The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.
Lysine Glutarylation Is a Protein Posttranslational Modification Regulated by SIRT5
Open accessAbstract
We report the identification and characterization of a five-carbon protein posttranslational modification (PTM) called lysine glutarylation (Kglu). This protein modification was detected by immunoblot and mass spectrometry (MS), and then comprehensively validated by chemical and biochemical methods. We demonstrated that the previously annotated deacetylase, sirtuin 5 (SIRT5), is a lysine deglutarylase. Proteome-wide analysis identified 683 Kglu sites in 191 proteins and showed that Kglu is highly enriched on metabolic enzymes and mitochondrial proteins. We validated carbamoyl phosphate synthase 1 (CPS1), the rate-limiting enzyme in urea cycle, as a glutarylated protein and demonstrated that CPS1 is targeted by SIRT5 for deglutarylation. We further showed that glutarylation suppresses CPS1 enzymatic activity in cell lines, mice, and a model of glutaric acidemia type I disease, the last of which has elevated glutaric acid and glutaryl-CoA. This study expands the landscape of lysine acyl modifications and increases our understanding of the deacylase SIRT5.
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In the citing paper
“This work resulted in the identification of novel modifications targeted by SIRT5: succinylation, malonylation and glutarylation as described in details below ((Du et al. 2011{Zhang, 2011 #16);(Peng et al. 2011);(Tan et al. 2014)}.”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Tan et al. 2014
In the citing paper
“SIRT5 positively regulates CPS1 activity by mediating desuccinylation, deglutarylation and possibly by deacetylation across multiple sites ((Du et al. 2011))((Tan et al. 2014))((Nakagawa et al. 2009)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Tan et al. 2014
In the citing paper
“Mice lacking SIRT5 fail to upregulate CPS1 activity and show elevated blood ammonia under these conditions ((Nakagawa et al. 2009))((Tan et al. 2014)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Tan et al. 2014
In the citing paper
“Moreover, HMGCS2 is also subject to glutarylation and malonylation ((Tan et al. 2014))((Nishida et al. 2015)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Tan et al. 2014
In the citing paper
“Interestingly, lysine 88 is also a target of succinylation and glutarylation ((Rardin, He, et al. 2013))((Tan et al. 2014)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Tan et al. 2014
In the citing paper
“Both MnSOD and the various mitochondrial superoxide sources are acylated ((Rardin, Newman, et al. 2013), (Rardin, He, et al. 2013);(Tan et al. 2014)); MnSOD also carries glutarylation, succinylation, and acetylation at functionally required lysine residues near its active site, K122 in particular bears all three modifications ((Tao et al. 2010)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Tan et al. 2014
In the citing paper
“Mass-spectrometry data has shown that there are an abundance of histone crotonylation sites in all four core histones22,40.”
From Histone deacetylase (HDAC) 1 and 2 complexes regulate both histone acetylation and crotonylation in vivo (2018) · cites this paper as [40]
In the citing paper
“For example, SIRT5 exhibits efficient activity to lysine desuccinylation, demalonylation and glutarylation12-14”
From HDAC8 catalyzes the hydrolysis of long chain fatty acyl lysine (2016) · cites this paper as [14]
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Citations
Cites
Huang, D. W., Sherman, B. T., & Lempicki, R. A. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkn923 · Cited by 14,108 · cited 2×
“Bioinformatic Analyses of Kglu Substrates To identify the possible association of Kglu substrates with cellular functions, we carried out gene ontology (GO) enrichment analysis using DAVID bioinformatics resources (Huang et al., 2009).”
MethodThe metabolic and molecular bases of inherited disease
Chen, Y.-T. (2001) · Medical Entomology and Zoology · Cited by 6,928
Self-citationAMPK: a nutrient and energy sensor that maintains energy homeostasis
Hardie, D. G., Ross, F. A., & Hawley, S. A. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3311 · Cited by 4,602 · cited 1×
“In addition to histones, PTM-regulatory enzymes, such as AMP-activated protein kinase (AMPK) and lysine deacetylases (KDACs or HDACs), can control activity of their substrates (Chalkiadaki and Guarente, 2012; Hardie et al., 2012), many of which are metabolic enzymes.”
BackgroundTranscriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
Imai, S.-I., Armstrong, C. M., Kaeberlein, M., & Guarente, L. (2000) · Nature · doi:10.1038/35001622 · Cited by 3,510 · cited 4×
“For example, acetyl-CoA, SAM, NAD+, and a-ketoglutarate are donors/substrates or cofactors for histone lysine-modifying enzymes, i.e., those modulating levels of acetylation and methylation (Imai et al., 2000; Takahashi et al., 2006; Tsukada et al., 2006; Wellen et al., 2009).”
BackgroundInfluentialThe complex language of chromatin regulation during transcription
Berger, S. L. (2007) · Nature · doi:10.1038/nature05915 · Cited by 2,768 · cited 1×
“These PTM enzymes have important roles in modulation of chromatin structure and transcriptional regulation (Berger, 2007; Chi et al., 2010).”
BackgroundATP-citrate lyase links cellular metabolism to histone acetylation
Wellen, K. E., Hatzivassiliou, G., Sachdeva, U. M., Bui, T. V., Cross, J. R., & Thompson, C. B. (2009) · Science · doi:10.1126/science.1164097 · Cited by 2,298 · cited 2×
“For example, acetyl-CoA, SAM, NAD+, and a-ketoglutarate are donors/substrates or cofactors for histone lysine-modifying enzymes, i.e., those modulating levels of acetylation and methylation (Imai et al., 2000; Takahashi et al., 2006; Tsukada et al., 2006; Wellen et al., 2009).”
BackgroundHistone demethylation by a family of JmjC domain-containing proteins
Tsukada, Y.-I., Fang, J., Erdjument‐Bromage, H., Warren, M., Borchers, C. H., Tempst, P., & Zhang, Y. (2005) · Nature · doi:10.1038/nature04433 · Cited by 2,244 · cited 2×
“For example, acetyl-CoA, SAM, NAD+, and a-ketoglutarate are donors/substrates or cofactors for histone lysine-modifying enzymes, i.e., those modulating levels of acetylation and methylation (Imai et al., 2000; Takahashi et al., 2006; Tsukada et al., 2006; Wellen et al., 2009).”
BackgroundSelf-citationTan, M., Luo, H., Lee, S., Jin, F., Yang, J. S., Montellier, E., Buchou, T., Cheng, Z., Rousseaux, S., Rajagopal, N., et al. (2011) · Cell · doi:10.1016/j.cell.2011.08.008 · Cited by 1,902 · cited 3×
“Our previous studies identified new lysine acylation modifications on histones (Chen et al., 2007; Tan et al., 2011; Xie et al., 2012), including lysine crotonylation and succinylation, revealing potential crosstalk between cellular physiology and gene transcription.”
BackgroundSelf-citationProtein Structure Modeling with MODELLER
Eswar, N., Eramian, D., Webb, B., Shen, M., & Šali, A. (2008) · Methods in molecular biology · doi:10.1007/978-1-60327-058-8_8 · Cited by 1,781
Substrate and Functional Diversity of Lysine Acetylation Revealed by a Proteomics Survey
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“coli and HeLa cells, we used an affinity enrichment-based proteomics approach as previously described (Chen et al., 2012; Kim et al., 2006).”
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Processes and therapeutic perspectives of acylation modifications of lysine and cysteine in tumors
Jiang, J., Chen, J., Huang, S., Tian, Y., Liu, L., Yao, J., Zhang, Y., Jiang, C., Zhang, X., Han, N., et al. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-026-02707-4
“This modification was first identified in mammalian cells by Tan et al. [163].”
