Mechanical strain in actin networks regulates FilGAP and integrin binding to filamin A

A. J. Ehrlicher (), F. Nakamura (), J. H. Hartwig, D. A. Weitz and T. P. Stossel
Additional contact information
A. J. Ehrlicher: Brigham and Women’s Hospital, Harvard Medical School
F. Nakamura: Brigham and Women’s Hospital, Harvard Medical School
J. H. Hartwig: Brigham and Women’s Hospital, Harvard Medical School
D. A. Weitz: School of Engineering and Applied Sciences, Harvard University
T. P. Stossel: Brigham and Women’s Hospital, Harvard Medical School

Nature, 2011, vol. 478, issue 7368, 260-263

Abstract: Mechanosensing by the actin cytoskeleton Living cells need to respond to mechanical forces for many essential biological functions. This mechanosensing activity is thought to be a property of the actin cytoskeleton, but no specific mechanisms have yet been identified. In this study, Ehrlicher et al. identify the actin-binding protein filamin A (FLNa) as a central mechanotransduction element. In a minimal reconstituted system, ligand binding to filamin is affected by mechanical forces, causing certain binding partners to dissociate and others to adhere more strongly. This selectivity may provide a direct molecular link between physical forces and biological activity.

Date: 2011
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DOI: 10.1038/nature10430

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