Illuminating the impact of N-terminal acetylation: from protein to physiology

Nina McTiernan (nina.tiernan@uib.no), Ine Kjosås (ine.kjosas@uib.no) and Thomas Arnesen (thomas.arnesen@uib.no)
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Nina McTiernan: University of Bergen
Ine Kjosås: University of Bergen
Thomas Arnesen: University of Bergen

Nature Communications, 2025, vol. 16, issue 1, 1-15

Abstract: Abstract 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.

Date: 2025
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DOI: 10.1038/s41467-025-55960-5

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