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- W2013974345 abstract "Focal adhesion kinase (FAK) is a crucial component of focal adhesion sites, transducing signals between the cytosol and the extracellular matrix. The translocation of FAK to focal adhesion sites and its functional activation by tyrosine phosphorylation leads to the formation of large multi-molecular focal adhesion complexes. The three-dimensional structure of FAK consists of a tyrosine kinase domain and two large non-catalytic regions. The N-terminal FERM domain is involved in auto-inhibition of the kinase by blocking a phosphorylation site (Tyr576/577)[1], and also includes a basic patch for anchoring FAK to membrane-embedded PIP2. The exposure of this phosphorylation site induces the maximum activity of FAK. We tested if mechanical forces as they are present at focal adhesion sites can induce an allosteric switch to an active state of FAK with an exposed phosphorylation site, using Molecular Dynamics simulations of membrane-bound and unbound FAK. We indeed find mechanical forces propagated onto FAK when tethered between the membrane and the cytoskeleton to remove the auto-inhibitory FERM domain from the kinase domain of FAK. We instead observe an only partial FAK activation upon anchoring FAK to the membrane in the absence of mechanical force. The mechano-transduction mechanism of FAK can explain how FAK acts as a force sensor, translating mechanical forces at the focal adhesion site into downstream biochemical signal events including the MAPK pathway. [1] D. Lietha, X. Cai, D.F.J. Ceccarelli, Y. Li, M. D. Schaller and M. J. Eck. Cell, 2007(129), 1177-1187" @default.
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- W2013974345 date "2013-01-01" @default.
- W2013974345 modified "2023-10-18" @default.
- W2013974345 title "Focal Adhesion Kinase as a Cellular Force Sensor" @default.
- W2013974345 doi "https://doi.org/10.1016/j.bpj.2012.11.365" @default.
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