## Abstract The generation of contractile force mediated by actinβmyosin interactions is essential for cell motility. Myosin activity is promoted by phosphorylation of myosin light chain (MLC). MLC phosphorylation in large part is controlled by kinases that are effectors of Rho family GTPases. Acco
Regulation of endothelial cell myosin light chain phosphorylation and permeability by vanadate
β Scribed by Lydia I. Gilbert-McClain; Alexander D. Verin; Shu Shi; Robert P. Irwin; Joe G.N. Garcia
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 213 KB
- Volume
- 70
- Category
- Article
- ISSN
- 0730-2312
No coin nor oath required. For personal study only.
β¦ Synopsis
The involvement of tyrosine protein phosphorylation in the regulation of endothelial cell (EC) contraction and barrier function is poorly understood. We have previously shown that myosin light chain (MLC) phosphorylation catalyzed by a novel 214 kDa EC myosin light chain kinase (MLCK) isoform is a key event in EC contraction and barrier dysfunction [Garcia et al.
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