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Identification of a molecular component of the mitochondrial acetyltransferase programme: a novel role for GCN5L1
Open accessAbstract
SIRT3 (sirtuin 3) modulates respiration via the deacetylation of lysine residues in electron transport chain proteins. Whether mitochondrial protein acetylation is controlled by a counter-regulatory program has remained elusive. In the present study we identify an essential component of this previously undefined mitochondrial acetyltransferase system. We show that GCN5L1 [GCN5 (general control of amino acid synthesis 5)-like 1; also known as Bloc1s1] counters the acetylation and respiratory effects of SIRT3. GCN5L1 is mitochondrial-enriched and displays significant homology with a prokaryotic acetyltransferase. Genetic knockdown of GCN5L1 blunts mitochondrial protein acetylation, and its reconstitution in intact mitochondria restores protein acetylation. GCN5L1 interacts with and promotes acetylation of SIRT3 respiratory chain targets and reverses global SIRT3 effects on mitochondrial protein acetylation, respiration and bioenergetics. The results of the present study identify GCN5L1 as a critical prokaryote-derived component of the mitochondrial acetyltransferase programme.
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“GCN5L1 interacts with and promotes acetylation respiratory chain target proteins and reverses global SIRT3 effects on mitochondrial protein acetylation, respiration and bioenergetics ((Scott et al. 2012)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Scott et al. 2012
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“Genetic knockdown of GCN5L1 blunts mitochondrial protein acetylation, and its reconstitution in intact mitochondria restores protein acetylation.”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Scott et al. 2012
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Mammalian Mitochondria and Aging: An Update
Kauppila, T. E. S., Kauppila, J. H. K., & Larsson, N.-G. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2016.09.017 · Cited by 578
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Metadata
- Authors
- Scott, I., Webster, B. R., Li, J. H., & Sack, M. N.
- Affiliations
- National Institutes of Health (US)
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2012-04-16
- Volume
- 443
- Issue
- 3
- Pages
- 655-661
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC7461726
- OpenAlex
- W2040736163
- Cited by
- 214
- References
- 23
- Citations by year
- 2026: 3 · 2025: 11 · 2024: 8 · 2023: 9 · 2022: 13 · 2021: 14 · 2020: 19 · 2019: 18 · 2018: 19 · 2017: 20 · 2016: 19 · 2015: 16 · 2014: 21 · 2013: 17 · 2012: 7
- FWCI
- 9.60
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Biochemical Journal (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Heart, Lung, and Blood Institute (ZIAHL006047)
- NHLBI Division of Intramural Research
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- GCN5L1, SIRT3, mitochondrial protein acetylation, electron transport chain, mitochondrial respiration, lysine acetylation, bioenergetics
- MeSH terms
- Acetylation, Acetyltransferases, Animals, Humans, Mitochondria, Nerve Tissue Proteins, Phylogeny, Oxidative Stress, Immunoprecipitation, Mice, Gene Knockdown Techniques, Sirtuin 3
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