Illuminating the impact of N-terminal acetylation: from protein to physiology.
review · Level V
Where this comes from
- Record sourced from PubMed, PMID 39814713.
- Also identified by DOI 10.1038/s41467-025-55960-5 and PMC identifier 11735805.
- Licence recorded as CC BY-NC-ND.
- Because redistribution is not established, this page shows the abstract only. Follow the links below for the full text.
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.
Medical subject headings
- Protein Processing, Post-Translational
- Acetyltransferases
- Proteins