Analysis of the binding of the Src homology 2 domain of Csk to tyrosine-phosphorylated proteins in the suppression and mitotic activation of c-Src.

No abstract is available for this paper.

• Publication year

  1994

• Venue

  Proceedings of the National Academy of Sciences of the United States of America

• Publication date

  1994-04-26

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1073/PNAS.91.9.3984PMID 7513429PMCID PMC43707
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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• Stable association of pp60src and pp59fyn with the focal adhesion-associated protein tyrosine kinase, pp125FAK

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• SH3 domains direct cellular localization of signaling molecules.

  1993cited by this paper
• Phosphorylation of Src mutants at Tyr 527 in fibroblasts does not correlate with in vitro phosphorylation by CSK.

  1993cited by this paper
• Constitutive activation of Src family kinases in mouse embryos that lack Csk.

  1993cited by this paper
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  1993cited by this paper
• Myristylation and amino-terminal phosphorylation are required for activation of pp60c-src during mitosis.

  1993cited by this paper
• Myristylation is required for Tyr-527 dephosphorylation and activation of pp60c-src in mitosis

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• SH2 domains recognize specific phosphopeptide sequences.

  1993cited by this paper
• Disruption of the csk gene, encoding a negative regulator of Src family tyrosine kinases, leads to neural tube defects and embryonic lethality in mice.

  1993cited by this paper
• Detection of Src homology 3-binding proteins, including paxillin, in normal and v-Src-transformed Balb/c 3T3 cells.

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  1993cited by this paper
• Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation

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  1992cited by this paper
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  1992cited by this paper
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• pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions.

  1992cited by this paper
• Role of p34cdc2-mediated phosphorylations in two-step activation of pp60c-src during mitosis.

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• Altered tyrosine 527 phosphorylation and mitotic activation of p60c-src

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  1991cited by this paper
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