What can yeast tell us about N-linked glycosylation in the Golgi apparatus?
The N-glycans found on eukaryotic glycoproteins occur in a vast range of different structures. A universal N-glycan core is attached to proteins during synthesis in the endoplasmic reticulum, and then diversity is generated as the proteins pass through the Golgi apparatus. Many of the Golgi-localised glycosyltransferases have now been identified in both yeast and mammalian cells, but it is still unclear how these enzymes are integrated into the Golgi and the rest of the cell so as to ensure efficient and specific processing of passing substrates. This review discusses the potential of the yeast system to address these issues.
Munro
S
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Medical Research Council Laboratory of Molecular Biology, Hills Road, CB2 2QH, Cambridge, UK. sean@mrc-lmb.cam.ac.uk
D006031:Glycosylation; D016695:Glycosyltransferases / Q000378:metabolism*; D006056:Golgi Apparatus / Q000201:enzymology / Q000378:metabolism*; D006801:Humans; D008351:Mannans / Q000378:metabolism*; D015394:Molecular Structure; D011134:Polysaccharides / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000502:physiology*; D013379:Substrate Specificity
D008351:Mannans; D011134:Polysaccharides; D016695:Glycosyltransferases