Stabilization of Suv39H1 by SirT1 is part of oxidative stress response and ensures genome protection.
Open accessAbstract
Sirtuins are NAD-dependent deacetylases that sense oxidative stress conditions and promote a protective cellular response. The Sirtuin SirT1 is involved in facultative heterochromatin formation through an intimate functional relationship with the H3K9me3 methyltransferase Suv39h1, a chromatin organization protein. However, SirT1 also regulates Suv39h1-dependent constitutive heterochromatin (CH) through an unknown mechanism; interestingly, SirT1 does not significantly localize in these regions. Herein, we report that SirT1 controls global levels of Suv39h1 by increasing its half-life through inhibition of Suv39h1 lysine 87 polyubiquitination by the E3-ubiquitin ligase MDM2. This in turn increases Suv39h1 turnover in CH and ensures genome integrity. Stress conditions that lead to SirT1 upregulation, such as calorie restriction, also induce higher levels of Suv39h1 in a SirT1-dependent manner in vivo. These observations reflect a direct link between oxidative stress response and Suv39h1 and support a dynamic view of heterochromatin, in which its structure adapts to cell physiology.
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In cultured rat embryonic fibroblasts and in the adult rat liver, metabolic stress induced by caloric restriction increases Suv39h1, the mammalian homolog of Su(var)3-9.
“In cultured rat embryonic fibroblasts and in the adult rat liver, metabolic stress induced by caloric restriction increases Suv39h1, the mammalian homolog of Su(var)3-945.”
From Tau promotes neurodegeneration through global chromatin relaxation (2014) · cites this paper as [45]
SUV39H1 is an Mdm2 substrate that is deubiquitinated and stabilized by USP7 in undamaged cells.
“The SUV39H1 methyltransferase (also known as KMT1A) is another Mdm2 substrate that is deubiquitinated and stabilized by USP7 in undamaged cells (Bosch-Presegué et al., 2011; Mungamuri et al., 2016).”
From USP7 Is a Master Regulator of Genome Stability (2020) · cites this paper as Bosch-Presegué et al., 2011
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“The SUV39H1 methyltransferase (also known as KMT1A) is another Mdm2 substrate that is deubiquitinated and stabilized by USP7 in undamaged cells (Bosch-Presegué et al., 2011; Mungamuri et al., 2016).”
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- Authors
- Bosch-Presegué, L., Raurell-Vila, H., Marazuela-Duque, A., Kane-Goldsmith, N., Valle, A., Oliver, J., Serrano, L., & Vaquero, A.
- Affiliations
- Institut d'Investigació Biomédica de Bellvitge (ES)
- Universitat de les Illes Balears (ES)
- Rutgers, The State University of New Jersey (US)
- Institució Catalana de Recerca i Estudis Avançats (ES)
- Corresponding author
- Vaquero, Alejandro
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2011-04
- Volume
- 42
- Issue
- 2
- Pages
- 210-223
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2074347699
- Cited by
- 138
- References
- 34
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 11 · 2023: 4 · 2022: 8 · 2021: 9 · 2020: 8 · 2019: 7 · 2018: 14 · 2017: 16 · 2016: 6 · 2015: 10 · 2014: 15 · 2013: 14 · 2012: 10
- FWCI
- 6.10
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- SIRT1, SUV39H1, sirtuins, oxidative stress response, constitutive heterochromatin, facultative heterochromatin, protein stabilization, polyubiquitination, MDM2, H3K9me3, genome stability, caloric restriction, NAD+-dependent deacetylase
- MeSH terms
- Amino Acid Sequence, Animals, Enzyme Stability, Half-Life, HeLa Cells, Heterochromatin, Humans, Lysine, Male, Methyltransferases, Molecular Sequence Data, Mutation, Recombinant Fusion Proteins, Repressor Proteins, Time Factors, Transfection, Rats, Sprague-Dawley, Oxidative Stress, Polyubiquitin, Caloric Restriction, RNA Interference, NIH 3T3 Cells, Chromatin Assembly and Disassembly, Genomic Instability, Mice, Rats, Proto-Oncogene Proteins c-mdm2, Ubiquitination, Sirtuin 1, HEK293 Cells
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