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

S J Taylor1, M Anafi, T Pawson

  • 1Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853, USA.

The Journal of Biological Chemistry
|April 28, 1995
PubMed
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The Src-associated in mitosis (Sam 68) protein is a key mitotic target of c-Src tyrosine kinase. Specific SH2 and SH3 domain interactions modulate Sam 68

Area of Science:

  • Cellular biology
  • Molecular biology
  • Biochemistry

Background:

  • c-Src tyrosine kinase plays a role in mitotic processes.
  • Sam 68 is a 68-kDa RNA-binding protein found in mitotic cells.

Purpose of the Study:

  • To investigate the mechanism and functional consequences of the interaction between c-Src and Sam 68.
  • To determine how c-Src targets Sam 68 during mitosis.

Main Methods:

  • Analysis of protein-protein interactions using recombinant SH2 and SH3 domains.
  • In vitro binding assays with immobilized poly(U) to assess RNA-binding activity.
  • Examination of Sam 68 phosphorylation by c-Src in mitotic cells.

Main Results:

  • Sam 68 is the predominant substrate and binding partner of overexpressed c-Src in mitotic cells.

Related Experiment Videos

  • Tyrosine-phosphorylated Sam 68 exhibits selective binding to SH2 domains, with varying affinities.
  • Sam 68 binds selectively to SH3 domains, and this binding can be inhibited by specific peptides.
  • c-Src and p85 SH3 domain binding to Sam 68 inhibits its direct binding to poly(U).

    • Conclusions:

    • The interaction between c-Src and Sam 68 is highly specific, mediated by SH2 and SH3 domains.
    • This specific interaction likely modulates the RNA-binding activity of Sam 68 during mitosis.
    • Sam 68 is identified as a significant mitotic target of c-Src.