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Actin's N‐terminal acetyltransferase uncovered

机译：肌动蛋白的N-末端乙酰转移酶未覆盖

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Abstract Humans express six highly conserved actin isoforms, which differ the most at their N‐termini. Actin's N‐terminus undergoes co‐ and post‐translational processing unique among eukaryotic proteins. During translation, the initiator methionine of the two cytoplasmic isoforms is N‐terminally acetylated (Nt‐acetylated) and that of the four muscle isoforms is removed and the exposed cysteine is Nt‐acetylated. Then, an unidentified acetylaminopeptidase post‐translationally removes the Ac‐Met (or Ac‐Cys), and all six isoforms are re‐acetylated at the N‐terminus. Despite the vital importance of actin for cellular processes ranging from cell motility to organelle trafficking and cell division, the mechanism and functional consequences of Nt‐acetylation remained unresolved. Two recent studies significantly advance our understanding of actin Nt‐acetylation. Drazic et al. (2018, Proc Natl Acad Sci U S A, 115, 4399–4404) identify actin's dedicated N‐terminal acetyltransferase (NAA80/NatH), and demonstrate that Nt‐acetylation critically impacts actin assembly in vitro and in cells. NAA80 knockout cells display increased filopodia and lamellipodia formation and accelerated cell motility. In vitro , the absence of Nt‐acetylation leads to a decrease in the rates of filament depolymerization and elongation, including formin‐induced elongation. Goris et al. (2018, Proc Natl Acad Sci U S A, 115, 4405–4410] describe the structure of Drosophila NAA80 in complex with a peptide‐CoA bi‐substrate analog mimicking the N‐terminus of β‐actin. The structure reveals the source of NAA80's specificity for actin's negatively‐charged N‐terminus. Nt‐acetylation neutralizes a positive charge, thus enhancing the overall negative charge of actin's unique N‐terminus. Actin's N‐terminus is exposed in the filament and influences the interactions of many actin‐binding proteins. These advances open the way to understanding the many likely consequences and functional roles of actin Nt‐acetylation.
机译：摘要人类表达了六种高度保守的肌动蛋白同种型，其N-Termini最多不同。 Actin的N-Terminus在真核蛋白质中进行独特的共同和翻译后处理。在翻译期间，两种细胞质同种型的引发剂甲硫氨酸是N-末端乙酰化（NT-乙酰化），并且除去四个肌肉同种型，并且暴露的半胱氨酸是NT-乙酰化的。然后，翻译后的未识别的乙酰氨基肽酶除去交流符合（或AC-Cys），所有六种同种型在N-末端都会重新乙酰化。尽管肌动蛋白对细胞的过程至关重要，但细胞杂志与细胞器贩运和细胞分裂，但NT-乙酰化的机制和功能后果仍未得到解决。最近的两项研究显着推进了我们对肌动蛋白NT-乙酰化的理解。 Drazic等人。 （2018年，PROC NATL ACAD SCI U S，115,4399-4404）识别肌动蛋白的专用N-末端乙酰转移酶（NAA80 / Nath），并证明NT-乙酰化致力于体外和细胞中的肌动蛋白组装。 NAA80敲除细胞显示出增加的箔片和层层胶质瘤形成和加速细胞运动。体外，没有NT-乙酰化导致长丝脱聚和伸长率的降低，包括素蛋白诱导的伸长率。 Goris等人。 （2018年，Proc Natl Acad Sci USA，115,4405-4410描述了果蝇Naa80在复合物中的结构与β-肌动蛋白的n-末端模拟肽-CoA二衬底模拟。该结构揭示了NaA80的特异性来源对于肌动蛋白的带负电的N-末端。NT-乙酰化中和阳性电荷，从而增强actin独特的N-末端的整体负电荷。actin的N-末端暴露在细丝中并影响许多肌动蛋白结合蛋白的相互作用。这些进步开启了理解肌动蛋白NT-乙酰化的许多可能后果和功能作用的方式。

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