Sirt2 interacts with 14-3-3 beta/gamma and down-regulates the activity of p53.

@article{citeulike:2359438, 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 beta and gamma 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 beta/gamma 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 beta/gamma. Therefore, our results suggest that the interaction between Sirt2 and 14-3-3 beta/gamma is a novel mechanism for the negative regulation of p53 beside the well-characterized Mdm2-mediated repression.}, address = {College of Pharmacy and Research Institute of Drug Development, Chonnam National University, Gwangju, Republic of Korea.}, author = {Jin, Yun-Hye H. and Kim, Yeon-Jin J. and Kim, Dae-Won W. and Baek, Kwang-Hyun H. and Kang, Bok Yun Y. and Yeo, Chang-Yeol Y. and Lee, Kwang-Youl Y. }, citeulike-article-id = {2359438}, doi = {10.1016/j.bbrc.2008.01.114}, issn = {1090-2104}, journal = {Biochem Biophys Res Commun}, keywords = {example, peptides}, month = {February}, posted-at = {2008-05-30 14:33:53}, priority = {2}, title = {Sirt2 interacts with 14-3-3 beta/gamma and down-regulates the activity of p53.}, url = {http://dx.doi.org/10.1016/j.bbrc.2008.01.114}, year = {2008} }

TY - JOUR ID - citeulike:2359438 L3 - citeulike-article-id:2359438 TI - Sirt2 interacts with 14-3-3 beta/gamma and down-regulates the activity of p53. JF - Biochem Biophys Res Commun AD - College of Pharmacy and Research Institute of Drug Development, Chonnam National University, Gwangju, Republic of Korea. SN - 1090-2104 N2 - 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 beta and gamma 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 beta/gamma 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 beta/gamma. Therefore, our results suggest that the interaction between Sirt2 and 14-3-3 beta/gamma is a novel mechanism for the negative regulation of p53 beside the well-characterized Mdm2-mediated repression. KW - example KW - peptides AU - Jin, Yun-Hye AU - Kim, Yeon-Jin AU - Kim, Dae-Won AU - Baek, Kwang-Hyun AU - Kang, Bok Yun AU - Yeo, Chang-Yeol AU - Lee, Kwang-Youl PY - 2008/02/01/ UR - http://dx.doi.org/10.1016/j.bbrc.2008.01.114 ER -