| Literature DB >> 28408476 |
Moyira Aquino-Gil1,2,3, Annick Pierce4, Yobana Perez-Cervera3, Edgar Zenteno5, Tony Lefebvre4.
Abstract
O-GlcNAcylation is a highly dynamic post-translational modification whose level depends on nutrient status. Only two enzymes regulate O-GlcNAcylation cycling, the glycosyltransferase OGT (O-GlcNAc transferase) and the glycoside hydrolase OGA (O-GlcNAcase), that add and remove the GlcNAc moiety to and from acceptor proteins, respectively. During the last 30 years, OGT has emerged as a master regulator of cell life with O-GlcNAcylation being found in viruses, bacteria, insects, protists and metazoans. The study of OGT in different biological systems opens new perspectives for understanding this enzyme in many kingdoms of life. In this review, we summarize recent and older findings regarding the distribution of OGT in living organisms.Entities:
Keywords: O-GlcNAc transferase; O-GlcNAcylation; OGT
Mesh:
Substances:
Year: 2017 PMID: 28408476 DOI: 10.1042/BST20160404
Source DB: PubMed Journal: Biochem Soc Trans ISSN: 0300-5127 Impact factor: 5.407