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Biochim Biophys Acta. 1999 Jan 6;1426(2):309-22.

Asparagine-linked glycosylation in the yeast Golgi.

Author information

1
Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, State University of New York, Stony Brook, NY 11794-5215, USA. ndean@mcbsgi.bio.sunnysb.edu

Abstract

The Golgi complex is the site where the terminal carbohydrate modification of proteins and lipids occurs. These carbohydrates play a variety of biological roles, ranging from the stabilization of glycoprotein structure to the provision of ligands for cell-cell interactions to the regulation of cell surface properties. Progress in our understanding of the biosynthesis and regulation of glycoconjugates has been accelerating at a rapid pace. Recent advances in the field of yeast glycobiology have been particularly impressive. This review focuses on glycosylation of proteins in the Golgi of the yeast Saccharomyces cerevisiae, with emphasis on the candidate mannosyltransferases that participate in the synthesis of N-linked oligosaccharides. Current views on how these enzymes may be regulated and how glycosylation relates on other cellular processes are also discussed.

PMID:
9878803
DOI:
10.1016/s0304-4165(98)00132-9
[Indexed for MEDLINE]

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