Feedback of the kinesin-1 neck-linker position on the catalytic site
Feedback of the kinesin-1 neck-linker position on the catalytic site
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DOI：
10.1074/jbc.m508019200
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发表时间：
2006-07-07
影响因子：
4.8
通讯作者：
Woehlke, Guenther
中科院分区：
文献类型：
--
作者：
Hahlen, Katrin;Ebbing, Bettina;Woehlke, Guenther
驱动蛋白-1马达蛋白沿着微管通过一种机制，其中头部以交错的方式循环通过微管结合和未结合状态。头-头协调的一个重要贡献来自颈连接器的作用，该颈连接器在ATP结合后停靠在核心运动结构域上。我们在这里表明，对接的颈部连接器不仅引导微管未结合的头部到下一个微管结合位点，但也信号的头部，它是连接到它的位置。对突变驱动蛋白构建体的交联研究表明，在界面电机核心/停靠颈接头，其中最重要的是一个保守的酪氨酸残基，参与这种反馈。对接的颈连接体的主要作用是降低ADP状态下的微管结合亲和力。
Kinesin-1 motor proteins step along microtubules by a mechanism in which the heads cycle through microtubule-bound and unbound states in an interlaced fashion. An important contribution to head-head coordination arises from the action of the neck-linker that docks onto the core motor domain upon ATP binding. We show here that the docked neck-linker not only guides the microtubule-unbound head to the next microtubule binding site but also signals its position to the head to which it is attached. Cross-linking studies on mutated kinesin constructs reveal that residues at the interface motor core/docked neck-linker, among them most importantly a conserved tyrosine, are involved in this feedback. The primary effect of the docked neck-linker is a reduced microtubule binding affinity in the ADP state.