{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Chen S"],"funding":["National Natural Science Foundation of China (National Science Foundation of China)"],"pagination":["5157"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11182771"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(1)"],"pubmed_abstract":["The eukaryotic asparagine (N)-linked glycan is pre-assembled as a fourteen-sugar oligosaccharide on a lipid carrier in the endoplasmic reticulum (ER). Seven sugars are first added to dolichol pyrophosphate (PP-Dol) on the cytoplasmic face of the ER, generating Man5GlcNAc2-PP-Dol (M5GN2-PP-Dol). M5GN2-PP-Dol is then flipped across the bilayer into the lumen by an ER translocator. Genetic studies identified Rft1 as the M5GN2-PP-Dol flippase in vivo but are at odds with biochemical data suggesting Rft1 is dispensable for flipping in vitro. Thus, the question of whether Rft1 plays a direct or an indirect role during M5GN2-PP-Dol translocation has been controversial for over two decades. We describe a completely reconstituted in vitro assay for M5GN2-PP-Dol translocation and demonstrate that pu"],"journal":["Nature communications"],"pubmed_title":["Rft1 catalyzes lipid-linked oligosaccharide translocation across the ER membrane."],"pmcid":["PMC11182771"],"funding_grant_id":["32271342","31971216"],"pubmed_authors":["Li H","Pei CX","Jin C","Gao XD","Xu S","Dean N","Chen S","Wang Y","Liu YS"],"additional_accession":[]},"is_claimable":false,"name":"Rft1 catalyzes lipid-linked oligosaccharide translocation across the ER membrane.","description":"The eukaryotic asparagine (N)-linked glycan is pre-assembled as a fourteen-sugar oligosaccharide on a lipid carrier in the endoplasmic reticulum (ER). Seven sugars are first added to dolichol pyrophosphate (PP-Dol) on the cytoplasmic face of the ER, generating Man5GlcNAc2-PP-Dol (M5GN2-PP-Dol). M5GN2-PP-Dol is then flipped across the bilayer into the lumen by an ER translocator. Genetic studies identified Rft1 as the M5GN2-PP-Dol flippase in vivo but are at odds with biochemical data suggesting Rft1 is dispensable for flipping in vitro. Thus, the question of whether Rft1 plays a direct or an indirect role during M5GN2-PP-Dol translocation has been controversial for over two decades. We describe a completely reconstituted in vitro assay for M5GN2-PP-Dol translocation and demonstrate that pu","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jun","modification":"2025-04-04T12:47:47.804Z","creation":"2025-04-04T12:47:47.804Z"},"accession":"S-EPMC11182771","cross_references":{"pubmed":["38886340"],"doi":["10.1038/s41467-024-48999-3"]}}