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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >The major α-tubulin K40 acetyltransferase αTAT1 promotes rapid ciliogenesis and efficient mechanosensation
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The major α-tubulin K40 acetyltransferase αTAT1 promotes rapid ciliogenesis and efficient mechanosensation

机译：主要的α-微管蛋白K40乙酰转移酶αTAT1促进快速纤毛发生和有效的机械感觉

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摘要

Long-lived microtubules found in ciliary axonemes, neuronal processes, and migrating cells are marked by α-tubulin acetylation on lysine 40, a modification that takes place inside the microtubule lumen. The physiological importance of microtubule acetylation remains elusive. Here, we identify a BBSome-associated protein that we name αTAT1, with a highly specific α-tubulin K40 acetyltransferase activity and a catalytic preference for microtubules over free tubulin. In mammalian cells, the catalytic activity of αTAT1 is necessary and sufficient for α-tubulin K40 acetylation. Remarkably, αTAT1 is universally and exclusively conserved in ciliated organisms, and is required for the acetylation of axonemal microtubules and for the normal kinetics of primary cilium assembly. In Caenorhabditis elegans, microtubule acetylation is most prominent in touch receptor neurons (TRNs) and MEC-17, a homo-log of αTAT1, and its paralog αTAT-2 are required for a-tubulin acetylation and for two distinct types of touch sensation. Furthermore, in animals lacking MEC-17,αTAT-2, and the sole C. elegans K40α-tubulin MEC-12, touch sensation can be restored by expression of an acetyl-mimic MEC-12[K40Q]. We conclude that αTAT1 is the major and possibly the sole a-tubulin K40 acetyltransferase in mammals and nematodes, and that tubulin acetylation plays a conserved role in several microtubule-based processes.
机译：在睫状轴突，神经元过程和迁移细胞中发现的长寿命微管的特征是赖氨酸40上的α-微管蛋白乙酰化，这是微管腔内部发生的修饰。微管乙酰化的生理重要性仍然难以捉摸。在这里，我们确定了一种BBSome相关蛋白，我们将其命名为αTAT1，它具有高度特异性的α-微管蛋白K40乙酰转移酶活性，并且相对于游离微管蛋白具有微管的催化优先性。在哺乳动物细胞中，αTAT1的催化活性对于α-微管蛋白K40的乙酰化是必要和充分的。值得注意的是，αTAT1在纤毛生物中普遍且唯一地保守，并且是轴突微管的乙酰化和初级纤毛组装的正常动力学所必需的。在秀丽隐杆线虫中，微管乙酰化在触摸受体神经元（TRNs）和MEC-17（αTAT1的同系物）中最突出，而其旁系同源物αTAT-2是α-微管蛋白乙酰化和两种不同类型的触感所必需的。此外，在缺乏MEC-17，αTAT-2和唯一秀丽隐杆线虫K40α-微管蛋白MEC-12的动物中，可以通过表达模拟乙酰的MEC-12 [K40Q]来恢复触感。我们得出的结论是，αTAT1是哺乳动物和线虫中的主要且可能是唯一的α-微管蛋白K40乙酰转移酶，并且微管蛋白的乙酰化作用在几种基于微管的过程中起着保守的作用。

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