View : 22 Download: 0

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
여창열scopus
Issue Date
2008
Journal Title
Biochemical and Biophysical Research Communications
ISSN
0006-291XJCR Link
Citation
vol. 368, no. 3, pp. 690 - 695
Indexed
SCI; SCIE; SCOPUS WOS 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. © 2008 Elsevier Inc. All rights reserved.
DOI
10.1016/j.bbrc.2008.01.114
Appears in Collections:
자연과학대학 > 생명과학전공 > Journal papers
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE