Bhabha Gira, Johnson Graham T, Schroeder Courtney M, Vale Ronald D
Department of Cellular and Molecular Pharmacology and the Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, CA, USA.
Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, San Francisco, CA, USA; California Institute for Quantitative Biosciences (QB3), University of California, San Francisco, CA, USA.
Trends Biochem Sci. 2016 Jan;41(1):94-105. doi: 10.1016/j.tibs.2015.11.004. Epub 2015 Dec 9.
Cytoplasmic dynein, a member of the AAA (ATPases Associated with diverse cellular Activities) family of proteins, drives the processive movement of numerous intracellular cargos towards the minus end of microtubules. Here, we summarize the structural and motile properties of dynein and highlight features that distinguish this motor from kinesin-1 and myosin V, two well-studied transport motors. Integrating information from recent crystal and cryoelectron microscopy structures, as well as high-resolution single-molecule studies, we also discuss models for how dynein biases its movement in one direction along a microtubule track, and present a movie that illustrates these principles.
胞质动力蛋白是与多种细胞活动相关的ATP酶(AAA)蛋白家族的成员,它驱动众多细胞内货物向微管负端进行持续性移动。在这里,我们总结了动力蛋白的结构和运动特性,并强调了该分子马达与驱动蛋白-1和肌球蛋白V这两种研究充分的运输分子马达的不同之处。整合来自近期晶体结构和冷冻电子显微镜结构以及高分辨率单分子研究的信息,我们还讨论了动力蛋白如何沿微管轨道在一个方向上偏向移动的模型,并展示了一部说明这些原理的影片。