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The role of focal adhesion anchoring domains of CAS in mechanotransduction

J. Braniš, C. Pataki, M. Spörrer, RC. Gerum, A. Mainka, V. Cermak, WH. Goldmann, B. Fabry, J. Brabek, D. Rosel,

. 2017 ; 7 (-) : 46233. [pub] 20170413

Jazyk angličtina Země Anglie, Velká Británie

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc19001275

CAS is a docking protein, which was shown to act as a mechanosensor in focal adhesions. The unique assembly of structural domains in CAS is important for its function as a mechanosensor. The tension within focal adhesions is transmitted to a stretchable substrate domain of CAS by focal adhesion-targeting of SH3 and CCH domain of CAS, which anchor the CAS protein in focal adhesions. Mechanistic models of the stretching biosensor propose equal roles for both anchoring domains. Using deletion mutants and domain replacements, we have analyzed the relative importance of the focal adhesion anchoring domains on CAS localization and dynamics in focal adhesions as well as on CAS-mediated mechanotransduction. We confirmed the predicted prerequisite of the focal adhesion targeting for CAS-dependent mechanosensing and unraveled the critical importance of CAS SH3 domain in mechanosensing. We further show that CAS localizes to the force transduction layer of focal adhesions and that mechanical stress stabilizes CAS in focal adhesions.

Citace poskytuje Crossref.org

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$a Gerum, Richard C $u Biophysics Group, Department of Physics, University of Erlangen-Nuremberg, Erlangen, Germany.
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$a Goldmann, Wolfgang H $u Biophysics Group, Department of Physics, University of Erlangen-Nuremberg, Erlangen, Germany.
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