| Rescue of secretion of rare-disease-associated misfolded mutant glycoproteins in UGGT1 knock-out mammalian cells. | Rescue of secretion of rare-disease-associated misfolded mutant glycoproteins in UGGT1 knock-out mammalian cells.
Tax G, Guay KP, Pantalone L, Ceci M, Soldà T, Hitchman CJ, Hill JC, Vasiljević S, Lia A, Modenutti CP, Straatman KR, Santino A, Molinari M, Zitzmann N, Hebert DN, Roversi P, Trerotola M., | 02/6/2024 |
| The ER folding sensor UGGT1 acts on TAPBPR-chaperoned peptide-free MHC I. | The ER folding sensor UGGT1 acts on TAPBPR-chaperoned peptide-free MHC I.
Sagert L, Winter C, Ruppert I, Zehetmaier M, Thomas C, Tampé R., Free PMC Article | 07/12/2023 |
| Polypeptide N-acetylgalactosaminyltransferase 18 retains in endoplasmic reticulum depending on its luminal regions interacting with ER resident UGGT1, PLOD3 and LPCAT1. | Polypeptide N-acetylgalactosaminyltransferase 18 retains in endoplasmic reticulum depending on its luminal regions interacting with ER resident UGGT1, PLOD3 and LPCAT1.
Jia W, Zou X, Xu Z, Bai L, Shan A, Li Y, Shi J, Yang F, Ding C, Narimatsu H, Zhang Y. | 04/9/2022 |
| Quantitative glycoproteomics reveals cellular substrate selectivity of the ER protein quality control sensors UGGT1 and UGGT2. | Quantitative glycoproteomics reveals cellular substrate selectivity of the ER protein quality control sensors UGGT1 and UGGT2.
Adams BM, Canniff NP, Guay KP, Larsen ISB, Hebert DN., Free PMC Article | 03/20/2021 |
| Glycan dependent refolding activity of ER glucosyltransferase (UGGT). | Glycan dependent refolding activity of ER glucosyltransferase (UGGT).
Wang N, Seko A, Takeda Y, Ito Y. | 01/9/2021 |
| The authors identify an interaction between TAPBPR and UDP-glucose:glycoprotein glucosyltransferase 1 (UGT1), a folding sensor in the calnexin/calreticulin quality control cycle that is known to regenerate the Glc1Man9GlcNAc2 moiety on glycoproteins. The results suggest the formation of a multimeric complex, dependent on a conserved cysteine at position 94 in TAPBPR, in which TAPBPR promotes the association of UGT1 with p | TAPBPR bridges UDP-glucose:glycoprotein glucosyltransferase 1 onto MHC class I to provide quality control in the antigen presentation pathway.
Neerincx A, Hermann C, Antrobus R, van Hateren A, Cao H, Trautwein N, Stevanović S, Elliott T, Deane JE, Boyle LH., Free PMC Article | 02/17/2018 |
| In this study, we aimed to clarify the contribution of the noncatalytic domains by comparing activities of truncated forms of recombinant HUGT1/HUGT2 and HUGT1/HUGT2 chimeras with full-length enzymes. | Effects of domain composition on catalytic activity of human UDP-glucose:glycoprotein glucosyltransferases.
Takeda Y, Seko A, Fujikawa K, Izumi M, Kajihara Y, Ito Y. | 01/6/2018 |
| both vIL-6 and VKORC1v2 interact with calnexin cycle proteins UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1), which catalyzes monoglucosylation of N-glycans, and oppositely acting glucosidase II (GlucII), and that vIL-6 can promote protein folding. | Human Herpesvirus 8 Interleukin-6 Interacts with Calnexin Cycle Components and Promotes Protein Folding.
Chen D, Xiang Q, Nicholas J., Free PMC Article | 11/4/2017 |
| These findings provide important insight on the role of unfolded protein response (UPR) and host UGGT1 in regulating RNA virus replication and pathogenicity. | UGGT1 enhances enterovirus 71 pathogenicity by promoting viral RNA synthesis and viral replication.
