Evidence for a Common Mechanism of SIRT1 Regulation by Allosteric Activators-Reference-Cited by-同舟云学术

Evidence for a Common Mechanism of SIRT1 Regulation by Allosteric Activators

Published:2013-03-08 Issue:6124 Volume:339 Page:1216-1219
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Hubbard Basil P.¹,Gomes Ana P.¹²,Dai Han³,Li Jun¹,Case April W.³,Considine Thomas³,Riera Thomas V.³,Lee Jessica E.⁴,E Sook Yen⁴,Lamming Dudley W.¹,Pentelute Bradley L.⁵,Schuman Eli R.³,Stevens Linda A.⁶,Ling Alvin J. Y.¹,Armour Sean M.¹,Michan Shaday¹,Zhao Huizhen⁷,Jiang Yong⁷,Sweitzer Sharon M.⁷,Blum Charles A.³,Disch Jeremy S.³,Ng Pui Yee³,Howitz Konrad T.⁸,Rolo Anabela P.²⁹,Hamuro Yoshitomo⁴,Moss Joel⁶,Perni Robert B.³,Ellis James L.³,Vlasuk George P.³,Sinclair David A.¹¹⁰

Affiliation:

1. Department of Genetics, Harvard Medical School, Boston, MA 02115, USA.

2. Center for Neurosciences and Cell Biology, Department of Life Sciences, University of Coimbra, Coimbra 3004-517, Portugal.

3. Sirtris, a GSK Company, Cambridge, MA 02139, USA.

4. ExSAR Corporation, Monmouth Junction, NJ 08852, USA.

5. Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.

6. NIH Cardiovascular and Pulmonary Branch/National Heart, Lung and Blood Institute, Bethesda, MD 20892, USA.

7. GlaxoSmithKline, Collegeville, PA 19426, USA.

8. BIOMOL Research Laboratories Inc., Plymouth Meeting, PA 19462, USA.

9. Department of Biology, University of Aveiro, Aveiro 3810-193, Portugal.

10. Department of Pharmacology, University of New South Wales, Sydney, NSW 2052, Australia.

Abstract

It's a SIRT Intense attention has focused on the SIRT1 deacetylase as a possible target for anti-aging drugs. But unexpected complications in assays of SIRT1 activity have made it unclear whether compounds thought to be sirtuin-activating compounds (STACs) are really direct regulators of the enzyme. Further exploration of these effects by Hubbard et al. (p. 1216 ; see the Perspective by Yuan and Marmorstein ) revealed that interaction of SIRT1 with certain substrates allows activation of SIRT1 by STACs and identified critical amino acids in SIRT1 required for these effects. Mouse myoblasts reconstituted with SIRT1 mutated at this amino acid lost their responsiveness to STACs.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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