Functional and structural characterization of the talin F0F1 domain

Biochem Biophys Res Commun. 2010 Jan 1;391(1):159-65. doi: 10.1016/j.bbrc.2009.11.024. Epub 2009 Nov 10.


The globular head domain of talin, a large multi-domain cytoplasmic protein, is required for inside-out activation of the integrins, a family of heterodimeric transmembrane cell adhesion molecules. Talin head contains a FERM domain that is composed of F1, F2, and F3 subdomains. A F0 subdomain is located N-terminus to F1. The F3 contains a canonical phosphotyrosine binding (PTB) fold that directly interacts with the membrane proximal NPxY/F motif in the integrin beta cytoplasmic tail. This interaction is stabilized by the F2 that interacts with the lipid head-groups of the plasma membrane. In comparison to F2 and F3, the properties of the F0F1 remains poorly characterized. Here, we showed that F0F1 is essential for talin-induced activation of integrin alphaLbeta2 (LFA-1). F0F1 has a high content of beta-sheet secondary structure, and it tends to homodimerize that may provide stability against proteolysis and chaotrope induced unfolding.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Line
  • Humans
  • Lymphocyte Function-Associated Antigen-1 / metabolism*
  • Protein Folding
  • Protein Stability
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Talin / chemistry*
  • Talin / genetics
  • Talin / metabolism*


  • Lymphocyte Function-Associated Antigen-1
  • TLN1 protein, human
  • Talin