SIRT5 regulates both cytosolic and mitochondrial protein malonylation with glycolysis as a major target
Open accessAbstract
Protein acylation links energetic substrate flux with cellular adaptive responses. SIRT5 is a NAD(+)-dependent lysine deacylase and removes both succinyl and malonyl groups. Using affinity enrichment and label free quantitative proteomics, we characterized the SIRT5-regulated lysine malonylome in wild-type (WT) and Sirt5(-/-) mice. 1,137 malonyllysine sites were identified across 430 proteins, with 183 sites (from 120 proteins) significantly increased in Sirt5(-/-) animals. Pathway analysis identified glycolysis as the top SIRT5-regulated pathway. Importantly, glycolytic flux was diminished in primary hepatocytes from Sirt5(-/-) compared to WT mice. Substitution of malonylated lysine residue 184 in glyceraldehyde 3-phosphate dehydrogenase with glutamic acid, a malonyllysine mimic, suppressed its enzymatic activity. Comparison with our previous reports on acylation reveals that malonylation targets a different set of proteins than acetylation and succinylation. These data demonstrate that SIRT5 is a global regulator of lysine malonylation and provide a mechanism for regulation of energetic flux through glycolysis.
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HMGCS2 is also subject to glutarylation and malonylation.
“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 Nishida et al. 2015
The three cytosolic urea cycle enzymes are malonylated at multiple sites and demalonylated at some sites by SIRT5.
“The three other enzymes in the urea cycle are located in the cytosol and are also malonylated at multiple sites with demalonylation at some sites by SIRT5 (Nishida et al. 2015).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Nishida et al. 2015
SIRT5 is present in the nucleus and cytoplasm in addition to mitochondria.
“Given that SIRT5 is present in the nucleus and cytoplasm in addition to mitochondria ((Matsushita et al. 2011))((Park et al. 2013))((Nishida et al. 2015)), it will be interesting to test whether SIRT5 modulates the activity of the urea cycle via targeting of both mitochondrial and cytosolic enzymes, or whether one compartment’s effects dominate.”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Nishida et al. 2015
ASSY is demalonylated by SIRT5 at 2 of 11, ARLY at 1 of 6, and ARG1 at 3 of 16 malonyllysine sites.
“These are argininosuccinate synthase (ASSY), argininosuccinate lyase (ARLY), and arginase (ARGI1); ASSY is demalonylated by SIRT5 at 2 of 11, ARLY at 1 of 6, and ARG1 at 3 of 16 malonyllysine sites.”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Nishida et al. 2015
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- Authors
- Nishida, Y., Rardin, M. J., Carrico, C., He, W., Sahu, A. K., Gut, P., Najjar, R., Fitch, M., Hellerstein, M., Gibson, B. W., & Verdin, E.
- Affiliations
- Gladstone Institutes (US)
- Buck Institute for Research on Aging (US)
- Cell Signaling Technology (United States) (US)
- University of California, Berkeley (US)
- KineMed (United States) (US)
- Corresponding author
- Gibson, Bradford W.
- Verdin, Eric
- ORCID
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2015-07
- Volume
- 59
- Issue
- 2
- Pages
- 321-332
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC4571487
- OpenAlex
- W1955146052
- Cited by
- 481
- References
- 52
- Citations by year
- 2026: 25 · 2025: 43 · 2024: 61 · 2023: 34 · 2022: 45 · 2021: 70 · 2020: 40 · 2019: 39 · 2018: 54 · 2017: 32 · 2016: 31 · 2015: 7
- FWCI
- 20.63
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Gladstone Institutes
- Uehara Memorial Foundation
- National Institutes of Health (1s10od016281-01)
- Japan Society for the Promotion of Science
- National Institute on Aging (PL1AG032118, T32AG000266)
- National Institute of Allergy and Infectious Diseases (P30AI027763)
- National Institute of Diabetes and Digestive and Kidney Diseases (R24DK085610, P30DK063720, P30DK026743)
- National Center for Research Resources (S10RR024615)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- SIRT5, lysine malonylation, protein acylation, glycolysis, glyceraldehyde-3-phosphate dehydrogenase, hepatocytes
- MeSH terms
- Acylation, Animals, Cytosol, Glyceraldehyde-3-Phosphate Dehydrogenases, Glycolysis, Humans, Liver, Malonates, Mice, Knockout, Molecular Mimicry, Amino Acid Substitution, Catalytic Domain, Mitochondrial Proteins, Sirtuins, Mice, Metabolic Networks and Pathways, Gene Knockdown Techniques, HEK293 Cells
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