Filamin A mediates interactions between cytoskeletal proteins that control cell adhesion

FEBS Lett. 2011 Jan 3;585(1):18-22. doi: 10.1016/j.febslet.2010.11.033. Epub 2010 Nov 21.

Abstract

Cell adhesion, spreading and migration on extracellular matrices are regulated by complex processes that involve the cytoskeleton and a large array of adhesion receptors, including the β1 integrin. Filamin A is a large, multi-domain, homodimeric actin binding protein that contributes to the mechanical stability of cells and interacts with several proteins that regulate cell adhesion including β1 integrin and several protein kinases. Here we review current data on the structure, mechanical properties and intracellular signaling functions of filamin that regulate cell adhesion. We also consider new data showing that interactions of filamin A with intermediate filaments and protein kinase C enable tight regulation of β1 integrin function and consequently early events in cell adhesion and migration on extracellular matrix proteins.

Publication types

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

MeSH terms

  • Cell Adhesion / physiology
  • Cell Movement / physiology
  • Contractile Proteins / metabolism*
  • Cytoskeletal Proteins / metabolism*
  • Filamins
  • Humans
  • Integrin beta1 / metabolism
  • Microfilament Proteins / metabolism*
  • Models, Biological
  • Protein Binding
  • Protein Kinase C / metabolism
  • Signal Transduction / physiology*

Substances

  • Contractile Proteins
  • Cytoskeletal Proteins
  • Filamins
  • Integrin beta1
  • Microfilament Proteins
  • Protein Kinase C