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首页> 外文期刊>Journal of Molecular Biology >N-terminal phosphorylation of p60 katanin directly regulates microtubule severing.
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N-terminal phosphorylation of p60 katanin directly regulates microtubule severing.

机译：p60 katanin的N末端磷酸化直接调节微管切断。

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摘要

Proteins of the AAA (ATPases associated with various cellular activities) family often have complex modes of regulation due to their central position in important cellular processes. p60 katanin, an AAA protein that severs and depolymerizes microtubules, is subject to multiple modes of regulation including a phosphorylation in the N-terminal domain involved in mitotic control of severing. Phosphorylation decreases severing activity in Xenopus egg extracts and is involved in controlling spindle length. Here, we show that the evolutionarily divergent N-terminal domains of p60 have maintained hotspots of mitotic kinase regulation. By reconstituting in vitro severing reactions, we show that phosphomimetic modification at amino acid position 131 in Xenopus laevis p60 decreases severing and microtubule-stimulated ATPase activity without affecting the binding affinity of p60 for microtubules. At high concentrations of the phosphomimetic mutant p60, wild-type levels of activity could be observed, indicating a more switch-like threshold of activity that is controlled by regulating oligomerization on the microtubule. This provides a cellular mechanism for high local concentrations of p60, like those found on spindle poles, to maintain severing activity while most of the protein is inhibited. Overall, we have shown that the modular domain architecture of AAA proteins allows for precise control of cellular activities with simple modifications.
机译：AAA（与各种细胞活动相关的ATP酶）家族的蛋白质由于其在重要细胞过程中的核心地位，通常具有复杂的调节模式。 p60 katanin是一种能使微管分裂和解聚的AAA蛋白，它受到多种调节模式的控制，包括参与切断的有丝分裂控制的N末端结构域的磷酸化。磷酸化降低非洲爪蟾卵提取物中的切断活性，并参与控制纺锤体的长度。在这里，我们显示p60在进化上不同的N末端域保持了有丝分裂激酶调控的热点。通过重建体外切断反应，我们表明非洲爪蟾p60氨基酸位置131的磷酸模拟修饰减少了切断和微管刺激的ATPase活性，而不影响p60对微管的结合亲和力。在模拟拟南芥突变体p60的高浓度下，可以观察到野生型的活性水平，这表明可以通过调节微管上的寡聚来控制活性的更接近开关的阈值。像在纺锤极上发现的那样，这为p60的高局部浓度提供了一种细胞机制，以维持切断活性，同时抑制了大多数蛋白质。总的来说，我们已经表明，AAA蛋白的模块化结构域体系结构允许通过简单的修改即可精确控制细胞活性。

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