Journal
MOLECULAR & CELLULAR PROTEOMICS
Volume 14, Issue 9, Pages 2308-2315Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/mcp.R114.046664
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Funding
- American Heart Association [12SDG8840004, 12IRG9010008]
- Ellison Medical Foundation
- National Institutes of Health [R01AA022146, R01AG045351, U54RR020389, U24CA160036, R01GM105933]
- Duke O'Brien Center for Kidney Research [5P30DK096493-02]
- Duke Pepper Older Americans Independence Center (OAIC) Program in Aging Research - National Institute of Aging [P30AG028716-01]
- American Cancer Society [RSG-13-198-01-DDC]
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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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