Aksnes Henriette, Ree Rasmus, Arnesen Thomas
Department of Biomedicine, University of Bergen, 5020 Bergen, Norway.
Department of Biomedicine, University of Bergen, 5020 Bergen, Norway.
Mol Cell. 2019 Mar 21;73(6):1097-1114. doi: 10.1016/j.molcel.2019.02.007. Epub 2019 Mar 13.
Recent studies of N-terminal acetylation have identified new N-terminal acetyltransferases (NATs) and expanded the known functions of these enzymes beyond their roles as ribosome-associated co-translational modifiers. For instance, the identification of Golgi- and chloroplast-associated NATs shows that acetylation of N termini also happens post-translationally. In addition, we now appreciate that some NATs are highly specific; for example, a dedicated NAT responsible for post-translational N-terminal acetylation of actin was recently revealed. Other studies have extended NAT function beyond Nt acetylation, including functions as lysine acetyltransferases (KATs) and non-catalytic roles. Finally, emerging studies emphasize the physiological relevance of N-terminal acetylation, including roles in calorie-restriction-induced longevity and pathological α-synuclein aggregation in Parkinson's disease. Combined, the NATs rise as multifunctional proteins, and N-terminal acetylation is gaining recognition as a major cellular regulator.
最近对N端乙酰化的研究发现了新的N端乙酰转移酶（NATs），并扩展了这些酶的已知功能，使其不再局限于作为核糖体相关的共翻译修饰因子。例如，高尔基体和叶绿体相关NATs的鉴定表明，N端的乙酰化也发生在翻译后。此外，我们现在认识到一些NATs具有高度特异性；例如，最近发现了一种专门负责肌动蛋白翻译后N端乙酰化的NAT。其他研究将NAT的功能扩展到N端乙酰化之外，包括作为赖氨酸乙酰转移酶（KATs）的功能和非催化作用。最后，新出现的研究强调了N端乙酰化的生理相关性，包括在热量限制诱导的长寿和帕金森病中病理性α-突触核蛋白聚集方面的作用。综合来看，NATs作为多功能蛋白崭露头角，N端乙酰化也越来越被认为是一种主要的细胞调节因子。
