K-loop insertion restores microtubule depolymerizing activity of a "neckless" MCAK mutant.
K-loop insertion restores microtubule depolymerizing activity of a "neckless" MCAK mutant.
复制标题
K 环插入恢复了“无颈”MCAK 突变体的微管解聚活性。
DOI：
10.1083/jcb.200205089
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发表时间：
2002-11-25
期刊：
影响因子：
--
通讯作者：
Wordeman L
中科院分区：
文献类型：
--
作者：
Ovechkina Y;Wagenbach M;Wordeman L
与大多数动蛋白不同，有丝分裂着丝粒相关动蛋白(MCAK)不是沿着微管(MTS)表面移位，而是解聚它们。在运动型动蛋白中，特定细胞功能特有的精细结构，如方向性和加工性，受到与ATP水解型运动域相邻的“颈”结构域的控制。尽管MCAK明显缺乏运动性，但它也包含一个颈部区域。我们发现，MCAK颈区高度保守的正电荷残基的缺失和丙氨酸取代显著降低了MT的解聚活性。此外，用带正电的KIF1AK-环或多赖氨酸取代MCAK的颈区可以挽救在无颈MCAK突变体中观察到的MT解聚活性的丧失。我们认为，类似于K环，颈部与微管蛋白COOH末端发生静电相互作用，从而允许MCAK沿MTS表面扩散移位。这种弱结合作用也可能在MCAK诱导的MT解聚过程中起重要作用。
Unlike most kinesins, mitotic centromere–associated kinesin (MCAK) does not translocate along the surface of microtubules (MTs), but instead depolymerizes them. Among the motile kinesins, refinements that are unique for specific cellular functions, such as directionality and processivity, are under the control of a “neck” domain adjacent to the ATP-hydrolyzing motor domain. Despite its apparent lack of motility, MCAK also contains a neck domain. We found that deletions and alanine substitutions of highly conserved positively charged residues in the MCAK neck domain significantly reduced MT depolymerization activity. Furthermore, substitution of MCAK's neck domain with either the positively charged KIF1A K-loop or poly-lysine rescues the loss of MT-depolymerizing activity observed in the neckless MCAK mutant. We propose that the neck, analogously to the K-loop, interacts electrostatically with the tubulin COOH terminus to permit diffusional translocation of MCAK along the surface of MTs. This weak-binding interaction may also play an important role in processivity of MCAK-induced MT depolymerization.
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影响因子：
64.5
作者：
Case, RB;Pierce, DW;Vale, RD
通讯作者：
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影响因子：
5.6
作者：
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作者：
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DOI：
10.1083/jcb.142.3.787
发表时间：
1998-08-10
期刊：
The Journal of cell biology
影响因子：
--
作者：
Maney T;Hunter AW;Wagenbach M;Wordeman L
通讯作者：
Wordeman L
影响因子：
64.5
作者：
Desai, A;Verma, S;Walczak, CE
通讯作者：
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