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Myosin VI: cellular functions and motor properties

机译:肌球蛋白VI:细胞功能和运动特性

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摘要

Myosin VI has been localized in membrane ruffles at the leading edge of cells. at the trans-Golgi network compartment of the Golgi complex and in clathrin-coated pits or vesicles. indicating that it functions in a wide variety of intracellular processes. Myosin VI moves along actin filaments towards their minus end, a which is the opposite direction to all of the other myosins so far studied (to our knowledge). and is therefore thought to have unique properties and functions. To investigate the cellular roles of myosin VI we identified various myosin VI binding partners and are currently characterizing their interactions within the cell. As an alternative approach, we have expressed and purified full-length myosin VI and studied its in vitro properties. Previous studies assumed that myosin VI was a dimer, but our biochemical, biophysical and electron on microscopic studies reveal that myosin VI can exist as a stable monomer. We observed, using an optical tweezers force transducer, that monomeric myosin VI is a non-processive motor which despite a relatively short lever arm, generates a large working stroke of 18 nm. Whether monomer and/or dimer forms of myosin VI exist in cells and their possible functions will be discussed.
机译:肌球蛋白VI已定位在细胞前沿的膜褶中。在高尔基复合体的反高尔基体网络隔室和网格蛋白包被的凹坑或囊泡中。表明它在各种各样的细胞内过程中起作用。肌球蛋白VI沿肌动蛋白丝向负端移动,这与迄今为止研究的所有其他肌球蛋白(据我们所知)相反。因此被认为具有独特的特性和功能。为了研究肌球蛋白VI的细胞作用,我们鉴定了各种肌球蛋白VI结合伴侣,目前正在表征它们在细胞内的相互作用。作为一种替代方法,我们表达并纯化了全长肌球蛋白VI,并研究了其体外特性。以前的研究假定肌球蛋白VI是二聚体,但我们的生化,生物物理和电子显微镜研究表明,肌球蛋白VI可以作为稳定的单体存在。我们使用光镊力传感器观察到,单体肌球蛋白VI是一种非过程性电机,尽管杠杆臂相对较短,但产生的工作行程为18 nm。将讨论细胞中是否存在肌球蛋白VI的单体和/或二聚体形式及其可能的功能。

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