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Marginal band microtubules are acetylated by alpha TAT1

机译：边缘带微管由αTat1乙酰化

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The discoid shape of resting platelets is maintained by a peripheral, circular bundle of microtubules called marginal band. Marginal band microtubules are acetylated on lysine 40 of the alpha-tubulin subunits. We have previously shown that the deacetylase HDAC6 is responsible for tubulin deacetylation in platelets and that the hyperacetylated state of the microtubules in HDAC6KO platelets correlates with faster activation/spreading kinetics, pointing to a regulatory role of this modification. So far, the question about the reverse enzyme, responsible for tubulin acetylation in platelets, has remained unanswered. Several enzymes have been described as having tubulin acetylation activity. Here we identify alpha TAT1 as the enzyme responsible for the acetylation of marginal band microtubules. We show that alpha TAT1 deficiency has only minor consequences for platelet production and function. A residual tubulin acetylation level in alpha TAT1 deficient platelet lysates suggests the presence of an additional tubulin-acetylating enzyme that is unable to acetylate marginal band microtubules.
机译：静止血小板的盘状形状由一个被称为边缘带的外周环状微管束维持。边缘带微管在α-微管蛋白亚单位的赖氨酸40上乙酰化。我们之前已经证明，去乙酰化酶HDAC6负责血小板中微管蛋白的去乙酰化，HDAC6KO血小板中微管的高乙酰化状态与更快的激活/扩散动力学相关，这表明这种修饰具有调节作用。到目前为止，有关血小板中负责微管蛋白乙酰化的反向酶的问题尚未得到解答。有几种酶被描述为具有微管蛋白乙酰化活性。在这里，我们确定α-TAT1是负责边缘带微管乙酰化的酶。我们发现，α-TAT1缺乏对血小板的生成和功能影响很小。α-TAT1缺陷的血小板裂解物中残留的微管蛋白乙酰化水平表明存在额外的微管蛋白乙酰化酶，该酶不能乙酰化边缘带微管。

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