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DOI	10.1073/pnas.2001892117
	Muscle myosins form folded monomers; dimers; and tetramers during filament polymerization in vitro
	Liu X.; Shu S.; Korn E.D.
发表日期	2020
ISSN	0027-8424
起始页码	15666
结束页码	15672
卷号	117 期号:27
英文摘要	Muscle contraction depends on the cyclical interaction of myosin and actin filaments. Therefore, it is important to understand the mechanisms of polymerization and depolymerization of muscle myosins. Muscle myosin 2 monomers exist in two states: one with a folded tail that interacts with the heads (10S) and one with an unfolded tail (6S). It has been thought that only unfolded monomers assemble into bipolar and side-polar (smooth muscle myosin) filaments. We now show by electron microscopy that, after 4 s of polymerization in vitro in both the presence (smooth muscle myosin) and absence of ATP, skeletal, cardiac, and smooth muscle myosins form tail-folded monomers without tail–head interaction, tail-folded antiparallel dimers, tail-folded antiparallel tetramers, unfolded bipolar tetramers, and small filaments. After 4 h, the myosins form thick bipolar and, for smooth muscle myosin, side-polar filaments. Nonphosphorylated smooth muscle myosin polymerizes in the presence of ATP but with a higher critical concentration than in the absence of ATP and forms only bipolar filaments with bare zones. Partial depolymerization in vitro of nonphosphorylated smooth muscle myosin filaments by the addition of MgATP is the reverse of polymerization. © 2020 National Academy of Sciences. All rights reserved.
英文关键词	Electron microscopy; Muscle myosins; Polymerization
语种	英语
scopus关键词	dimer; monomer; myosin; myosin II; tetramer; myosin; myosin II; animal tissue; Article; cardiac muscle; chicken; depolymerization; electron microscopy; electrophoresis; gizzard; in vitro study; light scattering; nonhuman; polymerization; priority journal; protein interaction; skeletal muscle; smooth muscle; actin filament; animal; chemistry; genetics; phosphorylation; polymerization; protein conformation; protein folding; protein multimerization; protein unfolding; ultrastructure; Actin Cytoskeleton; Animals; Chickens; Microscopy, Electron; Myosin Type II; Myosins; Phosphorylation; Polymerization; Protein Conformation; Protein Folding; Protein Multimerization; Protein Unfolding; Smooth Muscle Myosins
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/160265
作者单位	Liu, X., Laboratory of Cell Biology, Cell and Developmental Biology Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, United States; Shu, S., Laboratory of Cell Biology, Cell and Developmental Biology Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, United States; Korn, E.D., Laboratory of Cell Biology, Cell and Developmental Biology Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, United States
推荐引用方式 GB/T 7714	Liu X.,Shu S.,Korn E.D.. Muscle myosins form folded monomers; dimers; and tetramers during filament polymerization in vitro[J],2020,117(27).
APA	Liu X.,Shu S.,&Korn E.D..(2020).Muscle myosins form folded monomers; dimers; and tetramers during filament polymerization in vitro.Proceedings of the National Academy of Sciences of the United States of America,117(27).
MLA	Liu X.,et al."Muscle myosins form folded monomers; dimers; and tetramers during filament polymerization in vitro".Proceedings of the National Academy of Sciences of the United States of America 117.27(2020).