Tensin

Research output: Contribution to journalArticle

137 Scopus citations

Abstract

Tensin is a cytoplasmic phosphoprotein that localized to integrin-mediated focal adhesions. It binds to actin filaments and contains a phosphotyrosine- binding (PTB) domain, which interacts with the cytoplasmic tails of β integrin. These interactions allow tensin to link actin filaments to integrin receptors. In addition, tensin has an Src Homology 2 (SH2) domain capable of interacting with tyrosine-phosphorylated proteins. Furthermore, several factors induce tyrosine phosphorylation of tensin. Thus, tensin functions as a platform for dis/assembly of signaling complexes at focal adhesions by recruiting tyrosine-phosphorylated signaling molecules through the SH2 domain, and also by providing interaction sites for other SH2-containing proteins. Analysis of knockout mice has demonstrated critical roles of tensin in renal function, muscle regeneration, and cell migration. Therefore, tensin and its downstream signaling molecules may be targets for therapeutic interventions in renal disease, wound healing and cancer.

Original languageEnglish (US)
Pages (from-to)31-34
Number of pages4
JournalInternational Journal of Biochemistry and Cell Biology
Volume36
Issue number1
DOIs
StatePublished - Jan 2004

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Keywords

  • Focal adhesion
  • PTB domain
  • SH2 domain
  • Tensin

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology

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