InfluentialSelf-citationCPS1: a multipurpose mitochondrial enzyme, bile protein, acute liver injury biomarker, and cytokine
Chen, L., Li, P., Park, M.-J., Chen, Z., & Omary, M. B. (2026) · Gut · doi:10.1136/gutjnl-2024-333082
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Xu, K., Yang, G., Li, J., Liu, W., Jiang, X., & Xin, Y. (2026) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2026.04.004
Analyse multi-omique des acylations de lysines d'histones pendant la gamétogénèse
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“Recently, researchers have expanded their horizon to study the diverse acyl modifications besides acetylation at the e -lysine side chain (Chen et al., 2007; Du et al., 2011; Peng et al., 2011; Tan et al., 2014).”
Chen, G., Chen, Y., Chu, C., & Zhu, X. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1823993
Self-citationChemical biology tools for studying histone post-translational modifications
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AKT1 glutarylation regulated by GCDH and SIRT5 suppresses oncogenic signaling
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Self-citationGraff, S., Stransky, S., Kraz, I., Duraivelan, K., Poppel, A. J., Chatoff, A. G., Snyder, N. W., Garforth, S., Shechter, D., Maianti, J. P., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.29.728167
“These PTMs are typically not detectable as histone modifications in human cells but may have biological relevance in other organisms 5,33 – 35 .”
Turner, N. P., Baboo, S., Garrett, P., Diedrich, J. K., Bajo, M., Roberto, M., & Yates, J. R. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.6c01147 · Cited by 1
“A striking and serendipitous finding from our systematic evaluation was the dramatically enhanced identification of succinyl-lysine A B”
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“…emerged as a milestone in this field, with the first in vitro and in vivo demonstrations of its novel deacylase activities, including lysine desuccinylation (Ksucc) and lysine demalonylation (Kma) [ 18, 19]; in 2014, lysine deglutarylation (Kglu) was added to its repertoire of activities [20 ].”
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“To date, research on targeting succinylation has primarily focused on the desuccinylase SIRT5 and SIRT7.”
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“In contrast to the above neutral short-chain acylations, malonylation, succinylation, and glutarylation belong to dicarboxyl acylations, with malonyl-CoA, succinyl-CoA, and glutaryl-CoA serving as their respective acyl donors (Zhang et al., 2011; Tan et al., 2014).”
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“In addition, the C 3 -iminylated sites in carbamoyl-phosphate synthase Cps1 have previously been shown to be modified by various acylations, including acetylation, succinylation, and glutarylation, which generally reduced activity of this enzyme (62, 63).”
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Self-citationLysine butyrylation modulates central carbon metabolism and photosynthesis in cyanobacteria
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“…spectrometry has facilitated the discovery of numerous novel lysine acylation modifications in recent years (4), including propionylation (5), butyrylation (5), crotonylation (6), 2-hydroxyisobutyrylation (7), β -hydroxybutyrylation (8), malonylation (9), succinylation (9), and glutamylation (10).”
Self-citationLiu, W., Yang, Z., Zhang, H., Yang, M., Zhong, C., Li, X., Miao, Y., Ma, L., Wang, H.-L., & Yang, L. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6c01808
BindingDB Entry 50001308: The mimics of N
BindingDB (2020) · UC San Diego · doi:10.7270/q2gx4f1m
BindingDB (2025) · UC San Diego · doi:10.7270/q29w0m52
BindingDB (2023) · UC San Diego · doi:10.7270/q26w9g30
FAIRsharing record for: Protein Lysine Modifications Database
FAIRsharing Team, & Lister, A. (2022) · FAIRsharing.org · doi:10.25504/fairsharing.7b2e3b
BindingDB (2023) · UC San Diego · doi:10.7270/q2125xq3
BindingDB Entry 50016008: Potent and Specific Activators for Mitochondrial Sirtuins Sirt3 and Sirt5.
