Plant Physiol.
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Plant Physiology 87:291-295 (1988)
© 1988 American Society of Plant Biologists

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Metabolism and Enzymology

Glycoprotein Processing and Glycoprotein Processing Inhibitors 1

Alan D. Elbein

Department of Biochemistry, University of Texas Health Science Center, San Antonio, Texas 78284

Considerable evidence is now accumulating from both in vivo and in vitro studies that the oligosaccharide chains of the plant N-linked glycoproteins undergo modification or processing reactions after the oligosaccharide has been transferred from its lipid-linked oligosaccharide intermediate to the protein. These processing reactions occur in the endoplasmic reticulum and Golgi apparatus of the cell and involve the removal of certain sugars and the addition of other sugars. While the processing reactions appear to be generally similar to those that occur in animal cells, there are some notable differences, such as the addition of a {beta}-linked xylose to many of the plant glycoproteins. It will be interesting to determine the exact sequence of these reactions and how they are regulated in the cell. Recently, some very useful inhibitors have become available that act on the glycosidases that catalyze the removal of glucose and mannose. These inhibitors cause the accumulation of aberrant oligosaccharide chains on the glycoproteins. Such unusual glycoproteins should be valuable tools for studies on the role of oligosaccharide in glycoprotein function.


1 This work described from the author's laboratory was supported by National Institutes of Health grant AM 21800 and by a grant from the Robert A. Welch Foundation.




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W. Lukowitz, T. C. Nickle, D. W. Meinke, R. L. Last, P. L. Conklin, and C. R. Somerville
Arabidopsis cyt1 mutants are deficient in a mannose-1-phosphate guanylyltransferase and point to a requirement of N-linked glycosylation for cellulose biosynthesis
PNAS, February 27, 2001; 98(5): 2262 - 2267.
[Abstract] [Full Text] [PDF]




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Copyright © 1988 by the American Society of Plant Biologists