Kinesin's front head is gated by the backward orientation of its neck linker.
Kinesin's front head is gated by the backward orientation of its neck linker.
复制标题
DOI：
10.1016/j.celrep.2015.02.061
复制
发表时间：
2015-03-31
期刊：
影响因子：
8.8
通讯作者：
Yildiz A
中科院分区：
文献类型：
--
作者：
Dogan MY;Can S;Cleary FB;Purde V;Yildiz A
驱动蛋白-1是一个双头马达，其采取进行性8-nm的手-手步骤并将细胞内货物运输到微管的正端。进行性运动需要门控机制来协调两个头部的机械化学循环。驱动蛋白门控涉及颈接头（NL），一种连接头部的短肽，但仍不清楚门控是否由NL方向或张力促进。利用光学捕获技术，我们测量了驱动蛋白单体在不同核苷酸条件和拉伸几何条件下的力依赖性微管释放速率。我们发现，拉NL在向后的方向抑制核苷酸结合和随后的释放从微管。这种抑制与施加在NL上的张力的大小（2-8 pN）无关。我们的研究结果提供的证据表明，驱动蛋白二聚体的前端门控其NL的向后取向，直到后端从微管释放。
Kinesin-1 is a two-headed motor that takes processive 8-nm hand-over-hand steps and transports intracellular cargos towards the plus end of microtubules. Processive motility requires a gating mechanism to coordinate the mechanochemical cycles of the two heads. Kinesin gating involves the neck linker (NL), a short peptide that interconnects the heads, but it remains unclear whether gating is facilitated by the NL orientation or tension. Using optical trapping, we measured the force-dependent microtubule release rate of kinesin monomers under different nucleotide conditions and pulling geometries. We find that pulling NL in the backward direction inhibits nucleotide binding and subsequent release from the microtubule. This inhibition is independent from the magnitude of tension (2–8 pN) exerted on NL. Our results provide evidence that the front head of a kinesin dimer is gated by the backward orientation of its NL until the rear head releases from the microtubule.
登录
查看更多内容
影响因子：
56.9
作者：
Asbury, CL;Fehr, AN;Block, SM
通讯作者：
Block, SM
影响因子：
4.8
作者：
Rosenfeld, SS;Fordyce, PM;Block, SM
通讯作者：
Block, SM
影响因子：
11.4
作者：
Crevel, IMTC;Nyitrai, M;Cross, RA
通讯作者：
Cross, RA
影响因子：
64.8
作者：
通讯作者：
--
影响因子：
64.8
作者：
Rice, S;Lin, AW;Vale, RD
通讯作者：
Vale, RD