Hirokawa Nobutaka, Nitta Ryo, Okada Yasushi
Department of Cell Biology and Anatomy, University of Tokyo, Graduate School of Medicine, Bunkyo-ku, Tokyo, Japan.
Nat Rev Mol Cell Biol. 2009 Dec;10(12):877-84. doi: 10.1038/nrm2807.
Most kinesins move processively along microtubules by using energy derived from ATP hydrolysis. Almost all of the intermediate structures of this ATPase reaction cycle have been solved for the monomeric kinesin 3 family motor KIF1A. Based on this structural information, we propose a common mechanism of kinesin motility, focusing on the regulation of kinesin motility through their interaction with microtubules and by their 'neck-linker' region, which connects their motor domain to cargo and kinesin partner heads.
大多数驱动蛋白通过利用ATP水解产生的能量沿微管进行持续移动。驱动蛋白3家族单体马达KIF1A的ATP酶反应循环几乎所有的中间结构都已得到解析。基于这些结构信息，我们提出了一种驱动蛋白运动的通用机制，重点关注通过驱动蛋白与微管的相互作用以及其“颈链”区域（该区域将其马达结构域与货物及驱动蛋白伙伴头部相连）对驱动蛋白运动的调节。
