Nonenzymatic Protein Acylation as a Carbon Stress Regulated by Sirtuin Deacylases

被引:294
作者
Wagner, Gregory R. [1 ]
Hirschey, Matthew D. [1 ,2 ,3 ,4 ]
机构
[1] Duke Univ, Med Ctr, Duke Mol Physiol Inst, Durham, NC 27710 USA
[2] Duke Univ, Med Ctr, Sarah W Stedman Nutr & Metab Ctr, Durham, NC 27710 USA
[3] Duke Univ, Med Ctr, Dept Med, Durham, NC 27710 USA
[4] Duke Univ, Med Ctr, Dept Pharmacol & Canc Biol, Durham, NC 27710 USA
基金
美国国家卫生研究院;
关键词
METHIONINE SULFOXIDE REDUCTASE; HISTONE ACETYLTRANSFERASE GCN5; STEADY-STATE CONCENTRATIONS; 3-HYDROXY-3-METHYLGLUTARYL-COA SYNTHASE; SIRT3-MEDIATED DEACETYLATION; SACCHAROMYCES-CEREVISIAE; LYSINE SUCCINYLATION; CALORIE RESTRICTION; OXIDATIVE STRESS; ACETYLATION;
D O I
10.1016/j.molcel.2014.03.027
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
070307 [化学生物学]; 071010 [生物化学与分子生物学];
摘要
Cellular proteins are decorated with a wide range of acetyl and other acyl modifications. Many studies have demonstrated regulation of site-specific acetylation by acetyltransferases and deacetylases. Acylation is emerging as a new type of lysine modification, but less is known about its overall regulatory role. Furthermore, the mechanisms of lysine acylation, its overlap with protein acetylation, and how it influences cellular function are major unanswered questions in the field. In this review, we discuss the known roles of acetyltransferases and deacetylases and the sirtuins as a conserved family of a nicotinamide adenine dinucleotide (NAD(+))-dependent protein deacylases that are important for response to cellular stress and homeostasis. We also consider the evidence for an emerging idea of nonenzymatic protein acylation. Finally, we put forward the hypothesis that protein acylation is a form of protein "carbon stress" that the deacylases evolved to remove as a part of a global protein quality-control network.
引用
收藏
页码:5 / 16
页数:12
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