The integrin-actin connection, an eternal love affair

EMBO J. 2003 May 15;22(10):2324-33. doi: 10.1093/emboj/cdg245.

Abstract

Integrin receptors connect the extracellular matrix to the actin cytoskeleton. This interaction can be viewed as a cyclical liaison, which develops again and again at new adhesion sites only to cease at sites of de-adhesion. Recent work has demonstrated that multidomain proteins play crucial roles in the integrin-actin connection by providing a high degree of regulation adjusted to the needs of the cell. In this review we present several examples of this paradigm and with special emphasis on the ILK-PINCH-parvin complex, which amply demonstrates how structural and signalling functions are linked together.

Publication types

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

MeSH terms

  • Actinin / metabolism
  • Actins / metabolism*
  • Adaptor Proteins, Signal Transducing
  • Animals
  • Carrier Proteins / metabolism
  • Cell Adhesion / physiology*
  • Cytoskeleton / metabolism
  • DNA-Binding Proteins / metabolism
  • Extracellular Matrix / metabolism
  • Focal Adhesion Protein-Tyrosine Kinases
  • Integrins / metabolism*
  • Intracellular Signaling Peptides and Proteins*
  • Membrane Proteins*
  • Microfilament Proteins / metabolism
  • Protein Serine-Threonine Kinases / metabolism
  • Protein-Tyrosine Kinases / metabolism
  • Signal Transduction / physiology*

Substances

  • Actins
  • Adaptor Proteins, Signal Transducing
  • Carrier Proteins
  • DNA-Binding Proteins
  • ITGB1BP1 protein, human
  • Integrins
  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins
  • Microfilament Proteins
  • PARVA protein, human
  • PARVB protein, human
  • Actinin
  • integrin-linked kinase
  • Protein-Tyrosine Kinases
  • Focal Adhesion Protein-Tyrosine Kinases
  • Protein Serine-Threonine Kinases