Glycobiology Advance Access published online on May 11, 2005
Glycobiology, doi:10.1093/glycob/cwi075
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1 Research Institute, The Hospital for Sick Children
* To whom correspondence should be addressed. Hydrophobic proteins such as integral membrane proteins are difficult to separate, and therefore to study, at a proteomics level. However, the Asn-linked carbohydrates (N-glycans) contained in membrane glycoproteins are important in differentiation, embryogenesis, inflammation, cancer and metastasis, and other vital cellular processes. Thus, the identification of these proteins and their sites of glycosylation in a well characterized model organism is the first step towards understanding the mechanisms by which N-glycans and their associated proteins function in vivo. In this report a proteomics method recently developed by our group was applied to C.elegans extracts to identify 117 hydrophobic N-glycosylated proteins by analysis of 195 glycopeptides containing 199 Asn-linked oligosaccharides. Most of the proteins identified are involved in cell adhesion, metabolism, or the transport of small molecules. In addition, there are 18 proteins for which no function is known or predictable by sequence homologies, and two proteins which were previously predicted to exist only on the basis of genomic sequences in the C. elegans data base. Since N-glycosylation is initiated in the lumen of the endoplasmic reticulum, our data can be used to reassess the previously predicted subcellular localizations of these proteins. As well, the identification of N-glycosylation sites helps to establish the membrane topology of the associated glycoproteins. C.elegans strains are presently available with mutations in 17 of the genes we have identified. The powerful genetic tools available for C.elegans can be used to make other strains with mutations in genes encoding N-glycosylated proteins and thereby determine N-glycan function.
Received February 25, 2005
Revised April 25, 2005
Accepted May 6, 2005
Article
Identification of the Hydrophobic Glycoproteins of Caenorhabditis Elegans
2 Research Institute, The Hospital for Sick Children; Department of Biochemistry, University of Toronto
3 Research Institute, The Hospital for Sick Children; Department of Laboratory Medicine and Pathobiology, University of Toronto
Don J. Mahuran, E-mail: hex{at}sickkids.ca
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