期刊
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
卷 11, 期 24, 页码 4882-4889出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/b900964g
关键词
-
资金
- NSF IGERT
- National Science Foundation [MCB-0643832]
- Center for Biological and Environmental Nanotechnology [EEC-0118007]
- Welch Foundation [C-1625]
The collective function of motor proteins is known to be important for the directed transport of many intracellular cargos. However, understanding how multiple motors function as a group remains challenging and requires new methods that enable determination of both the exact number of motors participating in motility and their organization on subcellular cargos. Here we present a biosynthetic method that enables exactly two kinesin-1 molecules to be organized on linear scaffolds that separate the motors by a distance of 50 nm. Tracking the motions of these complexes revealed that while two motors produce longer average run lengths than single kinesins, the system effectively behaves as though a single-motor attachment state dominates motility. It is proposed that negative motor interference derived from asynchronous motor stepping and the communication of forces between motors leads to this behavior by promoting the rapid exchange between different microtubule-bound configurations of the assemblies.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据