神经丝沿微管的双向转运部分由动力蛋白/动力蛋白激活蛋白介导。
Bidirectional translocation of neurofilaments along microtubules mediated in part by dynein/dynactin.
作者信息
Shah J V, Flanagan L A, Janmey P A, Leterrier J F
机构信息
Harvard-Massachusetts Institute of Technology Division of Health Sciences and Technology, Cambridge, Massachusetts 02139, USA.
出版信息
Mol Biol Cell. 2000 Oct;11(10):3495-508. doi: 10.1091/mbc.11.10.3495.
Neuronal cytoskeletal elements such as neurofilaments, F-actin, and microtubules are actively translocated by an as yet unidentified mechanism. This report describes a novel interaction between neurofilaments and microtubule motor proteins that mediates the translocation of neurofilaments along microtubules in vitro. Native neurofilaments purified from spinal cord are transported along microtubules at rates of 100-1000 nm/s to both plus and minus ends. This motion requires ATP and is partially inhibited by vanadate, consistent with the activity of neurofilament-bound molecular motors. Motility is in part mediated by the dynein/dynactin motor complex and several kinesin-like proteins. This reconstituted motile system suggests how slow net movement of cytoskeletal polymers may be achieved by alternating activities of fast microtubule motors.
神经元细胞骨架成分，如神经丝、F-肌动蛋白和微管，通过一种尚未明确的机制进行主动转运。本报告描述了神经丝与微管运动蛋白之间的一种新型相互作用，该相互作用在体外介导神经丝沿微管的转运。从脊髓中纯化的天然神经丝以100-1000 nm/s的速度沿微管向正端和负端转运。这种运动需要ATP，并被钒酸盐部分抑制，这与神经丝结合的分子马达的活性一致。运动部分由动力蛋白/动力蛋白激活蛋白运动复合体和几种驱动蛋白样蛋白介导。这种重组的运动系统表明，细胞骨架聚合物的缓慢净运动可能是如何通过快速微管马达的交替活动来实现的。
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