Dynamic interplay between O-GlcNAc and O-phosphate: the sweet side of protein regulation.
Beta-O-linked N-acetylglucosamine (O-GlcNAc) is an abundant modification of cytosolic and nuclear proteins that occurs in metazoans. O-GlcNAc is dynamically processed by a unique set of enzymes that actively add and remove the modification. Functionally, O-GlcNAc appears to regulate protein stability, subcellular localization and protein-protein interactions. The modification often acts in a reciprocal manner to O-phosphate modifications of proteins and together they can synergistically control the activity of many cellular processes. Recently, O-GlcNAc has been demonstrated to play a significant role in diseases such as diabetes, cancer and neurodegeneration. For example, the increased levels of O-GlcNAc that occur in diabetes are associated with decreased insulin responsiveness in adipocytes.
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205-2185, USA.
Chad
C
Slawson
Gerald W
GW
Hart
D000117:Acetylglucosamine / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D006706:Homeostasis / Q000502:physiology; D006801:Humans; D009369:Neoplasms / Q000378:metabolism*; D010710:Phosphates / Q000737:chemistry / Q000378:metabolism*; D014176:Protein Biosynthesis; D011506:Proteins / Q000737:chemistry; D015398:Signal Transduction / Q000502:physiology*; D014158:Transcription, Genetic / Q000502:physiology*
D010710:Phosphates; D011506:Proteins; D000117:Acetylglucosamine