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Updated: May 3, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
Published on: February 27, 2016
Calorie restriction upregulated sirtuin 1 by attenuating its ubiquitin degradation in cancer cells
Limin Han1, Ganye Zhao, Hui Wang
1Peking University Research Center on Ageing, Peking University Health Science Center, Beijing, China; Department of Biochemistry & Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.
Abstract:
Sirtuin (SIRT) 1 is a key protein in mediating the benefits of calorie restriction (CR) in mammals. However, the molecular mechanisms underlying CR-induced SIRT1 upregulation in mammals remain unclear. Herein we show that the elevated SIRT1 levels are not due to increased SIRT1 mRNA expression. but rather to enhanced SIRT1 protein stability as a result of reduced ubiquitin-proteasome degradation of SIRT1 under limited nutrient conditions. Our observations have important implications for improving healthy aging in humans.
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