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Sirt2 interacts with 14-3-3 β/γ and down-regulates the activity of p53
- Title
- Sirt2 interacts with 14-3-3 β/γ and down-regulates the activity of p53
- Authors
- Jin Y.-H.; Kim Y.-J.; Kim D.-W.; Baek K.-H.; Kang B.Y.; Yeo C.-Y.; Lee K.-Y.
- Ewha Authors
- 여창열
- SCOPUS Author ID
- 여창열
- Issue Date
- 2008
- Journal Title
- Biochemical and Biophysical Research Communications
- ISSN
- 0006-291X
- Citation
- Biochemical and Biophysical Research Communications vol. 368, no. 3, pp. 690 - 695
- Indexed
- SCI; SCIE; SCOPUS
- Document Type
- Article
- 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. © 2008 Elsevier Inc. All rights reserved.
- DOI
- 10.1016/j.bbrc.2008.01.114
- Appears in Collections:
- 자연과학대학 > 생명과학전공 > Journal papers
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