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Fibronectin-Dependent Activation Of Camk-Ii Promotes Focal Adhesion Turnover By Inducing Tyrosine Dephosphorylation Of Fak And Paxillin, Charles Easley Iv

Theses and Dissertations

Transient elevations in Ca²⁺ have previously been shown to promote focal adhesion disassembly and cell motility. Yet the targets of these Ca²⁺ transients have not been fully examined. In this study, we demonstrate that CaMK-II, a Ca²⁺/calmodulin dependent protein kinase, is activated in response to β1 integrin engagement with fibronectin to influence fibroblast adhesion and motility. We also show that CaMK-II is dynamically localized to the cell surface using Total Internal Reflection Fluorescence microscopy (TIRFm) and that inhibition of CaMK-II with two mechanistically distinct, membrane permeant inhibitors accelerates spreading on fibronectin, enlarges paxillin-containing focal adhesions and …