Integrin avidity regulation: are changes in affinity and conformation underemphasized?

Curr Opin Cell Biol. 2003 Oct;15(5):547-56. doi: 10.1016/j.ceb.2003.08.003.

Abstract

Integrins play critical roles in development, wound healing, immunity and cancer. Central to their function is their unique ability to modulate dynamically their adhesiveness through both affinity- and valency-based mechanisms. Recent advances have shed light on the structural basis for affinity regulation and on the signaling mechanisms responsible for both affinity and valency modes of regulation.

Publication types

  • Review

MeSH terms

  • Animals
  • Binding Sites
  • Cell Adhesion*
  • Cell Membrane / metabolism
  • Cell Movement
  • Cell Polarity
  • Humans
  • Integrins / metabolism*
  • Lymphocyte Function-Associated Antigen-1 / metabolism
  • Molecular Conformation
  • Monomeric GTP-Binding Proteins
  • Protein Binding
  • Protein Structure, Tertiary / physiology
  • Protein Subunits / metabolism
  • Signal Transduction*
  • Talin / metabolism
  • rap1 GTP-Binding Proteins / metabolism

Substances

  • Integrins
  • Lymphocyte Function-Associated Antigen-1
  • Protein Subunits
  • RASSF5 protein, human
  • Talin
  • Monomeric GTP-Binding Proteins
  • rap1 GTP-Binding Proteins