title: A Prob(e)able Route to Lysine Acylation.
abstract: Non-enzymatic modification of proteins by acyl-CoA species involved in intermediary metabolism is a possible explanation for widespread protein acylation. In this issue, Kulkarni et al. (2017) develop a set of chemoproteomic probes to interrogate the role of malonyl-CoA in mediating protein malonylation and find malonylation influences glycolysis in cancer cells.
authors.affiliation: Duke Molecular Physiology Institute and the Sarah W. Stedman Nutrition and Metabolism Center, Duke University Medical Center, Durham, NC 27701, USA; Department of Medicine, Division of Endocrinology, Metabolism, and Nutrition, Durham, NC 27710, USA.
authors.forename: Gregory R
authors.initials: GR
authors.lastname: Wagner
authors.affiliation: Duke Molecular Physiology Institute and the Sarah W. Stedman Nutrition and Metabolism Center, Duke University Medical Center, Durham, NC 27701, USA; Department of Medicine, Division of Endocrinology, Metabolism, and Nutrition, Durham, NC 27710, USA; Department of Pharmacology & Cancer Biology and Duke University Medical Center, Durham, NC 27710, USA. Electronic address: matthew.hirschey@duke.edu.
authors.forename: Matthew D
authors.initials: MD
authors.lastname: Hirschey
mesh_terms: D000214:Acyl Coenzyme A; D000215:Acylation; D008239:Lysine; D008316:Malonyl Coenzyme A; D011506:Proteins
chemical_list: D000214:Acyl Coenzyme A; D011506:Proteins; D008316:Malonyl Coenzyme A; D008239:Lysine