Nonmuscle myosin II is an actin-based motor protein essential to cell motility, cell division, migration, adhesion and polarity. This myosin forms a hexameric complex comprised of two heavy chains (NMHC-II), two essential light chains, and two regulatory light chains (RLC). In vertebrates, there are three NMHC-II isoforms (NMHC-IIA, NMHC-IIB, and NMHC-IIC), which exhibit distinct patterns of expression in cells and tissues. Regulation of NMHC-II activity occurs through RLC and HC phosphorylation. RLCs are phosphorylated at Thr-18 and Ser-19, leading to activation of myosin II motor activity and increased myosin filament stability. By contrast, PKC phosphorylation of Ser-1/Ser-2 and Thr-9 in RLC may decrease activated myosin II interaction with actin. NMHC-II phosphorylation may be an important mode for regulating myosin-II assembly. PKC phosphorylates NMHC-IIA on Ser-1916 in the C-terminal region and NMHC-IIB on multiple serines in the tailpiece. Casein kinase II phosphorylates NMHC-IIA on Ser-1943 in the tailpiece and increases disassembly of NMHC-IIA filaments.
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Dulyaninova, N.G. et al. (2007) Mol Biol Cell 18:3144.
Murakami, N. et al. (1998) Biochemistry 37:1989.
*For more information, see UniProt Accession P35579
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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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