Huang PN, Jheng JR, Arnold JJ, Wang JR, Cameron CE, Shih SR., Free PMC Article | 09/16/2017 |
| The results demonstrated that FAM5C is an N-glycosylated protein, and N-glycosylation by UGGT1 is necessary for the secretion of FAM5C. | Interaction of FAM5C with UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1): Implication of N-glycosylation in FAM5C secretion.
Terao Y, Fujita H, Horibe S, Sato J, Minami S, Kobayashi M, Matsuoka I, Sasaki N, Satomi-Kobayashi S, Hirata KI, Rikitake Y. | 06/3/2017 |
| A novel UGGT1- and p97-dependent protein quality checkpoint is shown. This checkpoint is alerted to prevent secretion of a polypeptide that passes the luminal quality control scrutiny by BiP and CNX but contains an intramembrane ionizable residue. | A novel UGGT1 and p97-dependent checkpoint for native ectodomains with ionizable intramembrane residue.
Merulla J, Soldà T, Molinari M., Free PMC Article | 02/6/2016 |
| Kyte-Doolittle analysis as well as homology modeling revealed a cluster of hydrophobic amino acids that may be functional in the folding sensing mechanism of HUGT1 | Profiling Aglycon-Recognizing Sites of UDP-glucose:glycoprotein Glucosyltransferase by Means of Squarate-Mediated Labeling.
Ohara K, Takeda Y, Daikoku S, Hachisu M, Seko A, Ito Y. | 10/24/2015 |
| Results indicate that glycan structures are similar to endogenous glycans at low expression levels of uridine 5'-diphosphate-glucose: glycoprotein glucosyltransferase (UGGT1). | The relationship between glycan structures and expression levels of an endoplasmic reticulum-resident glycoprotein, UDP-glucose: Glycoprotein glucosyltransferase 1.
Daikoku S, Seko A, Son SH, Suzuki K, Ito Y, Kanie O. | 08/15/2015 |
| The UGGT1 is a well-documented enzyme which functions as a folding sensor in the endoplasmic reticulum, by the virtue of its ability to transfer a glucose residue to non-glucosylated high-mannose-type glycans of immature glycoproteins. | Both isoforms of human UDP-glucose:glycoprotein glucosyltransferase are enzymatically active.
Takeda Y, Seko A, Hachisu M, Daikoku S, Izumi M, Koizumi A, Fujikawa K, Kajihara Y, Ito Y. | 03/7/2015 |
| UGT1 aids in the folding of sequential domain-containing proteins such as prosaposin. | The role of UDP-Glc:glycoprotein glucosyltransferase 1 in the maturation of an obligate substrate prosaposin.
Pearse BR, Tamura T, Sunryd JC, Grabowski GA, Kaufman RJ, Hebert DN., Free PMC Article | 07/26/2010 |
| overexpression leads to increase in production of recombinant proteins; gene targeting | Identification of HUGT1 as a potential BiP activator and a cellular target for improvement of recombinant protein production using a cDNA screening system.
Ku SC, Lwa TR, Giam M, Yap MG, Chao SH. | 01/21/2010 |
| The substrate binding specificity | Substrate recognition by nucleotide sugar transporters: further characterization of substrate recognition regions by analyses of UDP-galactose/CMP-sialic acid transporter chimeras and biochemical analysis of the substrate specificity of parental and chimeric transporters.
Aoki K, Ishida N, Kawakita M. | 01/21/2010 |
| the amino-terminal 80% of HUGT1 is required for activation of the catalytic domain | The noncatalytic portion of human UDP-glucose: glycoprotein glucosyltransferase I confers UDP-glucose binding and transferase function to the catalytic domain.
Arnold SM, Kaufman RJ. | 01/21/2010 |