Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin
Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin
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DOI：
10.1126/science.1066648
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发表时间：
2002-01-25
期刊：
影响因子：
56.9
通讯作者：
Epstein, HF
中科院分区：
文献类型：
--
作者：
Barral, JM;Hutagalung, AH;Epstein, HF
将肌球蛋白组织成运动细胞结构需要精确的时间和空间调节。含有 UCS (UNC-45/CRO1/She4p) 结构域的蛋白质对于肌球蛋白在胞质分裂过程中掺入收缩环以及在肌肉发育过程中掺入粗丝是必需的。我们报告说，UNC-45 的羧基末端区域与肌球蛋白头部结合并发挥伴侣活性。 UNC-45 的氨基末端四肽重复结构域结合分子伴侣 Hsp90。因此，UNC-45既充当肌球蛋白的分子伴侣，又充当肌球蛋白的Hsp90共伴侣，这可以解释之前在秀丽隐杆线虫UNC-45突变体中组装改变和肌球蛋白积累减少的发现。
The organization of myosin into motile cellular structures requires precise temporal and spatial regulation. Proteins containing a UCS (UNC-45/CRO1/She4p) domain are necessary for the incorporation of myosin into the contractite ring during cytokinesis and into thick filaments during muscle development. We report that the carboxyl-terminal regions of UNC-45 bound and exerted chaperone activity on the myosin head. The amino-terminal tetratricopeptide repeat domain of UNC-45 bound the molecular chaperone Hsp90. Thus, UNC-45 functions both as a molecular chaperone and as an Hsp90 co-chaperone for myosin, which can explain previous findings of altered assembly and decreased accumulation of myosin in UNC-45 mutants of Caenorhabditis elegans.