Functional interaction between c-Src and its mitotic target, Sam 68 (Q24306924)

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M Anafi

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T Pawson

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D Shalloway

Journal of Biological Chemistry

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language of work or name

English

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publication date

28 April 1995

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published in

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volume

270

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issue

17

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page(s)

10120-4

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cites work

Altered phosphorylation and activation of pp60c-src during fibroblast mitosis

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Altered tyrosine 527 phosphorylation and mitotic activation of p60c-src

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Association of p60c-src with polyoma virus middle-T antigen abrogating mitosis-specific activation

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An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis

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A target for Src in mitosis.

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Molecular cloning and nucleic acid binding properties of the GAP-associated tyrosine phosphoprotein p62

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The pre-mRNA binding K protein contains a novel evolutionarily conserved motif

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The KH domain occurs in a diverse set of RNA-binding proteins that include the antiterminator NusA and is probably involved in binding to nucleic acid

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hnRNP proteins and the biogenesis of mRNA

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Selective binding of activated pp60c-src by an immobilized synthetic phosphopeptide modeled on the carboxyl terminus of pp60c-src

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Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites

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Structural basis for the binding of proline-rich peptides to SH3 domains

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Activation of phosphatidylinositol-3' kinase by Src-family kinase SH3 binding to the p85 subunit

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Suppression of c-Src activity by C-terminal Src kinase involves the c-Src SH2 and SH3 domains: analysis with Saccharomyces cerevisiae

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Direct interaction of v-Src with the focal adhesion kinase mediated by the Src SH2 domain

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Binding of the Src SH2 domain to phosphopeptides is determined by residues in both the SH2 domain and the phosphopeptides

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The v-Src SH3 domain binds phosphatidylinositol 3'-kinase

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Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho

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SH2 domains of the p85 alpha subunit of phosphatidylinositol 3-kinase regulate binding to growth factor receptors

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Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases

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Myristylation is required for Tyr-527 dephosphorylation and activation of pp60c-src in mitosis

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Characterization of two 85 kd proteins that associate with receptor tyrosine kinases, middle-T/pp60c-src complexes, and PI3-kinase

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Association of p62, a multifunctional SH2- and SH3-domain-binding protein, with src family tyrosine kinases, Grb2, and phospholipase C gamma-1

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Identification of Src, Fyn, and Lyn SH3-binding proteins: implications for a function of SH3 domains

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CD45 specifically modulates binding of Lck to a phosphopeptide encompassing the negative regulatory tyrosine of Lck.

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inferred from DOI database lookup

7 January 2021

based on heuristic

A mitotic function for Src?

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.17.10120