O-GlcNAc transferase substrate specificity is regulated by MYPT1 and other interacting proteins.
J Biol Chem. 2008 Oct 7;
Authors: Cheung WD, Sakabe K, Housley MP, Dias WB, Hart GW
O-GlcNAc transferase (OGT) substrate specificity is regulated by transiently interacting proteins. To further examine the regulation of OGT, we have identified 27 putative OGT interacting proteins through a yeast two-hybrid screen. Two of these proteins, Trak1 (OIP106) and O-GlcNAcase, have previously been shown to interact with and regulate OGT. We demonstrate here that MYPT1 and CARM1 also interact with and target OGT. MYPT1 and CARM1 are substrates of OGT in vitro and in vivo. MYPT1 and CARM1 also function to alter OGT substrate specificity in vitro. Furthermore, depletion of MYPT1 in Neuro-2a neuroblastoma cells alters GlcNAcylation of several proteins under basal conditions, suggesting that MYPT1 regulates OGT substrate specificity in vivo.
PMID: 18840611 [PubMed - as supplied by publisher]