Phosphorylation Primes Vinculin for Activation
| Autor: | Timothy J. Wendorff, Javad Golji, Mohammad R. K. Mofrad |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
Models
Molecular inorganic chemicals animal structures Protein Conformation Biophysics Plasma protein binding macromolecular substances Focal adhesion 03 medical and health sciences Cellular Biophysics and Electrophysiology Computer Simulation Phosphorylation Binding site Actin 030304 developmental biology Vinculin binding 0303 health sciences Binding Sites biology Kinase 030302 biochemistry & molecular biology Vinculin musculoskeletal system Protein Structure Tertiary Cell biology enzymes and coenzymes (carbohydrates) Models Chemical biology.protein Protein Kinases Protein Binding |
| Zdroj: | Biophysical Journal. 102(9):2022-2030 |
| ISSN: | 0006-3495 |
| DOI: | 10.1016/j.bpj.2012.01.062 |
| Popis: | 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 vinculin activation or vinculin binding to actin and PIP2. Simulation of vinculin activation after phosphorylation shows that the added phosphoryl groups can prime vinculin for activation. It remains to be seen if vinculin can be phosphorylated at S1033 in vivo, but these simulations highlight that in the event of a S1033 phophorylation vinculin will likely be primed for activation. |
| Databáze: | OpenAIRE |
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