期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 283, 期 23, 页码 15611-15618出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M710597200
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资金
- NHLBI NIH HHS [HL073050] Funding Source: Medline
- NIAMS NIH HHS [AR41653] Funding Source: Medline
Smooth muscle contraction is regulated by the phosphorylation of myosin. It is well known that tonic smooth muscles can maintain force with low energy consumption (latch state); however, the molecular mechanism underlying this phenomenon is unresolved. Here we show that single-head phosphorylated smooth myosin (SHPMII) exhibits fast (similar to 24s(-1)) and slow prolonged (similar to 1s(-1)) actin interactions, whereas double-head phosphorylated myosin (DHPMII) predominantly exhibits the fast (similar to 29s(-1)) interaction, suggesting that the phosphorylated head of SHPMII is mechanically as active as that of DHPMII. Both the fast and the slow actin interactions of SHPMII support the positive net mechanical displacement of actin. The actin translocating velocity of SHPMII was much slower than that of DHPMII, which is consistent with the slow actin interaction of SHPMII. We propose that the latch state can be explained by the motor characteristics of SHPMII that is present during the sustained phase of contraction.
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