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首页> 外文期刊>Journal of Molecular Biology >TRPM7 regulates myosin IIA filament stability and protein localization by heavy chain phosphorylation.
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TRPM7 regulates myosin IIA filament stability and protein localization by heavy chain phosphorylation.

机译：TRPM7通过重链磷酸化调节肌球蛋白IIA细丝稳定性和蛋白质定位。

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摘要

Deregulation of myosin II-based contractility contributes to the pathogenesis of human diseases, such as cancer, which underscores the necessity for tight spatial and temporal control of myosin II activity. Recently, we demonstrated that activation of the mammalian alpha-kinase TRPM7 inhibits myosin II-based contractility in a Ca(2+)- and kinase-dependent manner. However, the molecular mechanism is poorly defined. Here, we demonstrate that TRPM7 phosphorylates the COOH-termini of both mouse and human myosin IIA heavy chains--the COOH-terminus being a region that is critical for filament stability. Phosphorylated residues were mapped to Thr1800, Ser1803 and Ser1808. Mutation of these residues to alanine and that to aspartic acid lead to an increase and a decrease, respectively, in myosin IIA incorporation into the actomyosin cytoskeleton and accordingly affect subcellular localization. In conclusion, our data demonstrate that TRPM7 regulates myosin IIA filament stability and localization by phosphorylating a short stretch of amino acids within the alpha-helical tail of the myosin IIA heavy chain.
机译：基于肌球蛋白II的收缩力失调会导致人类疾病（例如癌症）的发病机理，这强调了对肌球蛋白II活性进行严格的时空控制的必要性。最近，我们证明了哺乳动物α激酶TRPM7的激活以Ca（2+）和激酶依赖的方式抑制基于肌球蛋白II的收缩力。但是，分子机制定义不清。在这里，我们证明TRPM7可使小鼠和人肌球蛋白IIA重链的COOH末端磷酸化-COOH末端是一个对灯丝稳定性至关重要的区域。磷酸化的残基定位于Thr1800，Ser1803和Ser1808。这些残基突变为丙氨酸和天冬氨酸突变分别导致肌球蛋白IIA掺入肌动球蛋白细胞骨架中的增加和减少，从而影响亚细胞定位。总之，我们的数据表明TRPM7通过磷酸化肌球蛋白IIA重链的α螺旋尾部中的一小段氨基酸来调节肌球蛋白IIA细丝的稳定性和定位。

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