N-alpha-acetyltransferase 80 (NAA80) was recently demonstrated to acetylate the N-terminus of actin, with NAA80 knockout cells showing actin cytoskeleton-related phenotypes, such as increased formation of membrane protrusions and accelerated migration. Here we report that NAA80 knockout cells additionally display fragmentation of the Golgi apparatus. We further employed rescue assays to demonstrate that this phenotype is connected to the ability of NAA80 to modify actin. Thus, re-expression of NAA80, which leads to re-establishment of actin's N-terminal acetyl group, rescued the Golgi fragmentation, whereas a catalytic dead NAA80 mutant could neither restore actin Nt-acetylation nor Golgi structure. The Golgi phenotype of NAA80 KO cells was shared by both migrating and non-migrating cells and live-cell imaging indicated increased Golgi dynamics in migrating NAA80 KO cells. Finally, we detected a drastic increase in the amount of F-actin in cells lacking NAA80, suggesting a causal relationship between this effect and the observed re-organization of Golgi structure. The findings further underscore the importance of actin Nt-acetylation and provide novel insight into its cellular roles, suggesting a mechanistic link between actin modification state and Golgi organization.

中文翻译：

---

NAA80对肌动蛋白的N末端乙酰化对于高尔基体结构的完整性至关重要。

N-α-乙酰基转移酶80（NAA80）最近被证明可以乙酰化肌动蛋白的N-末端，NAA80敲除细胞显示肌动蛋白细胞骨架相关的表型，例如增加的膜突起形成和加速的迁移。在这里我们报告NAA80基因敲除细胞还显示高尔基体的碎片。我们进一步采用抢救试验来证明该表型与NAA80修饰肌动蛋白的能力有关。因此，NAA80的重新表达导致肌动蛋白N末端乙酰基的重新建立，挽救了高尔基体片段化，而催化性死亡的NAA80突变体既不能恢复肌动蛋白Nt-乙酰化也不能恢复高尔基体结构。NAA80 KO细胞的高尔基表型由迁移和非迁移细胞共享，活细胞成像表明在迁移的NAA80 KO细胞中高尔基体动力学增加。最后，我们检测到缺乏NAA80的细胞中F-肌动蛋白的数量急剧增加，表明这种效应与观察到的高尔基体重组之间存在因果关系。这些发现进一步强调了肌动蛋白Nt-乙酰化的重要性，并提供了对其细胞作用的新颖见解，表明了肌动蛋白修饰状态与高尔基体之间的机制联系。