期刊
TRENDS IN BIOCHEMICAL SCIENCES
卷 33, 期 11, 页码 517-525出版社
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2008.08.001
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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.
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