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Publication : Serine phosphorylation on position 1033 of vinculin impacts cellular mechanics.

First Author  Auernheimer V Year  2014
Journal  Biochem Biophys Res Commun Volume  450
Issue  2 Pages  1095-8
PubMed ID  24996180 Mgi Jnum  J:220142
Mgi Id  MGI:5632279 Doi  10.1016/j.bbrc.2014.06.122
Citation  Auernheimer V, et al. (2014) Serine phosphorylation on position 1033 of vinculin impacts cellular mechanics. Biochem Biophys Res Commun 450(2):1095-8
abstractText  This study evaluates the influence of S1033 vinculin phosphorylation on the mechanical properties of cells. We demonstrate that MEFvcl KO cells transfected with the non-phosphorylatable eGFP-vinculin mutant S1033A are of lower stiffness compared to MEFvcl Rescue and phospho-mimicking mutant S1033D cells, which were of similar stiffness. Analogous, 2D traction microscopy indicates that MEFvcl Rescue and MEF mutant S1033D cells generate similar strain energy, but mutant S1033A cells display approximately 50% less strain energy. Fluorescence recovery after photobleaching demonstrates that the recovery time for mutant S1033A was significantly lower compared to MEFvcl Rescue and mutant S1033D and that the mobile fraction was smaller for MEFvcl Rescue and mutant S1033D than for mutant S1033A cells. This indicates that serine phosphorylation is required for the activation of vinculin and force transmission in focal adhesions.
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