Cytoskeletal protein radixin activates integrin alpha(M)beta(2) by binding to its cytoplasmic tail

FEBS Lett. 2007 Mar 20;581(6):1103-8. doi: 10.1016/j.febslet.2007.02.013. Epub 2007 Feb 15.

Abstract

Talin binding of integrins, via its band 4.1, ezrin, radixin, and moesin (FERM)-homologous domain, directly activates the integrin receptor. However, it is not known whether other FERM-containing proteins also possess such an integrin activating capability. We report here that radixin, one of the original FERM-domain proteins, binds to the membrane-proximal region of the integrin beta(2) but not alpha(M) cytoplasmic tail. Importantly, we show that radixin binding significantly enhances the adhesive activity of integrin alpha(M)beta(2). Given the distinct biological activities of radixin and talin, radixin may represent a novel talin-independent pathway for integrin activation under specific settings.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Binding Sites
  • CHO Cells
  • Cell Adhesion
  • Cricetinae
  • Cricetulus
  • Cytoplasm / chemistry
  • Cytoskeletal Proteins / metabolism*
  • Macrophage-1 Antigen / metabolism*
  • Membrane Proteins / metabolism*
  • Protein Binding
  • Transfection

Substances

  • Cytoskeletal Proteins
  • Macrophage-1 Antigen
  • Membrane Proteins
  • radixin