title: Metabolic Regulation by Lysine Malonylation, Succinylation, and Glutarylation.
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.
authors.affiliation: 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.
authors.forename: Matthew D
authors.initials: MD
authors.lastname: Hirschey
authors.affiliation: ¶Ben May Department for Cancer Research, The University of Chicago, Chicago, IL 60637 matthew.hirschey@duke.edu Yingming.Zhao@uchicago.edu.
authors.forename: Yingming
authors.initials: Y
authors.lastname: Zhao
mesh_terms: D000215:Acylation; D000818:Animals; D005786:Gene Expression Regulation; D006801:Humans; D042541:Intracellular Space / Q000378:metabolism; D008239:Lysine / Q000378:metabolism*; D009243:NAD / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism*; D037761:Sirtuins / Q000378:metabolism*
chemical_list: D011506:Proteins; D009243:NAD; C508544:SIRT5 protein, human; D037761:Sirtuins; D008239:Lysine