The Tensin-3 Protein, Including its SH2 Domain, Is Phosphorylated by Src and Contributes to Tumorigenesis and Metastasis

Xiaolan Qian, Guorong Li, William C. Vass, Alex Papageorge, Renard C. Walker, Laura Asnaghi, Peter J. Steinbach, Giovanna Tosato, Kent Hunter, Douglas R. Lowy

Research output: Contribution to journalArticlepeer-review

Abstract

In cell lines from advanced lung cancer, breast cancer, and melanoma, endogenous tensin-3 contributes to cell migration, anchorage-independent growth, and tumorigenesis. Although SH2 domains have not been reported previously to be phosphorylated, the tensin-3 SH2 domain is a physiologic substrate for Src. Tyrosines in the SH2 domain contribute to the biological activity of tensin-3, and phosphorylation of these tyrosines can regulate ligand binding. In a mouse breast cancer model, tensin-3 tyrosines are phosphorylated in a Src-associated manner in primary tumors, and experimental metastases induced by tumor-derived cell lines depend on endogenous tensin-3. Thus, tensin-3 is implicated as an oncoprotein regulated by Src and possessing an SH2 domain with a previously undescribed mechanism for the regulation of ligand binding.

Original languageEnglish (US)
Pages (from-to)246-258
Number of pages13
JournalCancer cell
Volume16
Issue number3
DOIs
StatePublished - Sep 8 2009

Keywords

  • CELLBIO
  • CELLCYCLE
  • SIGNALING

ASJC Scopus subject areas

  • Oncology
  • Cell Biology
  • Cancer Research

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