The AAA protein spastin possesses two levels of basal ATPase activity.
The AAA protein spastin possesses two levels of basal ATPase activity.
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AAA 蛋白 spastin 具有两个水平的基础 ATP 酶活性。
DOI：
10.1002/1873-3468.13075
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发表时间：
2018
期刊：
影响因子：
3.5
通讯作者：
Wang Chunguang
中科院分区：
文献类型：
--
作者：
Fan Xiangyu;Lin Zhijie;Fan Guanghui;Lu Jing;Hou Yongfei;Habai Gulijiazi;Sun Linyue;Yu Pengpeng;Shen Yuequan;Wen Maorong;Wang Chunguang
AAA ATP酶痉挛素是一种微管切断酶，在包括轴突再生在内的各种细胞事件中发挥重要作用。在此，我们发现痉挛素的基础ATP酶活性受痉挛素浓度的负调控。通过确定痉挛蛋白的晶体结构，我们证明了痉挛蛋白AAA域之间的亚基间相互作用的必要性。在低浓度下，痉挛素微管结合域（MTBD）中的正电荷的中和显著降低ATP酶活性，但ATP水解电位不受影响。这些结果表明，除了AAA结构域，痉挛蛋白的MTBD区域也参与调节ATP酶活性，使得痉挛蛋白原体之间的相互作用比预期的更复杂。
The AAA ATPase spastin is a microtubule‐severing enzyme that plays important roles in various cellular events including axon regeneration. Herein, we found that the basal ATPase activity of spastin is negatively regulated by spastin concentration. By determining a spastin crystal structure, we demonstrate the necessity of intersubunit interactions between spastin AAA domains. Neutralization of the positive charges in the microtubule‐binding domain (MTBD) of spastin dramatically decreases the ATPase activity at low concentration, although the ATP‐hydrolyzing potential is not affected. These results demonstrate that, in addition to the AAA domain, the MTBD region of spastin is also involved in regulating ATPase activity, making interactions between spastin protomers more complicated than expected.