Translocation of lipid-linked oligosaccharides across the ER membrane requires Rft1 protein

Jonne Helenius, Davis T. W. Ng, Cristina L. Marolda, Peter Walter, Miguel A. Valvano and Markus Aebi ()
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Jonne Helenius: Institute of Microbiology, Swiss Federal Institute of Technology, Zürich
Davis T. W. Ng: Pennsylvania State University
Cristina L. Marolda: University of Western Ontario
Peter Walter: University of California at San Francisco
Miguel A. Valvano: University of Western Ontario
Markus Aebi: Institute of Microbiology, Swiss Federal Institute of Technology, Zürich

Nature, 2002, vol. 415, issue 6870, 447-450

Abstract: Abstract N-linked glycosylation of proteins in eukaryotic cells follows a highly conserved pathway. The tetradecasaccharide substrate (Glc3Man9GlcNAc2) is first assembled at the membrane of the endoplasmic reticulum (ER) as a dolichylpyrophosphate (Dol-PP)-linked intermediate, and then transferred to nascent polypeptide chains in the lumen of the ER1. The assembly of the oligosaccharide starts on the cytoplasmic side of the ER membrane with the synthesis of a Man5GlcNAc2-PP-Dol intermediate. This lipid-linked intermediate is then translocated across the membrane so that the oligosaccharides face the lumen of the ER, where the biosynthesis of Glc3Man9GlcNAc2-PP-Dol continues to completion. The fully assembled oligosaccharide is transferred to selected asparagine residues of target proteins. The transmembrane movement of lipid-linked Man5GlcNAc2 oligosaccharide is of fundamental importance in this biosynthetic pathway, and similar processes involving phospholipids and glycolipids are essential in all types of cells2,3,4. The process is predicted to be catalysed by proteins, termed flippases, which to date have remained elusive2,3,4. Here we provide evidence that yeast RFT1 encodes an evolutionarily conserved protein required for the translocation of Man5GlcNAc2-PP-Dol from the cytoplasmic to the lumenal leaflet of the ER membrane.

Date: 2002
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DOI: 10.1038/415447a

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