Sirt2 interacts with 14-3-3 β/γ and down-regulates the activity of p53

Yun Hye Jin, Yeon Jin Kim, Dae Won Kim, Kwang Hyun Baek, Bok Yun Kang, Chang Yeol Yeo, Kwang Youl Lee

Research output: Contribution to journalArticle

84 Citations (Scopus)

Abstract

Sirt2 is a mammalian member of the Sirtuin family of NAD+ (nicotinamide adenine dinucleotide)-dependent protein deacetylases. Although Sir-2.1 (a Caenorhabditis elegans Sirt2 ortholog) has been reported to interact with PAR-5/FTT-2 (a C. elegans 14-3-3 homolog), the molecular significance of the interaction between Sirt2 and 14-3-3 proteins in mammalian cell is not understood. Here, we report that Sirt2 interacts with 14-3-3 β and γ among various 14-3-3 isoforms, and that this interaction is strengthened by AKT. Furthermore, Sirt2 deacetylates and down-regulates the transcriptional activity of p53, and 14-3-3 β/γ augment deacetylation and down-regulation of the p53 transcriptional activity by Sirt2 in an AKT-dependent manner. Treatment of cells with nicotinamide, an inhibitor of Sirtuins, relieves the inhibition of p53 by Sirt2 and 14-3-3 β/γ. Therefore, our results suggest that the interaction between Sirt2 and 14-3-3 β/γ is a novel mechanism for the negative regulation of p53 beside the well-characterized Mdm2-mediated repression.

Original languageEnglish
Pages (from-to)690-695
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume368
Issue number3
DOIs
Publication statusPublished - 2008 Apr 11

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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