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© The Rockefeller University Press, 0021-9525/2002/2/609 $5.00
The Journal of Cell Biology, Volume 156, Number 4, February 18, 2002 609-615

Force transduction by Triton cytoskeletons

Department of Biological Sciences, Columbia University, New York, NY 10027

Address correspondence to Michael P. Sheetz, Dept. of Biological Sciences, P.O. Box 2408, Columbia University, Sherman Fairchild Center, Rm. 713, 1212 Amsterdam Ave., New York, NY 10027. Tel.: (212) 854-4857. Fax: (212) 854-6399. E-mail: ms2001{at}columbia.edu

Force-initiated signal transduction can occur either via membrane-based ionic mechanisms or through changes in cytoskeletal–matrix linkages. We report here the stretch-dependent binding of cytoplasmic proteins to Triton X-100 cytoskeletons of L-929 cells grown on collagen-coated silicone. Triton X-100–insoluble cytoskeletons were stretched by 10% and incubated with biotinylated cytoplasmic proteins. Analysis with two-dimensional gel electrophoresis showed stretch-dependent binding of more than 10 cytoplasmic protein spots. Bound cytoplasmic proteins were purified by a photocleavable biotin tag and stretch-dependent binding of paxillin, focal adhesion kinase, and p130Cas was found, whereas the binding of vinculin was unchanged and actin binding decreased with stretch. Paxillin binding upon stretch was morphologically and biochemically similar in vitro and in vivo, that is, enhanced in the periphery and inhibited by the tyrosine phosphatase inhibitor, phenylarsine oxide. Thus, we suggest that transduction of matrix forces occurs through force-dependent conformation changes in the integrated cytoskeleton.

Key Words: mechanotransduction; focal contact; cytoskeleton; force; tyrosine phosphatase

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