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Direct binding of F actin to the cytoplasmic domain of the alpha 2 integrin chain in vitroThe transmembrane integrins have been shown to interact with the cytoskeleton via noncovalent binding between cytoplasmic domains (CDs) of integrin beta chains and various actin binding proteins within the focal adhesion complex. Direct or indirect integrin alpha chain CD binding to the actin cytoskeleton has not been reported. We show here that actin, as an abundant constituent of focal adhesion complex proteins isolated from fibroblasts, binds strongly and specifically to alpha 2 CD, but not to alpha 1 CD peptide. Similar specific binding to alpha 2 CD peptide was seen for highly purified F actin, free of putative actin-binding proteins. The bound complex of actin and peptide was visualized directly by coprecipitation, and actin binding was abrogated by removal of a five amino acid sequence from the alpha 2 CD peptide. Our findings may explain the earlier observation that, while integrins alpha 2 beta 1 and alpha 1 beta 1 both bind to collagen, only alpha 2 beta 1 can mediate contraction of extracellular collagen matrices.
Document ID
Document Type
Reprint (Version printed in journal)
External Source(s)
Kieffer, J. D. (Harvard Skin Disease Research Center, Brigham and Women's Hospital Division of Dermatology, Boston, MA 02115, United States)
Plopper, G.
Ingber, D. E.
Hartwig, J. H.
Kupper, T. S.
Date Acquired
August 22, 2013
Publication Date
December 14, 1995
Publication Information
Publication: Biochemical and biophysical research communications
Volume: 217
Issue: 2
ISSN: 0006-291X
Subject Category
Life Sciences (General)
Distribution Limits
Non-NASA Center
NASA Discipline Cell Biology