Ask about this productRelated genes to: UGCGL1 antibody
- Gene:
- UGGT1 NIH gene
- Name:
- UDP-glucose glycoprotein glucosyltransferase 1
- Previous symbol:
- UGCGL1
- Synonyms:
- HUGT1
- Chromosome:
- 2q14.3
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-05
- Date modifiied:
- 2014-11-19
Related products to: UGCGL1 antibody
Related articles to: UGCGL1 antibody
- Chinese hamster ovary (CHO) cells are widely utilised in the biopharmaceutical industry to produce therapeutic proteins. Understanding the mechanisms of endoplasmic reticulum (ER) stress and its interplay with protein degradation pathways remains pivotal for improving production efficiency and product quality. In this study, we investigated the proteomic responses of CHO-K1 (non-producer), CHO DP-12 (IgG-producer), and NISTCHO (IgG-producer) cell lines under ER stress induced by a combination of the proteasome inhibitor MG132 and the glycosylation inhibitor tunicamycin. Viability, cell growth, and IgG titre were measured after 24 h, 48 h, and 72 h of treatment and the 48 h timepoint was used for the comparative analysis of the proteomic data across the three cell lines. Proteasome inhibition with MG132 intensified ER stress and altered ER-associated protein degradation (ERAD). Combined tunicamycin + MG132 treatment was associated with cell line-specific proteomic changes: NISTCHO upregulated ER translocation and glycoprotein quality control proteins (SSR4, SEC24C, UGGT1), CHO DP-12 activated redox/disulfide regulators (DNAJC10, CAPN1), while CHO-K1 showed broad proteome shifts, suggesting differences in baseline stress handling. These findings provide mechanistic insights into ER stress and protein quality control in CHO cells, offering a foundation for strategies to enhance cell line robustness and optimise biopharmaceutical production. - Source: PubMed
Publication date: 2026/02/10
Sideri Christiana-KondyloRyan DavidHenry MichaelEfeoglu EsenMeleady Paula - Most nascent glycoproteins entering the endoplasmic reticulum (ER) undergo quality control via the calnexin/calreticulin (CNX/CRT) cycle, wherein GlcManGlcNAc (G1M9)-type glycans play a crucial role in monitoring protein folding. We have recently identified an endo-α-mannosidase activity within the ER, designated as ER-EM, which facilitates the release of misfolded glycoproteins from this cycle by converting G1M9-proteins into ManGlcNAc (M8A)-proteins in a single step. ER-EM appears to function as a complex comprising UDP-Glc:glycoprotein glucosyltransferase 1 (UGGT1), ERp57, and carboxylesterase 1D (Ces1d), although the role of Ces1d-primarily recognized for its involvement in lipid metabolism-in glycan-associated substrate recognition remains unclear. To elucidate the molecular basis of Ces1d-dependent recognition, we semi-synthesized a glycoprobe, G1M9-va-JW972, by conjugating the Ces1d-specific inhibitor JW972 to the aglycone of G1M9 using a linker via a click reaction. In the ER-EM reaction with this probe, M8A-va-piperidine was detected as an ER-EM product with the aglycone structural conversion via Ces1d-mediated hydrolysis of the JW972 moiety, demonstrating recognition of the substrate aglycone by the Ces1d component of ER-EM complex. Inhibition of the lipolysis site of Ces1d with WWL229 significantly reduced ER-EM activity, indicating that this site is essential for recognizing hydrophobic aglycones. Furthermore, the inactive substrate GlcMan-4MU was efficiently hydrolyzed in the presence of the Ces1d lipolysis site-specific inhibitor WWL229, demonstrating that the association of the hydrophobic compound WWL229 with the Ces1d lipolysis site contributes to allosteric activation of ER-EM. Our findings provide important insights into the functional regulation of ER-EM complex, a novel therapeutic target for protein misfolding diseases. - Source: PubMed
Publication date: 2026/01/03
Taira AkitoKuribara TaikiHirose MitsuakiTotani Kiichiro - - Source: PubMed
Publication date: 2025/12/15
Chu XuanZhang LigaiXiang ShiqingHuang Yuting - The precise spatial organization of biomolecules on the nanoscale is fundamental to cellular function. However, the molecular mechanisms governing this intricate architecture remain largely unexplored, particularly the role of RNA chemical modifications such as N6-methyladenosine (mA) in orchestrating nanoscale order and functional compartmentalization. Here, we developed a spatially resolved mA proximity labeling (mAPL) technique to directly map the subcellular localization and protein interaction network of mA-modified transcripts. This approach enables in situ mapping of mA sites, deciphers their RNA sequences, and identifies proteins in their immediate nanoscale vicinity. Applying mAPL, we discovered that influenza A virus (IAV) infection triggers the assembly of cytoplasmic, phase-separated inclusion bodies (IBs) that function as specialized, mA-enriched replication hubs. We found that the upregulation of mA on ribosome-related mRNAs, coupled with the enrichment of UGGT1 and SNRNP70 within these condensates, repurposes IBs into efficient factories for viral protein synthesis. Strikingly, we uncovered that SNRNP70 undergoes a spatial reallocation from the nucleus to the endoplasmic reticulum, driven by its strong affinity for the 3' conserved sequence of IAV mRNA. This redistribution is a critical event in nucleating the infection-induced biomolecular condensates. Our work establishes mA-mediated interactions as a key principle driving the formation and function of these virus-host compartments. - Source: PubMed
Publication date: 2025/12/15
He Zhong-DaWang Yi-FanHuang RentangHu YusiYu CongCheng YaoWang Zhi-GangLamb Don CPang Dai-WenLiu Shu-Lin - Protein N-glycosylation contributes to folding and quality control of secretory proteins involved in protein misfolding diseases. A central quality control machinery of nascent glycoproteins in the endoplasmic reticulum (ER) is the calnexin/calreticulin (CNX/CRT) cycle. This cycle assists and checks protein folding by monitoring glycan structure, however how terminally misfolded glycoproteins are discharged from the cycle has remained unclear. Here, we leveraged chemical probes to identify a previously uncharacterized ER endo-α-mannosidase complex (ER-EM) that provides this missing release step. ER-EM selectively cleaves the terminal Glc-Man disaccharide from glucosylated high-mannose glycans only when the glycan is attached to a hydrophobic aglycone─an intrinsic marker of misfolded proteins─thereby converting GlcManGlcNAc to ManGlcNAc glycans that cannot bind CNX/CRT. This activity is allosterically stimulated by hydrophobic ligands and shares the same aglycone preference as the folding sensor UDP-glucose: glycoprotein glucosyltransferase 1 (UGGT1), creating a two-tier surveillance system in which UGGT1 reglucosylates incompletely folded proteins, whereas ER-EM ejects those that fail to mature. Proteomic and native-gel analyses revealed that ER-EM is an ∼ 800 kDa assembly composed of at least carboxylesterase 1D (Ces1d), ERp57 and UGGT1; the lack of activity of recombinant Ces1d alone underscores that the catalytic function arises only through the concerted action of this multisubunit complex. ER-EM therefore acts as a folding-status-dependent triage factor that liberates terminally misfolded glycoproteins from the CNX/CRT cycle and targets them for degradation, adding a critical new branch to the ER quality-control network. - Source: PubMed
Publication date: 2025/10/16
Taira AkitoHirano MakotoKuribara TaikiWatanabe ChieHiraki SatoshiHirose MitsuakiHakki ZaliheWilliams Spencer JIto YukishigeTotani Kiichiro