High impact information on Ugcgl1

• The UDP-Glc:glycoprotein glucosyltransferase is a soluble enzyme of the endoplasmic reticulum that glucosylates protein-linked Man7-9GlcNAc2 to form the monoglucosylated derivatives [1].
• In this system UDP-Glc:glycoprotein glucosyltransferase (GT) serves as a glycoprotein specific folding sensor by specifically glucosylating N-linked glycans in misfolded glycoproteins thus retaining them in the calnexin/calreticulin chaperone cycle [2].
• Antisera raised against the C-terminus decapeptide of the alpha-subunit of the retinal guanine-nucleotide-binding protein (G-protein) transducing (Gt) cross-reacted with the alpha-subunit of the inhibitory G-protein Gi [3].
• A novel 100 kDa protein, localized to receptor-enriched endosomes, is immunologically related to the signal-transducing guanine-nucleotide-binding proteins Gt and Gi [3].
• The immunoreactivity of both Gt and p100 was specifically inhibited by the immunizing peptide with similar dose-dependencies [concn. causing 50% inhibition (IC50) = 300 ng/ml] [3].

Biological context of Ugcgl1

• This chapter discusses two of the steps that regulate the abundance of such N-glycan structures, including glycoprotein deglucosylation (by glucosidase II) and reglucosylation (by the UDP-Glc:glycoprotein glucosyltransferase), as well as an overview of methods to evaluate the N-glycans prevalent during glycoprotein biogenesis in the ER [4].

Anatomical context of Ugcgl1

• The UDP-Glc:glycoprotein glucosyltransferase is a soluble protein of the endoplasmic reticulum that catalyzes the glucosylation of protein-linked, glucose-free, high mannose-type oligosaccharides [5].
• The assay of UDP-Glc:glycoprotein glucosyltransferase allowed detection of the activity in microsomal membranes in which endogenous acceptors appeared to be absent or almost absent, such as those derived from mung bean, Mucor rouxii, Crithidia fasciculata, and Trypanosoma cruzi cells.(ABSTRACT TRUNCATED AT 250 WORDS)[6]
• On the other hand, the beta gamma subunits of heterotrimeric Gt protein was localized in plasma membranes but not in granule membranes [7].
• The short-circuit current (Isc), potential difference (PD), tissue conductance (Gt), and Na and Cl fluxes in the short-circuit state across rat ileum were studied in Ussing chambers using a variety of bathing solutions [8].

References