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

Christopher V Carman; Timothy A Springer

doi:10.1016/j.ceb.2003.08.003

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.

Authors

Christopher V Carman¹, Timothy A Springer

Affiliation

¹ Center for Blood Research, Harvard Medical School, Department of Pathology, 200 Longwood Avenue, Boston, MA 02115, USA.

PMID: 14519389
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

Adaptor Proteins, Signal Transducing
Animals
Apoptosis Regulatory Proteins
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

Adaptor Proteins, Signal Transducing
Apoptosis Regulatory Proteins
Integrins
Lymphocyte Function-Associated Antigen-1
Protein Subunits
RASSF5 protein, human
Talin
Monomeric GTP-Binding Proteins
rap1 GTP-Binding Proteins