Nicholas Matthew P, Höök Peter, Brenner Sibylle, Wynne Caitlin L, Vallee Richard B, Gennerich Arne
Department of Anatomy and Structural Biology and Gruss-Lipper Biophotonics Center, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Department of Pathology and Cell Biology, Columbia University College of Physicians and Surgeons, New York, New York 10032, USA.
Nat Commun. 2015 Feb 11;6:6206. doi: 10.1038/ncomms7206.
Cytoplasmic dynein is a microtubule motor involved in cargo transport, nuclear migration and cell division. Despite structural conservation of the dynein motor domain from yeast to higher eukaryotes, the extensively studied S. cerevisiae dynein behaves distinctly from mammalian dyneins, which produce far less force and travel over shorter distances. However, isolated reports of yeast-like force production by mammalian dynein have called interspecies differences into question. We report that functional differences between yeast and mammalian dynein are real and attributable to a C-terminal motor element absent in yeast, which resembles a 'cap' over the central pore of the mammalian dynein motor domain. Removal of this cap increases the force generation of rat dynein from 1 pN to a yeast-like 6 pN and greatly increases its travel distance. Our findings identify the CT-cap as a novel regulator of dynein function.
细胞质动力蛋白是一种参与货物运输、核迁移和细胞分裂的微管马达蛋白。尽管从酵母到高等真核生物，动力蛋白马达结构域在结构上具有保守性，但经过广泛研究的酿酒酵母动力蛋白与哺乳动物动力蛋白的行为明显不同，后者产生的力要小得多，移动的距离也更短。然而，关于哺乳动物动力蛋白产生类似酵母的力的个别报道对种间差异提出了质疑。我们报告称，酵母和哺乳动物动力蛋白之间的功能差异是真实存在的，这归因于酵母中不存在的一个C端马达元件，它类似于哺乳动物动力蛋白马达结构域中央孔上的一个“帽”。去除这个帽可将大鼠动力蛋白的力产生从1皮牛增加到类似酵母的6皮牛，并大大增加其移动距离。我们的研究结果确定CT帽是动力蛋白功能的一种新型调节因子。
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