A two-segment model for thin filament architecture in skeletal muscle

被引：52

作者：

Gokhin, David S. ^{[1
]}

Fowler, Velia M. ^{[1
]}

机构：

[1] Scripps Res Inst, Dept Cell Biol, La Jolla, CA 92037 USA

来源：

NATURE REVIEWS MOLECULAR CELL BIOLOGY | 2013年 / 14卷 / 02期

基金：

美国国家卫生研究院;

关键词：

MYOSIN-ACTIN INTERACTION; CAPPING-PROTEIN-BETA; POINTED ENDS; NEMALINE MYOPATHY; SARCOMERE-LENGTH; TROPOMYOSIN STABILIZES; SARCOPLASMIC-RETICULUM; NEBULIN INTERACTS; STRIATED-MUSCLE; BINDING PROTEIN;

D O I：

10.1038/nrm3510

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Correct specification of myofilament length is essential for efficient skeletal muscle contraction. The length of thin actin filaments can be explained by a novel 'two-segment' model, wherein the thin filaments consist of two concatenated segments, which are of either constant or variable length. This is in contrast to the classic 'nebulin ruler' model, which postulates that thin filaments are uniform structures, the lengths of which are dictated by nebulin. The two-segment model implicates position-specific microregulation of actin dynamics as a general principle underlying actin filament length and stability.

引用

页码：113 / 119

页数：7

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