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原肌球蛋白在秀丽隐杆线虫体壁肌肉中作为F-肌动蛋白稳定剂和肌肉收缩调节因子的双重作用。

Dual roles of tropomyosin as an F-actin stabilizer and a regulator of muscle contraction in Caenorhabditis elegans body wall muscle.

作者信息

Yu Robinson, Ono Shoichiro

机构信息

Department of Pathology, Emory University, Atlanta, Georgia 30322, USA.

出版信息

Cell Motil Cytoskeleton. 2006 Nov;63(11):659-72. doi: 10.1002/cm.20152.

DOI:10.1002/cm.20152
PMID:16937397
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1705952/
Abstract

Tropomyosin is a well-characterized regulator of muscle contraction. It also stabilizes actin filaments in a variety of muscle and non-muscle cells. Although these two functions of tropomyosin could have different impacts on actin cytoskeletal organization, their functional relationship has not been studied in the same experimental system. Here, we investigated how tropomyosin stabilizes actin filaments and how this function is influenced by muscle contraction in Caenorhabditis elegans body wall muscle. We confirmed the antagonistic role of tropomyosin against UNC-60B, a muscle-specific ADF/cofilin isoform, in actin filament organization using multiple UNC-60B mutant alleles. Tropomyosin was also antagonistic to UNC-78 (AIP1) in vivo and protected actin filaments from disassembly by UNC-60B and UNC-78 in vitro, suggesting that tropomyosin protects actin filaments from the ADF/cofilin-AIP1 actin disassembly system in muscle cells. A mutation in the myosin heavy chain caused greater reduction in contractility than tropomyosin depletion. However, the myosin mutation showed much weaker suppression of the phenotypes of ADF/cofilin or AIP1 mutants than tropomyosin depletion. These results suggest that muscle contraction has only minor influence on the tropomyosin's protective role against ADF/cofilin and AIP1, and that the two functions of tropomyosin in actin stability and muscle contraction are independent of each other.

摘要

原肌球蛋白是一种已被充分表征的肌肉收缩调节因子。它还能稳定多种肌肉和非肌肉细胞中的肌动蛋白丝。尽管原肌球蛋白的这两种功能可能对肌动蛋白细胞骨架组织有不同影响,但它们的功能关系尚未在同一实验系统中进行研究。在这里,我们研究了原肌球蛋白如何稳定肌动蛋白丝,以及这种功能如何受到秀丽隐杆线虫体壁肌肉中肌肉收缩的影响。我们使用多个UNC-60B突变等位基因,证实了原肌球蛋白在肌动蛋白丝组织中对UNC-60B(一种肌肉特异性ADF/丝切蛋白异构体)的拮抗作用。原肌球蛋白在体内也对UNC-78(AIP1)具有拮抗作用,并在体外保护肌动蛋白丝不被UNC-60B和UNC-78拆解,这表明原肌球蛋白在肌肉细胞中保护肌动蛋白丝免受ADF/丝切蛋白-AIP1肌动蛋白拆解系统的影响。肌球蛋白重链突变导致的收缩力下降比原肌球蛋白缺失更严重。然而,肌球蛋白突变对ADF/丝切蛋白或AIP1突变体表型的抑制作用比原肌球蛋白缺失弱得多。这些结果表明,肌肉收缩对原肌球蛋白针对ADF/丝切蛋白和AIP1的保护作用影响较小,并且原肌球蛋白在肌动蛋白稳定性和肌肉收缩中的两种功能相互独立。

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Zoolog Sci. 2006 Nov;23(11):969-75. doi: 10.2108/zsj.23.969.
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Aip1 and cofilin promote rapid turnover of yeast actin patches and cables: a coordinated mechanism for severing and capping filaments.Aip1和丝切蛋白促进酵母肌动蛋白斑点和肌动蛋白丝束的快速周转:一种切断和封端肌动蛋白丝的协同机制。
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Caenorhabditis elegans kettin, a large immunoglobulin-like repeat protein, binds to filamentous actin and provides mechanical stability to the contractile apparatuses in body wall muscle.秀丽隐杆线虫肌联蛋白是一种大型免疫球蛋白样重复蛋白,它与丝状肌动蛋白结合,并为体壁肌肉中的收缩装置提供机械稳定性。
Mol Biol Cell. 2006 Jun;17(6):2722-34. doi: 10.1091/mbc.e06-02-0114. Epub 2006 Apr 5.
4
Enhancement of actin-depolymerizing factor/cofilin-dependent actin disassembly by actin-interacting protein 1 is required for organized actin filament assembly in the Caenorhabditis elegans body wall muscle.肌动蛋白相互作用蛋白1增强肌动蛋白解聚因子/丝切蛋白依赖性肌动蛋白解聚,这是秀丽隐杆线虫体壁肌肉中有序肌动蛋白丝组装所必需的。
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