Titin N2A Domain and Its Interactions at the Sarcomere.

Titin N2A Domain and Its Interactions at the Sarcomere.
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Titin N2A域及其在肌节的相互作用。

DOI:
10.3390/ijms22147563
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发表时间:
2021-07-15
影响因子:
5.6
通讯作者:
Ahn YH
Ahn YH
中科院分区:
生物学2区
文献类型:
--
作者:
Adewale AO;Ahn YH

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肌联蛋白是肌节中的一种巨大蛋白质,与肌动蛋白和肌球蛋白丝一起在肌肉收缩中起重要作用。然而,它的实用性超出了机械功能,扩展到肌节组织和维护,被动力,机械传感和信号的多功能和复杂的角色。Titin的多种功能部分归因于其大尺寸和与无数蛋白质伴侣相互作用的模块化结构。在肌联蛋白的结构域中,N2 A元件是肌联蛋白的独特片段之一,其有助于肌联蛋白的顺应性、收缩、结构稳定性以及通过与肌动蛋白丝、伴侣蛋白、应力传感蛋白和蛋白酶的蛋白质-蛋白质相互作用的信号传导功能。考虑到N2 A的重要性,本文综述了N2 A的结构构象,其倾向于蛋白质-蛋白质相互作用,以及其多个相互作用的蛋白质伴侣,使肌联蛋白的生物学效应的调制。最后,N2 A与分子伴侣和蛋白酶相互作用的性质包括在内,将其作为影响肌联蛋白结构和功能完整性的重要节点。
Titin is a giant protein in the sarcomere that plays an essential role in muscle contraction with actin and myosin filaments. However, its utility goes beyond mechanical functions, extending to versatile and complex roles in sarcomere organization and maintenance, passive force, mechanosensing, and signaling. Titin’s multiple functions are in part attributed to its large size and modular structures that interact with a myriad of protein partners. Among titin’s domains, the N2A element is one of titin’s unique segments that contributes to titin’s functions in compliance, contraction, structural stability, and signaling via protein–protein interactions with actin filament, chaperones, stress-sensing proteins, and proteases. Considering the significance of N2A, this review highlights structural conformations of N2A, its predisposition for protein–protein interactions, and its multiple interacting protein partners that allow the modulation of titin’s biological effects. Lastly, the nature of N2A for interactions with chaperones and proteases is included, presenting it as an important node that impacts titin’s structural and functional integrity.
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