Metabolic Regulation by Lysine Malonylation, Succinylation, and Glutarylation
Year: 2015
Type: review
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.
Source: Molecular & Cellular Proteomics
Authors: Matthew D. Hirschey, Yingming Zhao
Institutions: Duke University, Duke Medical Center, University of Chicago
Language: English
Subfield: Geriatrics and Gerontology
Field: Medicine
Domain: Health Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
Funders: National Institutes of Health, National Institute on Alcohol Abuse and Alcoholism, National Institute on Aging, National Cancer Institute, National Institute of General Medical Sciences, National Institute of Diabetes and Digestive and Kidney Diseases, National Center for Research Resources
Awards: G2186646940, Studies on the Mechanisms by which SIRT5 Regulates Aging and Disease, George M. O'Brien Kidney Research Core Centers, G4699019166, Proteome Characterization Center: A Genoproteomics Pipeline for Cancer Biomarkers, Ethanol-induced Protein Acylation Regulates Metabolism, G7730770270, Biochemistry of lysine crotonylation pathway, Duke Claude D. Pepper Older Americans Independence Center
OpenAlex ID: W2121046220