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Four Things to Know about Myosin Light Chains as Reporters for Non-muscle Myosin-2 Dynamics in Live Cells

机译：关于肌球蛋白轻链作为活细胞中非肌肉肌球蛋白2动态报告基因的四件事

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摘要

The interplay between non-muscle myosins-2 and filamentous actin results in cytoplasmic contractility which is essential for eukaryotic life. Concomitantly, there is tremendous interest in elucidating the physiological function and temporal localization of non-muscle myosin-2 in cells. A commonly used method to study the function and localization of non-muscle myosin-2 is to overexpress a fluorescent protein (FP)-tagged version of the regulatory light chain (RLC) which binds to the myosin-2 heavy chain by mass action. Caveats about this approach include findings from recent studies indicating that the RLC does not bind exclusively to the non-muscle myosin-2 heavy chain. Rather, it can also associate with the myosin heavy chains of several other classes as well as other targets than myosin. In addition, the presence of the FP moiety may compromise myosin's enzymatic and mechanical performance. This and other factors to be discussed in this commentary raise questions about the possible complications in using FP-RLC as a marker for the dynamic localization and regulatory aspects of non-muscle myosin-2 motor functions in cell biological experiments. Published 2015. This article is a U.S. Government work and is in the public domain in the USA.
机译：非肌肉肌球蛋白2和丝状肌动蛋白之间的相互作用会导致胞质收缩，这对于真核生物的生活至关重要。同时，阐明细胞中非肌肉肌球蛋白2的生理功能和时间定位引起了极大的兴趣。研究非肌肉肌球蛋白2的功能和定位的一种常用方法是过表达荧光蛋白（FP）标记的调节轻链（RLC）的形式，该质量轻链与肌球蛋白2重链结合。有关此方法的注意事项包括最近的研究结果，这些结果表明RLC并非仅与非肌肉肌球蛋白2重链结合。而是，它还可以与其他几类的肌球蛋白重链以及肌球蛋白以外的其他靶标结合。另外，FP部分的存在可能损害肌球蛋白的酶和机械性能。此评论中将讨论的这一因素和其他因素提出了有关使用FP-RLC作为细胞生物学实验中非肌肉肌球蛋白2运动功能的动态定位和调控方面的标志物的可能并发症的疑问。 2015年发布。本文是美国政府的工作，在美国属于公共领域。

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