Phosphorylation of the Src substrate Sam68 by Cdc2 during mitosis
about
Sik (BRK) phosphorylates Sam68 in the nucleus and negatively regulates its RNA binding abilitySam68 enhances the cytoplasmic utilization of intron-containing RNA and is functionally regulated by the nuclear kinase Sik/BRK.Characterization of Sam68-like mammalian proteins SLM-1 and SLM-2: SLM-1 is a Src substrate during mitosisActopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesionCyclin E and Cdk2 control GLD-1, the mitosis/meiosis decision, and germline stem cells in Caenorhabditis elegansThe STAR/GSG family protein rSLM-2 regulates the selection of alternative splice sitesEvidence for SH3 domain directed binding and phosphorylation of Sam68 by SrcFunctional interaction of Sam68 and heterogeneous nuclear ribonucleoprotein Kp68 Sam is a substrate of the insulin receptor and associates with the SH2 domains of p85 PI3KA role for KH domain proteins (Sam68-like mammalian proteins and quaking proteins) in the post-transcriptional regulation of HIV replication.Selected glimpses into the activation and function of Src kinase.Phosphorylation of the Drosophila melanogaster RNA-binding protein HOW by MAPK/ERK enhances its dimerization and activityEvolutionary Dynamics of GLD-1-mRNA complexes in Caenorhabditis nematodes.Analysis of the interaction between host factor Sam68 and viral elements during foot-and-mouth disease virus infectionsRole of Sam68 in post-transcriptional gene regulation.Structural investigations of the RNA-binding properties of STAR proteins.Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68.The nuclear tyrosine kinase BRK/Sik phosphorylates and inhibits the RNA-binding activities of the Sam68-like mammalian proteins SLM-1 and SLM-2.Retardation of the G2-M phase progression on gene disruption of RNA binding protein Sam68 in the DT40 cell line.A single point mutation in the nuclear localization domain of Sam68 blocks the Rev/RRE-mediated transactivation.The nuclear RNA-binding protein Sam68 translocates to the cytoplasm and associates with the polysomes in mouse spermatocytes.Neoplastic transformation and tumorigenesis associated with sam68 protein deficiency in cultured murine fibroblasts.
P2860
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P2860
Phosphorylation of the Src substrate Sam68 by Cdc2 during mitosis
description
1997 nî lūn-bûn
@nan
1997 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Phosphorylation of the Src substrate Sam68 by Cdc2 during mitosis
@ast
Phosphorylation of the Src substrate Sam68 by Cdc2 during mitosis
@en
Phosphorylation of the Src substrate Sam68 by Cdc2 during mitosis
@nl
type
label
Phosphorylation of the Src substrate Sam68 by Cdc2 during mitosis
@ast
Phosphorylation of the Src substrate Sam68 by Cdc2 during mitosis
@en
Phosphorylation of the Src substrate Sam68 by Cdc2 during mitosis
@nl
prefLabel
Phosphorylation of the Src substrate Sam68 by Cdc2 during mitosis
@ast
Phosphorylation of the Src substrate Sam68 by Cdc2 during mitosis
@en
Phosphorylation of the Src substrate Sam68 by Cdc2 during mitosis
@nl
P2093
P356
P1433
P1476
Phosphorylation of the Src substrate Sam68 by Cdc2 during mitosis
@en
P2093
P2888
P304
P356
10.1038/SJ.ONC.1201289
P407
P577
1997-09-01T00:00:00Z
P5875
P6179
1025983438