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Glycobiology Advance Access originally published online on June 29, 2005
Glycobiology 2005 15(11):1156-1163; doi:10.1093/glycob/cwj002
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© The Author 2005. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oupjournals.org

ALG9 mannosyltransferase is involved in two different steps of lipid-linked oligosaccharide biosynthesis

Christian G. Frank2 and Markus Aebi1

Institute of Microbiology, Department of Biology, Swiss Federal Institute of Technology Zürich, ETH Hönggerberg, CH-8093 Zürich, Switzerland

1 To whom correspondence should be addressed; e-mail: aebi{at}micro.biol.ethz.ch

2 Present address: Department of Biochemistry, University of Wisconsin-Madison, 433 Babcock Drive, Madison, WI 53706-1544

Received on May 26, 2005; revised on June 21, 2005; accepted on June 21, 2005

N-linked protein glycosylation follows a conserved pathway in eukaryotic cells. The assembly of the lipid-linked core oligosaccharide Glc3Man9GlcNAc2, the substrate for the oligosaccharyltransferase (OST), is catalyzed by different glycosyltransferases located at the membrane of the endoplasmic reticulum (ER). The substrate specificity of the different glycosyltransferase guarantees the ordered assembly of the branched oligosaccharide and ensures that only completely assembled oligosaccharide is transferred to protein. The glycosyltransferases involved in this pathway are highly specific, catalyzing the addition of one single hexose unit to the lipid-linked oligosaccharide (LLO). Here, we show that the dolichylphosphomannose-dependent ALG9 mannosyltransferase is the exception from this rule and is required for the addition of two different {alpha}-1,2-linked mannose residues to the LLO. This report completes the list of lumen-oriented glycosyltransferases required for the assembly of the LLO.

Key words: endoplasmic reticulum / dolichol / Saccharomyces cerevisiae


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