Hancock William O
Department of Biomedical Engineering, Pennsylvania State University, University Park, Pennsylvania.
Biophys J. 2016 Mar 29;110(6):1216-25. doi: 10.1016/j.bpj.2016.02.025.
Kinesin-1 serves as a model for understanding fundamentals of motor protein mechanochemistry and for interpreting functional diversity across the kinesin superfamily. Despite sustained work over the last three decades, disagreements remain regarding the events that trigger the two key transitions in the stepping cycle: detachment of the trailing head from the microtubule and binding of the tethered head to the next tubulin binding site. This review describes the conflicting views of these events and highlights recent work that sheds light on these long-standing controversies. It concludes by presenting a consensus kinesin-1 chemomechanical that incorporates recent work, resolves discrepancies, and highlights key questions for future experimental work. It is hoped that this model provides a framework for understanding how diverse kinesins are tuned for their specific cellular roles.
驱动蛋白-1是理解运动蛋白机械化学基本原理以及解释驱动蛋白超家族功能多样性的模型。尽管在过去三十年里进行了持续研究，但对于触发步进循环中两个关键转变的事件仍存在分歧：尾部头部与微管的分离以及束缚头部与下一个微管蛋白结合位点的结合。本综述描述了对这些事件的相互冲突的观点，并强调了最近有助于阐明这些长期争议的研究工作。它通过提出一个整合了近期研究成果、解决了差异并突出了未来实验工作关键问题的驱动蛋白-1化学机械共识模型来得出结论。希望这个模型能为理解各种驱动蛋白如何针对其特定细胞功能进行调节提供一个框架。
