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SRC substrate surprise

G Steven Martin1

  • 1Department of Molecular and Cell Biology and Cancer Research Laboratory, University of California, Berkeley, Berkeley, CA 94720, USA. gsm@berkeley.edu

Cancer Cell
|September 8, 2009
PubMed

Insights

Tensin-3

Area of Science:

  • Oncology
  • Molecular Biology
  • Cell Signaling

Background:

  • Tensin-3 is implicated in cancer progression.
  • Regulation of tensin-3 activity is crucial for understanding its role in oncogenesis.

Purpose of the Study:

  • To investigate the regulatory mechanisms of tensin-3.
  • To elucidate how Src influences tensin-3 function.

Main Methods:

  • Phosphorylation assays
  • Analysis of SH2 domain function
  • Studies on oncogenic activity

Main Results:

  • Src phosphorylates the SH2 domain of tensin-3.
  • This phosphorylation enhances the oncogenic function of tensin-3.
  • Phosphorylation regulates SH2 ligand binding.

Conclusions:

  • Src-mediated phosphorylation of the tensin-3 SH2 domain is a novel regulatory mechanism.
  • This mechanism contributes to the oncogenic potential of tensin-3.

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