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
β¦ LIBER β¦
Regulation of myosin light chain phosphorylation by RhoB in neuronal cells
β Scribed by A.-M. Conway; A.B. James; E.M. O'Kane; S. Rakhit; B.J. Morris
- Book ID
- 116981104
- Publisher
- Elsevier Science
- Year
- 2004
- Tongue
- English
- Weight
- 345 KB
- Volume
- 300
- Category
- Article
- ISSN
- 0014-4827
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## 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