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Acetylation of Sirt2 by p300 attenuates its deacetylase activity.
Biochem Biophys Res Commun. 2008 Oct 31; 375(4):576-80.BB

Abstract

Histone deacetylases (HDACs) are subdivided into three classes--HDAC I, HDAC II, and Sir2. Sirt proteins are mammalian members of the Sir2 family of NAD+ (nicotinamide adenine dinucleotide)-dependent protein deacetylases. The balance between acetylation and deacetylation of histone and non-histone proteins, regulated by protein acetyltransferases and deacetylases, affects the expression of genes involved in a variety of cellular processes. In addition, HDAC1 is acetylated and regulated by p300, a transcriptional co-activator with protein acetyltransferase activity, suggesting that protein acetyltransferases and deacetylases they control the activities of each other. Although the regulation of HDAC1 by p300 is well characterized, the relationship between Sir2 homologs and p300 is not understood. Here, we report that p300 interacts with Sirt2, a member of the Sir2 family, and triggers the acetylation and subsequent down-regulation of the deacetylation activity of Sirt2, and that the acetylation of Sirt2 by p300 relieves the inhibitory effect of Sirt2 on the transcriptional activity of p53. These observations demonstrate that p300 can inactivate Sirt2 by acetylation and that p300 may regulate the activity of p53 indirectly through Sirt2 in addition to its direct modification of p53.

Authors+Show Affiliations

College of Pharmacy and Research Institute of Drug Development, Chonnam National University, Yongbong-dong 300, Gwangju 500-757, Republic of Korea.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

18722353

Citation

Han, Younho, et al. "Acetylation of Sirt2 By P300 Attenuates Its Deacetylase Activity." Biochemical and Biophysical Research Communications, vol. 375, no. 4, 2008, pp. 576-80.
Han Y, Jin YH, Kim YJ, et al. Acetylation of Sirt2 by p300 attenuates its deacetylase activity. Biochem Biophys Res Commun. 2008;375(4):576-80.
Han, Y., Jin, Y. H., Kim, Y. J., Kang, B. Y., Choi, H. J., Kim, D. W., Yeo, C. Y., & Lee, K. Y. (2008). Acetylation of Sirt2 by p300 attenuates its deacetylase activity. Biochemical and Biophysical Research Communications, 375(4), 576-80. https://doi.org/10.1016/j.bbrc.2008.08.042
Han Y, et al. Acetylation of Sirt2 By P300 Attenuates Its Deacetylase Activity. Biochem Biophys Res Commun. 2008 Oct 31;375(4):576-80. PubMed PMID: 18722353.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Acetylation of Sirt2 by p300 attenuates its deacetylase activity. AU - Han,Younho, AU - Jin,Yun-Hye, AU - Kim,Yeon-Jin, AU - Kang,Bok-Yun, AU - Choi,Hyun-Jin, AU - Kim,Dae-Won, AU - Yeo,Chang-Yeol, AU - Lee,Kwang-Youl, Y1 - 2008/08/21/ PY - 2008/08/05/received PY - 2008/08/12/accepted PY - 2008/8/30/pubmed PY - 2008/10/28/medline PY - 2008/8/30/entrez SP - 576 EP - 80 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 375 IS - 4 N2 - Histone deacetylases (HDACs) are subdivided into three classes--HDAC I, HDAC II, and Sir2. Sirt proteins are mammalian members of the Sir2 family of NAD+ (nicotinamide adenine dinucleotide)-dependent protein deacetylases. The balance between acetylation and deacetylation of histone and non-histone proteins, regulated by protein acetyltransferases and deacetylases, affects the expression of genes involved in a variety of cellular processes. In addition, HDAC1 is acetylated and regulated by p300, a transcriptional co-activator with protein acetyltransferase activity, suggesting that protein acetyltransferases and deacetylases they control the activities of each other. Although the regulation of HDAC1 by p300 is well characterized, the relationship between Sir2 homologs and p300 is not understood. Here, we report that p300 interacts with Sirt2, a member of the Sir2 family, and triggers the acetylation and subsequent down-regulation of the deacetylation activity of Sirt2, and that the acetylation of Sirt2 by p300 relieves the inhibitory effect of Sirt2 on the transcriptional activity of p53. These observations demonstrate that p300 can inactivate Sirt2 by acetylation and that p300 may regulate the activity of p53 indirectly through Sirt2 in addition to its direct modification of p53. SN - 1090-2104 UR - https://www.unboundmedicine.com/medline/citation/18722353/Acetylation_of_Sirt2_by_p300_attenuates_its_deacetylase_activity_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(08)01585-4 DB - PRIME DP - Unbound Medicine ER -