Catalysis of the microtubule on-rate is the major parameter regulating the depolymerase activity of MCAK.

Catalysis of the microtubule on-rate is the major parameter regulating the depolymerase activity of MCAK.
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DOI:
10.1038/nsmb.1728
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发表时间:
2010-01
影响因子:
16.8
通讯作者:
--
中科院分区:
生物学1区
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运动蛋白13,MCAK,是真核细胞微管动力学的关键调节器。我们从功能上剖析了MCAK强大的微管解聚活性的结构特征。MCAK带正电的颈部增强了其向微管末端的传递,而不是像通常认为的那样,通过在扩散过程中将分子拴在微管上,而是通过催化MCAK与微管的结合。另一方面,这个带正电的颈略微削弱了MCAK在微管末端移除微管蛋白亚基的能力。相反,二聚化减少MCAK的传递,但提高MCAK去除微管蛋白亚基的能力。这些事件的动力学预测了一种非特异性结合机制,可能代表了许多微管结合蛋白的扩散相互作用的范例。
The kinesin-13, MCAK, is a critical regulator of microtubule dynamics in eukaryotic cells. We have functionally dissected the structural features responsible for MCAK’s potent microtubule depolymerization activity. MCAK’s positively charged neck enhances its delivery to microtubule ends, not by tethering the molecule to microtubules during diffusion, as commonly thought, but by catalyzing the association of MCAK to microtubules. On the other hand, this same positively charged neck slightly diminishes MCAK’s ability to remove tubulin subunits once at the microtubule end. Conversely, dimerization reduces MCAK delivery but improves MCAK’s ability to remove tubulin subunits. The reported kinetics for these events predict a non-specific binding mechanism that may represent a paradigm for the diffusive interaction of many microtubule binding proteins.
MCAK通过促进动力学微管营业额来促进染色体运动。
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