McTiernan Nina, Kjosås Ine, Arnesen Thomas
Department of Biomedicine, University of Bergen, Bergen, Norway.
Department of Surgery, Haukeland University Hospital, Bergen, Norway.
Nat Commun. 2025 Jan 15;16(1):703. doi: 10.1038/s41467-025-55960-5.
N-terminal acetylation is a highly abundant protein modification in eukaryotic cells. This modification is catalysed by N-terminal acetyltransferases acting co- or post-translationally. Here, we review the eukaryotic N-terminal acetylation machinery: the enzymes involved and their substrate specificities. We also provide an overview of the impact of N-terminal acetylation, including its effects on protein folding, subcellular targeting, protein complex formation, and protein turnover. In particular, there may be competition between N-terminal acetyltransferases and other enzymes in defining protein fate. At the organismal level, N-terminal acetylation is highly influential, and its impairment was recently linked to cardiac dysfunction and neurodegenerative diseases.
N 端乙酰化是真核细胞中一种高度丰富的蛋白质修饰。这种修饰由 N 端乙酰转移酶在翻译过程中或翻译后催化。在这里，我们综述了真核生物的 N 端乙酰化机制：所涉及的酶及其底物特异性。我们还概述了 N 端乙酰化的影响，包括其对蛋白质折叠、亚细胞定位、蛋白质复合物形成和蛋白质周转的作用。特别是，在决定蛋白质命运方面，N 端乙酰转移酶和其他酶之间可能存在竞争。在生物体水平上，N 端乙酰化具有高度影响力，最近其功能受损与心脏功能障碍和神经退行性疾病有关。