BindingDB (2023) · UC San Diego · doi:10.7270/q2s75mb0
BindingDB Entry 50000621: Potent and Selective Inhibitors of Human Sirtuin 5.
BindingDB (2019) · UC San Diego · doi:10.7270/q2ww7m4j
Metadata
- Authors
- Tan, M., Peng, C., Anderson, K. A., Chhoy, P., Xie, Z., Dai, L., Park, J., Chen, Y., Huang, H., Zhang, Y., Ro, J., Wagner, G. R., Green, M. F., Madsen, A. S., Schmiesing, J., Peterson, B. S., Xu, G., Ilkayeva, O. R., Muehlbauer, M. J., Braulke, T., Mühlhausen, C., Backos, D. S., Olsen, C. A., McGuire, P. J., Pletcher, S. D., Lombard, D. B., Hirschey, M. D., & Zhao, Y.
- Affiliations
- Chinese Academy of Sciences (CN)
- University of Chicago (US)
- Duke University (US)
- University of Michigan (US)
- Technical University of Denmark (DK)
- University Medical Center Hamburg-Eppendorf (DE)
- University of Colorado Anschutz (US)
- National Institutes of Health (US)
- Corresponding author
- Hirschey, Matthew D.
- Zhao, Yingming
- ORCID
- Tan, Minjia
- Peng, Chao
- Chhoy, Peter
- Xie, Zhongyu
- Dai, Lunzhi
- Huang, He
- Zhang, Yi
- Ro, Jennifer
- Green, Michelle F.
- Madsen, Andreas S.
- Xu, Guofeng
- Ilkayeva, Olga R.
- Muehlbauer, Michael J.
- Braulke, Thomas
- Mühlhausen, Chris
- Backos, Donald S.
- Olsen, Christian A.
- McGuire, Peter J.
- Pletcher, Scott D.
- Lombard, David B.
- Hirschey, Matthew D.
- Zhao, Yingming
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2014-04
- Volume
- 19
- Issue
- 4
- Pages
- 605-617
- ISSN
- 1550-4131 (ISSN-L)
- PMC
- PMC4108075
- OpenAlex
- W2088511656
- Cited by
- 844
- References
- 45
- Citations by year
- 2026: 49 · 2025: 63 · 2024: 86 · 2023: 50 · 2022: 79 · 2021: 106 · 2020: 67 · 2019: 74 · 2018: 80 · 2017: 53 · 2016: 70 · 2015: 50 · 2014: 16
- FWCI
- 32.61
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
- Technical University of Denmark, DTU Orbit (Technical University of Denmark, DTU) (submittedVersion)
- Funders
- Lundbeckfonden (R52-2010-5054)
- National Institutes of Health (UL1TR000430)
- National Institute on Alcohol Abuse and Alcoholism (AA022146, R01AA022146)
- National Institute on Aging (F31AG047696, R01AG045351, AG045351, P30AG013283, T32AG000114)
- National Cancer Institute (R21CA177925, CA160036, CA059365-19, U24CA160036, T32CA059365, CA177925)
- National Institute of General Medical Sciences (GM105933, T32GM007105, GM101171, T32GM007315, R01GM101171, R01GM105933)
- National Institute of Diabetes and Digestive and Kidney Diseases (P30DK096493, P30DK020572)
- National Center for Research Resources (RR020839, U54RR020839)
- National Center for Advancing Translational Sciences
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Keywords
- SIRT5, protein posttranslational modification, urea cycle, glutaric aciduria type I, glutaryl-CoA, mitochondrial proteins, metabolic enzymes
- MeSH terms
- Acyl Coenzyme A, Animals, Carbamoyl-Phosphate Synthase (Ammonia), Lysine, Models, Biological, Protein Processing, Post-Translational, Mass Spectrometry, Immunoblotting, Molecular Structure, Sirtuins, Proteomics, Mice
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 ›
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