Documentation and localization of force-mediated filamin A domain perturbations in moving cells

Fumihiko Nakamura (), Mia Song, John H. Hartwig and Thomas P. Stossel
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Fumihiko Nakamura: Brigham and Women’s Hospital, Harvard Medical School
Mia Song: Brigham and Women’s Hospital, Harvard Medical School
John H. Hartwig: Brigham and Women’s Hospital, Harvard Medical School
Thomas P. Stossel: Brigham and Women’s Hospital, Harvard Medical School

Nature Communications, 2014, vol. 5, issue 1, 1-11

Abstract: Abstract Endogenously and externally generated mechanical forces influence diverse cellular activities, a phenomenon defined as mechanotransduction. Deformation of protein domains by application of stress, previously documented to alter macromolecular interactions in vitro, could mediate these effects. We engineered a photon-emitting system responsive to unfolding of two repeat domains of the actin filament (F-actin) crosslinker protein filamin A (FLNA) that binds multiple partners involved in cell signalling reactions and validated the system using F-actin networks subjected to myosin-based contraction. Expressed in cultured cells, the sensor-containing FLNA construct reproducibly reported FLNA domain unfolding strikingly localized to dynamic, actively protruding, leading cell edges. The unfolding signal depends upon coherence of F-actin-FLNA networks and is enhanced by stimulating cell contractility. The results establish protein domain distortion as a bona fide mechanism for mechanotransduction in vivo.

Date: 2014
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DOI: 10.1038/ncomms5656

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