期刊
BIOCHEMISTRY
卷 44, 期 18, 页码 6867-6876出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi0500776
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资金
- NIGMS NIH HHS [GM069945] Funding Source: Medline
Previous studies suggested that heavy chain phosphorylation regulates non-muscle myosin-11 assembly in an isoform-specific manner, affecting the assembly of myosin-IIB, but not myosin-IIA. We re-examined the effects of heavy chain phosphorylation on myosin-IIA filament formation and also examined mts1 binding. We demonstrated that heavy chain phosphorylation by either protein kinase C (PKC) or casein kinase 2 (CK2) inhibits the assembly of myosin-IIA into filaments. PKC phosphorylation had no affect on ruts I binding, but CK2 phosphorylation decreased the affinity of mts I for the myosin-IIA rod by approximately 6.5-fold. Mts1 destabilized PKC-phosphorylated myosin-IIA filaments and inhibited the assembly of myosin-IIA monomers with maximal inhibition of assembly and promotion of disassembly occurring at a molar ratio of one mts] dimer per myosin-IIA rod. At this molar ratio, mts] only weakly disassembled CK2-phosphorylated myosin-IIA filaments and weakly inhibited the assembly of CK2-phosphorylated myosin-IIA monomers. These observations demonstrate that CK2 phosphorylation of the myosin-IIA heavy chain protects against mts1-induced filament disassembly and inhibition of assembly, and suggest that heavy chain phosphorylation provides an additional level of regulation for the mts1-myosin-IIA interaction.
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