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Updated: Mar 13, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
Published on: February 27, 2016
SirT3 and p53 Deacetylation in Aging and Cancer
Jijun Chen1,2, Aiqin Wang3, Qingqi Chen3
1Research and Development, Allonger LLC, Columbia, Maryland.
Abstract:
The mammalian Sirtuins are a family of highly conserved nicotinamide adenine dinucleotide (NAD+)-dependent histone deacetylase. The mammalian Sirtuins family has identified seven different types of sirtuin. Sirtuins 3(SirT3) is localized to mitochondria, and is a multiple functional protein deacylase through deacetylating a variety of substrates. Cellular senescence represents a permanent withdraw from cell cycle in response to diverse stress; it is controlled by the p53 and retinoblastoma protein (RB) tumor suppressors, and constitutes a potent anticancer mechanisms. p53 can be deacetylated by a protein complex containing histone deacetylases (HDAC1). There is possibility that SirT3 may also deacetylate p53. We introduce the recent research on the SirT3-p53 interplay directly and indirectly, and discuss the significance of p53 deacetylation by SirT3 in the aging and cancer. J. Cell. Physiol. 232: 2308-2311, 2017. © 2016 Wiley Periodicals, Inc.
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