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Published 3 September 2002. doi:10.1083/jcb.200206011
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© The Rockefeller University Press, 0021-9525/2002/9/833 $5.00
The Journal of Cell Biology, Volume 158, Number 5, September 2, 2002 833-839


Mini-Reviews

Integrin activation takes shape



R.C. Liddington1 and M.H. Ginsberg2

1 Program in Cell Adhesion, The Burnham Institute, La Jolla, CA 92037
2 Division of Vascular Biology, Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037

Address correspondence to Robert C. Liddington, Program in Cell Adhesion, The Burnham Institute, 10901 N. Torrey Pines Rd., La Jolla, CA 92037. Tel.: (858) 646-3136. Fax: (858) 646-3136. E-mail: rlidding{at}burnham.org; or Mark H. Ginsberg, Div. of Vascular Biology, Dept. of Cell Biology, The Scripps Research Institute, VB-2, 10550 N. Torrey Pines Rd., La Jolla, CA 92037. Tel.: (858) 784-7124. Fax: (858) 784-7343. E-mail: ginsberg{at}scripps.edu


Abstract

Integrins are cell surface adhesion receptors that are essential for the development and function of multicellular animals. Here we summarize recent findings on the regulation of integrin affinity for ligand (activation), one mechanism by which cells modulate integrin function. The focus is on the structural basis of integrin activation, the role of the cytoplasmic domain in integrin affinity regulation, and potential mechanisms by which activation signals are propagated from integrin cytoplasmic domains to the extracellular ligand-binding domain.

Key Words: integrin; adhesion; affinity regulation; cytoplasmic domain; transmembrane domain


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