Rft1 catalyzes lipid-linked oligosaccharide translocation across the ER membrane

Shuai Chen, Cai-Xia Pei, Si Xu, Hanjie Li, Yi-Shi Liu, Yicheng Wang, Cheng Jin (), Neta Dean () and Xiao-Dong Gao ()
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Shuai Chen: Jiangnan University
Cai-Xia Pei: Chinese Academy of Sciences
Si Xu: Jiangnan University
Hanjie Li: Jiangnan University
Yi-Shi Liu: Jiangnan University
Yicheng Wang: Chinese Academy of Sciences
Cheng Jin: Chinese Academy of Sciences
Neta Dean: Stony Brook University, Stony Brook
Xiao-Dong Gao: Jiangnan University

Nature Communications, 2024, vol. 15, issue 1, 1-10

Abstract: 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 purified Rft1 catalyzes the translocation of M5GN2-PP-Dol across the lipid bilayer. These data, combined with in vitro results demonstrating substrate selectivity and rft1∆ phenotypes, confirm the molecular identity of Rft1 as the M5GN2-PP-Dol ER flippase.

Date: 2024
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DOI: 10.1038/s41467-024-48999-3

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