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Differential binding of pp60c-src and pp60v-src to cytoskeleton is mediated by SH2 and catalytic domains

H Okamura1, M D Resh

  • 1Cell Biology and Genetics Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021.

Oncogene
|August 1, 1994
PubMed

Insights

The SH2 domain mediates cytoskeletal association for Rous sarcoma virus pp60v-src, differing from its cellular homolog pp60c-src. This binding is regulated by the catalytic (SH1) domain, indicating coordinated function.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Virology

Background:

  • Rous sarcoma virus transforming protein pp60v-src and its cellular homolog pp60c-src exhibit distinct oncogenic potential, subcellular localization, and cytoskeletal binding.
  • pp60v-src stably associates with the detergent-insoluble cytoskeletal matrix, unlike pp60c-src.

Purpose of the Study:

  • To identify the specific regions responsible for cytoskeletal association in pp60v-src and pp60c-src.
  • To elucidate the mechanism underlying the differential cytoskeletal binding between pp60v-src and pp60c-src.

Main Methods:

  • Generation of precise deletion and truncation mutants of Src homology (SH) domains within pp60v-src and pp60c-src.
  • Analysis of cytoskeletal association based on crystal and solution structures of SH domains.

Main Results:

  • The SH2 domain, not the SH3 domain, mediates pp60v-src cytoskeletal association via a phosphotyrosine-dependent interaction.
  • Cytoskeletal binding is regulated by the catalytic (SH1) domain; truncating it reduces pp60v-src binding.
  • Removing the catalytic domain from pp60c-src confers cytoskeletal binding similar to pp60v-src.

Conclusions:

  • The SH2 and catalytic domains cooperate to regulate cytoskeletal association in both pp60v-src and pp60c-src.
  • Differential regulation of these domains explains the distinct cytoskeletal binding properties of viral and cellular Src proteins.

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