Regulation of tensin-promoted cell migration by its focal adhesion binding and Src homology domain 2

Huaiyang Chen, Su Hao Lo

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51 Scopus citations


Tensin1 is an actin- and phosphotyrosine-binding protein that localizes to focal adhesions. Recently, we have shown that both tensin1 and a new family member, tensin2, promote cell migration [Chen, Duncan, Bozorgchami and Lo (2002) Proc. Natl. Acad. Sci. U.S.A. 99, 733-738]. Since localization of proteins to particular intracellular compartments often regulates their functions, and Src homology domain 2 may mediate signals related to cell migration, we hypothesize that tensin-mediated cell migration is regulated by the focal adhesion localization and the Src homology domain 2 of tensin. To test this hypothesis, we have analysed the effects of a series of tensin1 mutants on cell migration. Our results have shown that (1) tensin1 contains two focal adhesion-binding sites, (2) the wild-type tensin1 significantly promotes cell migration, (3) mutants with one focal adhesion-binding site do not promote cell migration, (4) the non-focal adhesion localized mutant suppresses cell migration and (5) the mutant that is not able to bind to phosphotyrosine-containing proteins has no effect on cell migration. These results have indicated that focal adhesion localization of tensin1 and the phosphotyrosine-binding activity are two critical factors in regulating tensin-mediated cell migration.

Original languageEnglish (US)
Pages (from-to)1039-1045
Number of pages7
JournalBiochemical Journal
Issue number3
StatePublished - Mar 15 2003


  • Actin binding
  • NPXY sequence
  • Phosphotyrosine binding domain
  • Wound healing

ASJC Scopus subject areas

  • Biochemistry


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