FEBS Letters
Volume 583, