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Multiple SH2-mediated interactions in v-src-transformed cells.

C A Koch1, M F Moran, D Anderson

  • 1Division of Molecular and Developmental Biology, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada.

Molecular and Cellular Biology
|March 1, 1992
PubMed
Summary
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The Src homology 2 (SH2) domain directly binds tyrosine-phosphorylated proteins, mediating interactions essential for signaling. This study demonstrates SH2 domains recognize specific phosphorylated targets, crucial for protein-tyrosine kinase function.

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Protein Interactions

Background:

  • The Src homology 2 (SH2) domain is a conserved noncatalytic region in signaling proteins like protein-tyrosine kinases and Ras GTPase-activating protein (GAP).
  • The SH2 domain of p60v-src (v-Src) is critical for v-Src transforming activity and may mediate interactions with tyrosine-phosphorylated proteins.

Purpose of the Study:

  • To investigate the ability of the v-Src SH2 domain to mediate protein-protein interactions.
  • To determine if SH2 domains directly bind to tyrosine-phosphorylated proteins.

Main Methods:

  • Expressed v-Src polypeptides as fusion proteins in Escherichia coli.
  • Analyzed binding of bacterial v-Src SH2 domain to tyrosine-phosphorylated proteins in v-src-transformed Rat-2 cell lysates.

Related Experiment Videos

  • Tested binding of SH2 domains (v-Src, GAP, v-Crk) to denatured and immobilized phosphotyrosine-containing proteins.

    • Main Results:

    • The bacterial v-Src SH2 domain bound tyrosine-phosphorylated p130 and p62 proteins from v-src-transformed Rat-2 cells.
    • In vivo binding of p130 and p62 to v-Src was dependent on the v-Src SH2 domain.
    • SH2 domains of v-Src, GAP, and v-Crk directly recognized immobilized phosphotyrosine proteins, including GAP-associated p190.

    Conclusions:

    • SH2 domains directly bind to tyrosine-phosphorylated proteins.
    • The v-Src SH2 domain can bind phosphorylated targets of the v-Src kinase domain, confirming its role in mediating specific protein interactions.