Post‐translational modifications of vertebrate striated muscle myosin heavy chains

IF 2.4 4区生物学 Q4 CELL BIOLOGY

Cytoskeleton Pub Date : 2024-04-08 DOI:10.1002/cm.21857

Paula Nieto Morales, Arianna N. Coons, Amelia J. Koopman, Sonu Patel, P. Bryant Chase, Michelle S. Parvatiyar, Jose R. Pinto

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Abstract

Post‐translational modifications (PTMs) play a crucial role in regulating the function of many sarcomeric proteins, including myosin. Myosins comprise a family of motor proteins that play fundamental roles in cell motility in general and muscle contraction in particular. A myosin molecule consists of two myosin heavy chains (MyHCs) and two pairs of myosin light chains (MLCs); two MLCs are associated with the neck region of each MyHC's N‐terminal head domain, while the two MyHC C‐terminal tails form a coiled‐coil that polymerizes with other MyHCs to form the thick filament backbone. Myosin undergoes extensive PTMs, and dysregulation of these PTMs may lead to abnormal muscle function and contribute to the development of myopathies and cardiovascular disorders. Recent studies have uncovered the significance of PTMs in regulating MyHC function and showed how these PTMs may provide additional modulation of contractile processes. Here, we discuss MyHC PTMs that have been biochemically and/or functionally studied in mammals' and rodents' striated muscle. We have identified hotspots or specific regions in three isoforms of myosin (MYH2, MYH6, and MYH7) where the prevalence of PTMs is more frequent and could potentially play a significant role in fine‐tuning the activity of these proteins.

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脊椎动物横纹肌肌球蛋白重链的翻译后修饰

翻译后修饰（PTM）在调节包括肌球蛋白在内的许多肌球蛋白的功能方面发挥着至关重要的作用。肌球蛋白由运动蛋白家族组成，在细胞运动特别是肌肉收缩中发挥着重要作用。肌球蛋白分子由两条肌球蛋白重链（MyHC）和两对肌球蛋白轻链（MLC）组成；两条 MLC 与每条肌球蛋白重链的 N 端头部结构域的颈部区域相关联，而两条肌球蛋白重链的 C 端尾部则形成一个线圈，与其他肌球蛋白重链聚合形成粗丝骨架。肌球蛋白会发生大量的 PTM，这些 PTM 的失调可能会导致肌肉功能异常，并导致肌病和心血管疾病的发生。最近的研究揭示了 PTMs 在调节 MyHC 功能中的重要作用，并显示了这些 PTMs 如何为收缩过程提供额外的调节。在此，我们将讨论已在哺乳动物和啮齿动物横纹肌中进行生化和/或功能研究的 MyHC PTM。我们在肌球蛋白的三种同工酶（MYH2、MYH6 和 MYH7）中发现了热点或特定区域，在这些区域中，PTMs 的发生更为频繁，并有可能在微调这些蛋白的活性方面发挥重要作用。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Cytoskeleton CELL BIOLOGY-

CiteScore

5.50

自引率

3.40%

发文量

审稿时长

6-12 weeks

期刊介绍： Cytoskeleton focuses on all aspects of cytoskeletal research in healthy and diseased states, spanning genetic and cell biological observations, biochemical, biophysical and structural studies, mathematical modeling and theory. This includes, but is certainly not limited to, classic polymer systems of eukaryotic cells and their structural sites of attachment on membranes and organelles, as well as the bacterial cytoskeleton, the nucleoskeleton, and uncoventional polymer systems with structural/organizational roles. Cytoskeleton is published in 12 issues annually, and special issues will be dedicated to especially-active or newly-emerging areas of cytoskeletal research.