Metabolic Regulation by Lysine Malonylation, Succinylation, and Glutarylation

被引：331

作者：

Hirschey, Matthew D. ^{[1
,2
,3
]}

Zhao, Yingming ^{[4
]}

机构：

[1] Duke Univ, Duke Mol Physiol Inst, Med Ctr, Sarah W Stedman Metab & Nutr Ctr, Durham, NC 27710 USA

[2] Duke Univ, Med Ctr, Dept Med & Pharmacol, Durham, NC 27710 USA

[3] Duke Univ, Med Ctr, Dept Canc Biol, Durham, NC 27710 USA

[4] Univ Chicago, Ben May Dept Canc Res, Chicago, IL 60637 USA

来源：

MOLECULAR & CELLULAR PROTEOMICS | 2015年 / 14卷 / 09期

基金：

美国国家卫生研究院;

关键词：

HISTONE DEACETYLASE INHIBITOR; COA SYNTHETASE; SIR2; HOMOLOG; PROTEIN; ACETYLATION; DEFICIENCY; SIRTUINS; ENZYMES; NAD; IDENTIFICATION;

D O I：

10.1074/mcp.R114.046664

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Protein acetylation is a well-studied regulatory mechanism for several cellular processes, ranging from gene expression to metabolism. Recent discoveries of new post-translational modifications, including malonylation, succinylation, and glutarylation, have expanded our understanding of the types of modifications found on proteins. These three acidic lysine modifications are structurally similar but have the potential to regulate different proteins in different pathways. The deacylase sirtuin 5 (SIRT5) catalyzes the removal of these modifications from a wide range of proteins in different subcellular compartments. Here, we review these new modifications, their regulation by SIRT5, and their emerging role in cellular regulation and diseases.

引用

页码：2308 / 2315

页数：8

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