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Glycobiology Advance Access published online on June 29, 2005
Glycobiology, 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
Received May 26, 2005
Revised June 21, 2005
Accepted June 21, 2005

Article

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

Christian G. Frank 1 and Markus Aebi 2*

1 Institute of Microbiology, Department of Biology, Swiss Federal Institute if Technology Zürich, ETH Hönggerberg, CH-8093 Zürich, Switzerland; present address: Department of Biochemistry, University of Wisconsin-Madison, 433 Babcock Drive, Madison, WI 53706-1544, USA
2 Institute of Microbiology, Department of Biology, Swiss Federal Institute if Technology Zürich, ETH Hönggerberg, CH-8093 Zürich, Switzerland

* To whom correspondence should be addressed.
Markus Aebi, E-mail: aebi{at}micro.biol.ethz.ch


  Abstract

N-linked protein glycosylation follows a conserved pathway in eukaryotic cells. The assembly of the lipid-linked core oligosaccharide Glc3Man9GlcNAc2, the substrate for the oliogsaccharlytransferase (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. Here, we show that the dolichoylphosphomannose-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 lipid-linked oligosaccharide. This report completes the list of lumen-oriented glycosyltransferases required for the assembly of the lipid-linked oligosaccharide.


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