Metabolic Regulation by Lysine Malonylation, Succinylation, and Glutarylation

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...

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Bibliographic Details
Published inMolecular & cellular proteomics Vol. 14; no. 9; pp. 2308 - 2315
Main Authors Hirschey, Matthew D., Zhao, Yingming
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.09.2015
The American Society for Biochemistry and Molecular Biology
Subjects
Acylation
Animals
Gene Expression Regulation
Humans
Intracellular Space - metabolism
Lysine - metabolism
NAD - metabolism
Protein Processing, Post-Translational
Proteins - metabolism
Sirtuins - metabolism
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Summary: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.
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ISSN:1535-9476
1535-9484
DOI:10.1074/mcp.R114.046664