Ontology highlight
ABSTRACT:
SUBMITTER: Whelan SA
PROVIDER: S-EPMC2490780 | biostudies-literature | 2008 Aug
REPOSITORIES: biostudies-literature
Whelan Stephen A SA Whelan Stephen A SA Lane M Daniel MD Hart Gerald W GW
The Journal of biological chemistry 20080602 31
O-Linked beta-N-acetylglucosamine (O-GlcNAc) transferase (OGT) catalyzes the addition of O-linked beta-N-acetylglucosamine (O-GlcNAc) onto serine and threonine residues in response to stimuli or stress analogous to phosphorylation by Ser/Thr-kinases. Like protein phosphatases, OGT appears to be targeted to myriad specific substrates by transiently interacting with specific targeting subunits. Here, we show that OGT is activated by insulin signaling. Insulin treatment of 3T3-L1 adipocytes stimula ...[more]