Illuminating the impact of N-terminal acetylation: from protein to physiology
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...
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2025-01-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-025-55960-5 |
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| _version_ | 1832594553437159424 |
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| author | Nina McTiernan Ine Kjosås Thomas Arnesen |
| author_facet | Nina McTiernan Ine Kjosås Thomas Arnesen |
| author_sort | Nina McTiernan |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-7771aed29dc64e988c840c26cd82ce64 |
| institution | Kabale University |
| issn | 2041-1723 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj-art-7771aed29dc64e988c840c26cd82ce642025-01-19T12:30:43ZengNature PortfolioNature Communications2041-17232025-01-0116111510.1038/s41467-025-55960-5Illuminating the impact of N-terminal acetylation: from protein to physiologyNina McTiernan0Ine Kjosås1Thomas Arnesen2Department of Biomedicine, University of BergenDepartment of Biomedicine, University of BergenDepartment of Biomedicine, University of BergenAbstract 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.https://doi.org/10.1038/s41467-025-55960-5 |
| spellingShingle | Nina McTiernan Ine Kjosås Thomas Arnesen Illuminating the impact of N-terminal acetylation: from protein to physiology Nature Communications |
| title | Illuminating the impact of N-terminal acetylation: from protein to physiology |
| title_full | Illuminating the impact of N-terminal acetylation: from protein to physiology |
| title_fullStr | Illuminating the impact of N-terminal acetylation: from protein to physiology |
| title_full_unstemmed | Illuminating the impact of N-terminal acetylation: from protein to physiology |
| title_short | Illuminating the impact of N-terminal acetylation: from protein to physiology |
| title_sort | illuminating the impact of n terminal acetylation from protein to physiology |
| url | https://doi.org/10.1038/s41467-025-55960-5 |
| work_keys_str_mv | AT ninamctiernan illuminatingtheimpactofnterminalacetylationfromproteintophysiology AT inekjosas illuminatingtheimpactofnterminalacetylationfromproteintophysiology AT thomasarnesen illuminatingtheimpactofnterminalacetylationfromproteintophysiology |