accumulation of pre-mRNA processing factorsSelf-association of the single-KH-domain family members Sam68, GRP33, GLD-1, and Qk1: role of the KH domainSam68 exerts separable effects on cell cycle progression and apoptosisSAM68: Signal Transduction and RNA Metabolism in Human CancerCrystal structure of ERA: a GTPase-dependent cell cycle regulator containing an RNA binding motifThe STAR/GSG family protein rSLM-2 regulates the selection of alternative splice sitesAltered localization and activity of the intracellular tyrosine kinase BRK/Sik in prostate tumor cellsRegulation of SRC family kinases in human cancersSpecificity and determinants of Sam68 RNA binding. Implications for the biological function of K homology domainsIdentification of a Torpedo homolog of Sam68 that interacts with the synapse organizing protein rapsynHigh expression level and nuclear localization of Sam68 are associated with progression and poor prognosis in colorectal cancerp68 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 cytoplasmNext-generation insights into regulatory T cells: expression profiling and FoxP3 occupancy in HumanDetection of Brk expression in non-small cell lung cancer: clinicopathological relevance.Sam68 is tyrosine phosphorylated and recruited to signalling in peripheral blood mononuclear cells from HIV infected patients.The distinct capacity of Fyn and Lck to phosphorylate Sam68 in T cells is essentially governed by SH3/SH2-catalytic domain linker interactions.Characterization of G3BPs: tissue specific expression, chromosomal localisation and rasGAP(120) binding studies.Mechanisms of HGF/Met signaling to Brk and Sam68 in breast cancer progression.Selected glimpses into the activation and function of Src kinase.The KH domain of the branchpoint sequence binding protein determines specificity for the pre-mRNA branchpoint sequenceGene regulation at the RNA layer: RNA binding proteins in intercellular signaling networks.Sam68 Mediates the Activation of Insulin and Leptin Signalling in Breast Cancer CellsA 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.SAM68: a downstream target of angiotensin II signaling in vascular smooth muscle cells in genetic hypertension.Protein methylation and stress granules: posttranslational remodeler or innocent bystander?Cell line profiling to improve monoclonal antibody production.Identification of cellular mRNA targets for RNA-binding protein Sam68Oncogenic functions of PTK6 are enhanced by its targeting to plasma membrane but abolished by its targeting to nucleus.Tyrosine phosphorylation of sam68 by breast tumor kinase regulates intranuclear localization and cell cycle progression.The nuclear tyrosine kinase BRK/Sik phosphorylates and inhibits the RNA-binding activities of the Sam68-like mammalian proteins SLM-1 and SLM-2.The RNA binding protein Sam68 is acetylated in tumor cell lines, and its acetylation correlates with enhanced RNA binding activity.An increase in the expression and total activity of endogenous p60(c-Src) in several factor-independent mutants of a human GM-CSF-dependent leukemia cell line (TF-1).Retardation of the G2-M phase progression on gene disruption of RNA binding protein Sam68 in the DT40 cell line.
P2860
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P2860
A role for Sam68 in cell cycle progression antagonized by a spliced variant within the KH domain
description
1997 nî lūn-bûn
@nan
1997 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
name
A role for Sam68 in cell cycle ...... d variant within the KH domain
@ast
A role for Sam68 in cell cycle ...... d variant within the KH domain
@en
A role for Sam68 in cell cycle ...... d variant within the KH domain
@en-gb
A role for Sam68 in cell cycle ...... d variant within the KH domain
@nl
type
label
A role for Sam68 in cell cycle ...... d variant within the KH domain
@ast
A role for Sam68 in cell cycle ...... d variant within the KH domain
@en
A role for Sam68 in cell cycle ...... d variant within the KH domain
@en-gb
A role for Sam68 in cell cycle ...... d variant within the KH domain
@nl
prefLabel
A role for Sam68 in cell cycle ...... d variant within the KH domain
@ast
A role for Sam68 in cell cycle ...... d variant within the KH domain
@en
A role for Sam68 in cell cycle ...... d variant within the KH domain
@en-gb
A role for Sam68 in cell cycle ...... d variant within the KH domain
@nl
P2093
P2860
P3181
P356
P1476
A role for Sam68 in cell cycle ...... d variant within the KH domain
@en
P2093
F Schweighoffer
M Duchesne
P2860
P304
P3181
P356
10.1074/JBC.272.6.3129
P407
P577
1997-02-07T00:00:00Z