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Gestalt-Binding of tropomyosin on actin during thin filament activation

机译:细丝活化过程中原肌球蛋白与肌动蛋白的格式塔结合

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摘要

Our thesis is that thin filament function can only be fully understood and muscle regulation then elucidated if atomic structures of the thin filament are available to reveal the positions of tropomyosin on actin in all physiological states. After all, it is tropomyosin influenced by troponin that regulates myosin-crossbridge cycling on actin and therefore controls contraction in all muscles. In addition, we maintain that a complete appreciation of thin filament activation also requires that the mechanical properties of tropomyosin itself are recognized and then related to the effect of myosin-association on actin. Taking the Gestalt-binding of tropomyosin into account, coupled with our electron microscopy structures and computational chemistry, we propose a comprehensive mechanism for tropomyosin regulatory movement over the actin filament surface that explains the cooperative muscle activation process. In fact, well-known point mutations of critical amino acids on the actin–tropomyosin binding interface disrupt Gestalt-binding and are associated with a number of inherited myopathies. Moreover, dysregulation of tropomyosin may also be a factor that interferes with the gatekeeping operation of non-muscle tropomyosin in the controlling interactions of a wide variety of cellular actin-binding proteins. The clinical relevance of Gestalt-binding is discussed in articles by the Marston and the Gunning groups in this special journal issue devoted to the impact of tropomyosin on biological systems.
机译:我们的观点是,如果细丝的原子结构可用于揭示在所有生理状态下原肌球蛋白在肌动蛋白上的位置,则只有细丝功能才能被完全理解,然后阐明肌肉调节。毕竟,肌钙蛋白受到肌钙蛋白的影响,从而调节肌动蛋白的肌球蛋白跨桥循环,从而控制所有肌肉的收缩。另外,我们认为,对细丝活化的完全理解还需要识别原肌球蛋白本身的机械性能,然后与肌球蛋白缔合对肌动蛋白的作用有关。考虑到原肌球蛋白的格式塔结合,再加上我们的电子显微镜结构和计算化学,我们为肌动蛋白丝表面上的原肌球蛋白调节运动提出了一个综合机制,解释了协同性肌肉激活过程。实际上,肌动蛋白-原肌球蛋白结合界面上关键氨基酸的众所周知的点突变破坏了格式塔结合,并与许多遗传性肌病有关。而且,原肌球蛋白的失调也可能是在控制多种细胞肌动蛋白结合蛋白相互作用中干扰非肌肉原肌球蛋白的门控操作的因素。 Marston和Gunning小组在本期特刊中针对原肌球蛋白对生物系统的影响的文章中讨论了格式塔结合的临床意义。

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