The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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
In the citing paper
“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
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
A simple method for displaying the hydropathic character of a protein
Kyte, J., & Doolittle, R. F. (1982) · Journal of Molecular Biology · doi:10.1016/0022-2836(82)90515-0 · Cited by 22,927
A Mitochondrial Protein Compendium Elucidates Complex I Disease Biology
Pagliarini, D. J., Calvo, S. E., Chang, B., Sheth, S. A., Vafai, S. B., Ong, S.-E., Walford, G. A., Sugiana, C., Boneh, A., Chen, W. K., et al. (2008) · Cell · doi:10.1016/j.cell.2008.06.016 · Cited by 1,994
SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation
Hirschey, M. D., Shimazu, T., Goetzman, E., Jing, E., Schwer, B., Lombard, D. B., Grueter, C. A., Harris, C., Biddinger, S., Ilkayeva, O. R., et al. (2010) · Nature · doi:10.1038/nature08778 · Cited by 1,687
Substrate and Functional Diversity of Lysine Acetylation Revealed by a Proteomics Survey
Kim, S. C., Sprung, R., Chen, Y., Xu, Y., Ball, H., Pei, J., Cheng, T., Kho, Y., Xiao, H., Xiao, L., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.026 · Cited by 1,487
A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis
Ahn, B.-H., Kim, H.-S., Song, S., Lee, I. H., Liu, J., Vassilopoulos, A., Deng, C.-X., & Finkel, T. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803790105 · Cited by 1,291
Someya, S., Yu, W., Hallows, W. C., Xu, J., Vann, J. M., Leeuwenburgh, C., Tanokura, M., Denu, J. M., & Prolla, T. A. (2010) · Cell · doi:10.1016/j.cell.2010.10.002 · Cited by 1,150
Tao, R., Coleman, M. C., Pennington, J. D., Ozden, O., Park, S.-H., Jiang, H., Kim, H.-S., Flynn, C. R., Hill, S., Hayes McDonald, W., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.12.013 · Cited by 899
Sirt3 promotes the urea cycle and fatty acid oxidation during dietary restriction
Hallows, W. C., Yu, W., Smith, B. C., Devires, M. K., Ellinger, J. J., Someya, S., Shortreed, M. R., Prolla, T., Markley, J. L., Smith, L. M., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.01.002 · Cited by 389
Expanded Lysine Acetylation Specificity of Gcn5 in Native Complexes
Grant, P. A., Eberharter, A., John, S., Cook, R. G., Turner, B. M., & Workman, J. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.9.5895 · Cited by 383
Starai, V. J., & Escalante‐Semerena, J. C. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.05.010 · Cited by 260
Huang, J.-Y., Hirschey, M. D., Shimazu, T., Ho, L., & Verdin, E. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.12.021 · Cited by 231
SIRT3 is regulated by nutrient excess and modulates hepatic susceptibility to lipotoxicity
Bao, J., Scott, I., Lu, Z., Pang, L., Dimond, C. C., Gius, D., & Sack, M. N. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.07.009 · Cited by 157
Self-citationPopov, K. M., Kedishvili, N. Y., Zhao, Y., Shimomura, Y., Crabb, D. W., & Harris, R. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74354-3 · Cited by 154
Bao, J., Lu, Z., Joseph, J. J., Carabenciov, D., Dimond, C. C., Pang, L., Samsel, L., McCoy, J. P., Leclerc, J., Nguyen, P., et al. (2010) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22531 · Cited by 116
Self-citationLaw, I. K. M., Liu, L., Xu, A., Lam, K. S. L., Vanhoutte, P. M., Che, C., Leung, P. T. Y., & Wang, Y. (2009) · PROTEOMICS · doi:10.1002/pmic.200800738 · Cited by 114
The role of sirtuins in modulating redox stressors
Webster, B. R., Lu, Z., Sack, M. N., & Scott, I. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.10.484 · Cited by 95
Self-citationSIRT3‐dependent deacetylation exacerbates acetaminophen hepatotoxicity
Lu, Z., Bourdi, M., Li, J. H., Aponte, A. M., Chen, Y., Lombard, D. B., Guček, M., Pohl, L. R., & Sack, M. N. (2011) · EMBO Reports · doi:10.1038/embor.2011.121 · Cited by 80
Self-citationLu, Z., Scott, I., Webster, B. R., & Sack, M. N. (2009) · Circulation Research · doi:10.1161/circresaha.109.204974 · Cited by 61
Self-citationChapter 8 Acetylation of Mitochondrial Proteins
Hirschey, M. D., Shimazu, T., Huang, J., & Verdin, E. (2009) · Methods in Enzymology · doi:10.1016/s0076-6879(09)05008-3 · Cited by 55
Bedekovics, T., Gajdos, G. B., Kispál, G., & Isaya, G. (2007) · FEMS Yeast Research · doi:10.1111/j.1567-1364.2007.00296.x · Cited by 29
Margulis, L. (1970) · Journal of Theoretical Biology · doi:10.1016/s0022-5193(70)80023-6 · Cited by 23
lnoue, M., Isomura, M., lkegawa, S., Fujiwara, T., Shin, S. M., Moriya, H., & Nakamura, Y. (2008) · Cytogenetics and Cell Genetics · doi:10.1159/000134324 · Cited by 20
Cloning and structural analysis of the murine GCN5L1 gene
Driessen, C. A. G. G., Winkens, H. J., Kuhlmann, L. D., Janssen, B. P. M., van Vugt, A. H. M., Deutman, A. F., & Janssen, J. J. M. (1997) · Gene · doi:10.1016/s0378-1119(97)00486-1 · Cited by 16
Cited by
Sorted by citations
Functions and mechanisms of non-histone protein acetylation
Narita, T., Weinert, B. T., & Choudhary, C. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0081-3 · Cited by 1,232
Mitochondrial dysfunction in pathophysiology of heart failure
Zhou, B., & Tian, R. (2018) · Journal of Clinical Investigation · doi:10.1172/jci120849 · Cited by 973
The world of protein acetylation
Drazic, A., Myklebust, L. M., Ree, R., & Arnesen, T. (2016) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2016.06.007 · Cited by 847
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
Wagner, G. R., & Payne, R. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.486753 · Cited by 490
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
