Phosphorylation primes vinculin for activation.
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ABSTRACT:
SUBMITTER: Golji J
PROVIDER: S-EPMC3341567 | biostudies-literature | 2012 May
REPOSITORIES: biostudies-literature
Publications
Phosphorylation primes vinculin for activation.
Golji Javad J Wendorff Timothy T Mofrad Mohammad R K MR
Biophysical journal 20120501 9
Vinculin phosphorylation has been implicated as a potential mechanism for focal adhesion growth and maturation. Four vinculin residues-Y100, S1033, S1045, and Y1065-are phosphorylated by kinases during focal adhesion maturation. In this study, phosphorylation at each of these residues is simulated using molecular dynamics models. The simulations demonstrate that once each phosphorylated vinculin structure is at equilibrium, significant local conformational changes result that may impact either v ...[more]
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