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Trends Biochem Sci. 2008 Nov;33(11):517-25. doi: 10.1016/j.tibs.2008.08.001. Epub 2008 Sep 18.

The ups and downs of SIRT1.

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1
Gladstone Institute of Virology and Immunology, University of California, San Francisco, CA 94158, USA.

Abstract

Reversible acetylation has emerged as a key post-translational modification of proteins. Although the number of acetylated proteins is rapidly growing, the ways in which protein acetyltransferases and deacetylases connect with extracellular stimuli remain unclear. Recently, a regulatory network has emerged that controls the expression and activity of SIRT1, a mammalian class-III protein deacetylase. SIRT1 is an important regulator of metabolism, senescence, cancer and, possibly, longevity and is connected with crucial stress-responsive signal-transduction pathways. These connections provide important clues about how protein acetylation and deacetylation mediate cellular adaptations to extrinsic stress.

PMID:
18805010
DOI:
10.1016/j.tibs.2008.08.001
[Indexed for MEDLINE]

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