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• W2035390295 endingPage "705" @default.
• W2035390295 startingPage "698" @default.
• W2035390295 abstract "Focal adhesion kinase (FAK) is a nonreceptor tyrosine kinase that regulates cell signaling, proliferation, migration, and development. A major mechanism of regulation of FAK activity is an intramolecular autoinhibitory interaction between two of its domains--the catalytic and FERM domains. Upon cell adhesion to the extracellular matrix, FAK is being translocated toward focal adhesion sites and activated. Interactions of FAK with phosphoinositide phosphatidylinsositol-4,5-bis-phosphate (PIP₂) are required to activate FAK. However, the molecular mechanism of the activation remains poorly understood. Recent fluorescence resonance energy transfer experiments revealed a closure of the FERM-kinase interface upon ATP binding, which is reversed upon additional binding of PIP₂. Here, we addressed the allosteric regulation of FAK by performing all-atom molecular-dynamics simulations of a FAK fragment containing the catalytic and FERM domains, and comparing the dynamics in the absence or presence of ATP and PIP₂. As a major conformational change, we observe a closing and opening motion upon ATP and additional PIP₂ binding, respectively, in good agreement with the fluorescence resonance energy transfer experiments. To reveal how the binding of the regulatory PIP₂ to the FERM F2 lobe is transduced to the very distant F1/N-lobe interface, we employed force distribution analysis. We identified a network of mainly charged residue-residue interactions spanning from the PIP₂ binding site to the distant interface between the kinase and FERM domains, comprising candidate residues for mutagenesis to validate the predicted mechanism of FAK activation." @default.
• W2035390295 created "2016-06-24" @default.
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• W2035390295 date "2015-02-01" @default.
• W2035390295 modified "2023-09-25" @default.
• W2035390295 title "Allosteric Regulation of Focal Adhesion Kinase by PIP2 and ATP" @default.
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• W2035390295 doi "https://doi.org/10.1016/j.bpj.2014.11.3454" @default.
• W2035390295 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4317530" @default.
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• W2035390295 hasPublicationYear "2015" @default.
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