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Sirt2 interacts with 14-3-3 β/γ and down-regulates the activity of p53
- Sirt2 interacts with 14-3-3 β/γ and down-regulates the activity of p53
- Jin Y.-H.; Kim Y.-J.; Kim D.-W.; Baek K.-H.; Kang B.Y.; Yeo C.-Y.; Lee K.-Y.
- Ewha Authors
- SCOPUS Author ID
- Issue Date
- Journal Title
- Biochemical and Biophysical Research Communications
- vol. 368, no. 3, pp. 690 - 695
- SCI; SCIE; SCOPUS
- 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. © 2008 Elsevier Inc. All rights reserved.
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