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Sorting out glycosylation enzymes in the Golgi apparatus

Journal

FEBS LETTERS
Volume 583, Issue 23, Pages 3764-3769

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2009.10.064

Keywords

Golgi apparatus; Glycosylation; COPI; Protein transport; Protein sorting

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The study of glycosylation and glycosylation enzymes has been instrumental for the advancement of Cell Biology. After Neutra and Leblond showed that the Golgi apparatus is the main site of glycosylation, elucidation of oligosaccharide structures by Baenziger and Kornfeld and subsequent mapping of glycosylation enzymes followed. This enabled development of an in vitro transport assay by Rothman and co-workers using glycosylation to monitor intra Golgi transport which, complemented by yeast genetics by Schekman and co-workers, provided much of the fundamental insights and key components of the secretory pathway that we today take for granted. Glycobiology continues to play a key role in Cell Biology and here, we look at the use of glycosylation enzymes to elucidate intra Golgi transport. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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