Cited by 262Sirtuins and Resveratrol in MedicineAdipose Tissue and MetabolismAutophagy in Disease and Therapy

Mitochondrial sirtuins: regulators of protein acylation and metabolism

He, Wenjuan, Newman, John C., Wang, Margaret Z., Ho, Linh, Verdin, Eric·2012·Trends in Endocrinology & Metabolism

Abstract

Sirtuins are NAD(+)-dependent protein deacetylases and have been implicated in the regulation of metabolism, stress responses, and aging. Three sirtuins are located in mitochondria: SIRT3, 4, and 5. SIRT3 deacetylates and regulates the enzymatic activity of many metabolic enzymes in mitochondria, whereas SIRT5 removes two novel post-translational modifications, lysine malonylation and succinylation. Here, we review the current knowledge of how mitochondrial sirtuins function in metabolism and metabolic diseases, and offer a conceptual model how they may regulate mitochondrial function through distinct deacylation activities (deacetylation, demalonylation, or desuccinylation).

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Crossref · 10.1016/j.tem.2012.07.004

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  • Some sirtuin family members mediate non-acetyl lysine acylations, such as succinylation, malonylation and fatty acid acylation, whose cellular functions are poorly understood.

    “Additionally, some members of the sirtuin family mediate non-acetyl lysine acylations (for example, succinylation, malonylation and fatty acid acylation)13–15, the cellular functions of which are so far poorly understood16.”

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References 100 · Cited by 262

Authors
He, W., Newman, J. C., Wang, M. Z., Ho, L., & Verdin, E.
Affiliations
University of California, San Francisco (US)
Venue
Trends in Endocrinology & Metabolism
Publisher
Elsevier BV
Published
2012-09
Volume
23
Issue
9
Pages
467-476
ISSN
1043-2760 (ISSN-L)
OpenAlex
W2045303676
Cited by
262
References
100
Citations by year
2026: 10 · 2025: 14 · 2024: 10 · 2023: 15 · 2022: 12 · 2021: 19 · 2020: 23 · 2019: 15 · 2018: 19 · 2017: 20 · 2016: 15 · 2015: 32 · 2014: 26 · 2013: 29 · 2012: 2
FWCI
2.41
Type
journal article
Language
en
Open access
closed
Locations
  • Trends in Endocrinology and Metabolism (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Institute of Allergy and Infectious Diseases (P30AI027763)
Topics
  • Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
  • Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
  • Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
Keywords
mitochondrial sirtuins, SIRT3, SIRT4, SIRT5, NAD+-dependent deacetylase, protein acylation, lysine malonylation, lysine succinylation, desuccinylation, mitochondrial metabolism, metabolic disorders, aging, stress response
MeSH terms
Acylation, Animals, Humans, Mitochondrial Proteins, Sirtuins

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