Molecular and cellular mechanisms regulating myosin light chain phosphorylation
✍ Scribed by James Stull; Daniel Fitzsimons; Patricia Gallagher; Paul Herring; Kristine Kamm; Da-Chun Tang; Malú Tansey; Ann Word
- Book ID
- 115984541
- Publisher
- Elsevier Science
- Year
- 1992
- Tongue
- English
- Weight
- 95 KB
- Volume
- 24
- Category
- Article
- ISSN
- 0022-2828
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## Abstract The generation of contractile force mediated by actin‐myosin 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
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 k