ArticleThe Journal of biological chemistry2015
Ubiquitinated sirtuin 1 (SIRT1) function is modulated during DNA damage-induced cell death and survival.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- ERα/SIRT1 signaling mediates the metabolic regulatory benefits of pterostilbene.The Journal of biological chemistry · 2026Article
- Fibrillarin Resists Cellular Senescence Via SIRT1-Dependent Nicotinamide Metabolism and Its Inhibition Sensitizes Senolytic Therapy in Esophageal Squamous Cell Carcinoma.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Review
- Melatonin Attenuates the Inflammatory Response of Astrocyte Following Ischemia Stroke through SIRT1/NF-κΒ Signaling Pathway.Molecular neurobiology · 2025Article
- Exploring NNMT: from metabolic pathways to therapeutic targets.Archives of pharmacal research · 2024Review
- Review
- Review
- SIRT1 ISGylation accelerates tumor progression by unleashing SIRT1 from the inactive state to promote its deacetylase activity.Experimental & molecular medicine · 2024Article
- Does Selection for Longevity inInternational journal of molecular sciences · 2024Article
- CoClFEBS open bio · 2023Article
- SIRT1 ubiquitination is regulated by opposing activities of APC/C-Cdh1 and AROS during stress-induced premature senescence.Experimental & molecular medicine · 2023Article
- Oxidative stress impairs the Nur77-Sirt1 axis resulting in a decline in organism homeostasis during aging.Aging cell · 2023Article
- Contribution of microRNA-30d to the prevention of the thyroid cancer occurrence and progression: mechanism and implications.Apoptosis : an international journal on programmed cell death · 2023Article
- Bone marrow mesenchymal stem cell-derived exosomal lncRNA KLF3-AS1 stabilizes Sirt1 protein to improve cerebral ischemia/reperfusion injury via miR-206/USP22 axis.Molecular medicine (Cambridge, Mass.) · 2023Article
- Role of Post-translational Modification of Silent Mating Type Information Regulator 2 Homolog 1 in Cancer and Other Disorders.Journal of cancer prevention · 2022Review
- MHY2245, a Sirtuin Inhibitor, Induces Cell Cycle Arrest and Apoptosis in HCT116 Human Colorectal Cancer Cells.International journal of molecular sciences · 2022Article
- Genes and Longevity of Lifespan.International journal of molecular sciences · 2022Review
- Regulation of SIRT1 and Its Roles in Inflammation.Frontiers in immunology · 2022Review
- Post-translational Modification in Control of SIRT1 Stability during DNA Damage Response.International journal of biological sciences · 2022Article
- CaCancer science · 2021Article
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Authors and funding
10 authors.
Funding
Abstract
Downstream signaling of physiological and pathological cell responses depends on post-translational modification such as ubiquitination. The mechanisms regulating downstream DNA damage response (DDR) signaling are not completely elucidated. Sirtuin 1 (SIRT1), the founding member of Class III histone deacetylases, regulates multiple steps in DDR and is closely associated with many physiological and pathological processes. However, the role of post-translational modification or ubiquitination of SIRT1 during DDR is unclear. We show that SIRT1 is dynamically and distinctly ubiquitinated in response to DNA damage. SIRT1 was ubiquitinated by the MDM2 E3 ligase in vitro and in vivo. SIRT1 ubiquitination under normal conditions had no effect on its enzymatic activity or rate of degradation; hypo-ubiquitination, however, reduced SIRT1 nuclear localization. Ubiquitination of SIRT1 affected its function in cell death and survival in response to DNA damage. Our results suggest that ubiquitination is required for SIRT1 function during DDR.
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