Int J Biochem Cell Biol. 2004 Jan;36(1):31-4. doi: 10.1016/s1357-2725(03)00171-7.


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 beta 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Actins / metabolism
  • Animals
  • Binding Sites
  • Focal Adhesions / metabolism
  • Gene Expression
  • Humans
  • Microfilament Proteins / biosynthesis
  • Microfilament Proteins / chemistry*
  • Microfilament Proteins / genetics
  • Microfilament Proteins / metabolism*
  • Phosphorylation
  • Phosphotyrosine / metabolism
  • Protein Structure, Tertiary
  • Substrate Specificity
  • Tensins
  • Tissue Distribution
  • Tyrosine / metabolism
  • src Homology Domains


  • Actins
  • Microfilament Proteins
  • Tensins
  • Phosphotyrosine
  • Tyrosine