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Mol Cell Proteomics. 2015 Sep;14(9):2308-15. doi: 10.1074/mcp.R114.046664. Epub 2015 Feb 25.

Metabolic Regulation by Lysine Malonylation, Succinylation, and Glutarylation.

Author information

1
From the ‡Duke Molecular Physiology Institute, Sarah W. Stedman Metabolism and Nutrition Center, §Departments of Medicine & Pharmacology and Cancer Biology, Duke University, Medical Center, Durham, NC 27710; matthew.hirschey@duke.edu Yingming.Zhao@uchicago.edu.
2
¶Ben May Department for Cancer Research, The University of Chicago, Chicago, IL 60637 matthew.hirschey@duke.edu Yingming.Zhao@uchicago.edu.

Abstract

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.

PMID:
25717114
PMCID:
PMC4563717
DOI:
10.1074/mcp.R114.046664
[Indexed for MEDLINE]
Free PMC Article

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