Both smooth muscle and nonmuscle myosin II activity is regulated by the phosphorylation state of the myosin regulatory light chain (MLC, MRLC, MLC20, Myl9). Phosphorylation of MLC at Thr-18 and Ser-19 activates myosin II motor activity and increases myosin filament stability. This activation has important roles in various cell motile processes. By contrast, other phosphorylation sites on MLC may inhibit myosin II activity. PKC phosphorylates Ser-1/Ser-2 and Thr-9 in MLC, and this phosphorylation decreases activated myosin II interaction with actin, as well as inhibits MLC interaction with the activation site kinase, myosin light-chain kinase. The Ser-1/Ser-2 region may be the major inhibitory site since Ser-1 is phosphorylated during PDGF-induced stress fiber disassembly and expression of unphosphorylatable MLC20 at the Ser-1/Ser-2 site suppresses this disassembly. Thus, inhibition of myosin II activity through phosphorylation of Ser-1/Ser-2 may have important roles in growth factor-induced reorganization of actomyosin filaments.
Tan, J.L. et al. (1992) Annu. Rev. Biochem. 61:721.
Sellers, J.R. (1991) Curr. Opin. Cell Biol. 3:98.
*For more information, see UniProt Accession P19105
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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