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Glycobiology Advance Access originally published online on April 20, 2007
Glycobiology 2007 17(10):1031-1044; doi:10.1093/glycob/cwm046
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© The Author 2007. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

REVIEW

Structural views of glycoprotein-fate determination in cells

Koichi Kato1,2,3,4,5 and Yukiko Kamiya2

2 Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Japan
3 Institute for Molecular Science, National Institutes of Natural Sciences, 5-1 Higashiyama Myodaiji, Okazaki 444-8787, Japan
4 GLYENCE Co., Ltd., 406 Nagoya Life Science Incubator, 2-22-8 Chikusa, Chikusa-ku, Nagoya 474-0858, Japan
5 The Glycoscience Institute, Ochanomizu University, 2-1-1 Ohtsuka, Bunkyo-ku, Tokyo 112-8610, Japan

1 To whom correspondence should be addressed; e-mail: kkato{at}phar.nagoya-cu.ac.jp

Received on March 19, 2007; revised on April 13, 2007; accepted on April 13, 2007

Processing of the N-glycans is coupled with the fates of glycoproteins in cells. A series of processing intermediates of high-mannose-type glycans are generated by specific glycosidases and thereby express biological signals recognized by intracellular lectins operating as molecular chaperones, cargo receptors, and ubiquitin ligases. Consequently, these lectins govern the intracellular processes of folding, transport, and degradation of the carrier polypeptides. To understand the underlying mechanisms of glycoprotein-fate determination, structural information on modes of molecular recognition by these lectins and enzymes is undoubtedly important. This article overviews our current knowledge of the structural basis for quality control of glycoproteins in cells.

Key words: glycoproteins / quality control / lectins / glycosidases / ERAD


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