SirT3 and p53 Deacetylation in Aging and Cancer

J Cell Physiol. 2017 Sep;232(9):2308-2311. doi: 10.1002/jcp.25669. Epub 2017 Apr 10.

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.

Publication types

  • Review

MeSH terms

  • Acetylation
  • Aging / metabolism*
  • Aging / pathology
  • Animals
  • Humans
  • Models, Molecular
  • Neoplasms / enzymology*
  • Neoplasms / pathology
  • Protein Conformation
  • Signal Transduction*
  • Sirtuin 3 / chemistry
  • Sirtuin 3 / metabolism*
  • Tumor Suppressor Protein p53 / chemistry
  • Tumor Suppressor Protein p53 / metabolism*

Substances

  • TP53 protein, human
  • Tumor Suppressor Protein p53
  • SIRT3 protein, human
  • Sirtuin 3