Direct binding of F actin to the cytoplasmic domain of the alpha 2 integrin chain in vitro

Biochem Biophys Res Commun. 1995 Dec 14;217(2):466-74. doi: 10.1006/bbrc.1995.2799.

Abstract

The transmembrane integrins have been shown to interact with the cytoskeleton via noncovalent binding between cytoplasmic domains (CDs) of integrin beta chains and various actin binding proteins within the focal adhesion complex. Direct or indirect integrin alpha chain CD binding to the actin cytoskeleton has not been reported. We show here that actin, as an abundant constituent of focal adhesion complex proteins isolated from fibroblasts, binds strongly and specifically to alpha 2 CD, but not to alpha 1 CD peptide. Similar specific binding to alpha 2 CD peptide was seen for highly purified F actin, free of putative actin-binding proteins. The bound complex of actin and peptide was visualized directly by coprecipitation, and actin binding was abrogated by removal of a five amino acid sequence from the alpha 2 CD peptide. Our findings may explain the earlier observation that, while integrins alpha 2 beta 1 and alpha 1 beta 1 both bind to collagen, only alpha 2 beta 1 can mediate contraction of extracellular collagen matrices.

MeSH terms

  • Actins / metabolism*
  • Amino Acid Sequence
  • Antigens, CD / metabolism*
  • Cell Adhesion
  • Cells, Cultured
  • Cytoplasm / metabolism
  • Gelsolin / metabolism
  • Humans
  • Integrin alpha2
  • Macromolecular Substances
  • Male
  • Molecular Sequence Data
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • Peptides, Cyclic / metabolism
  • Protein Binding

Substances

  • Actins
  • Antigens, CD
  • Gelsolin
  • Integrin alpha2
  • Macromolecular Substances
  • Peptide Fragments
  • Peptides, Cyclic
  • phallacidin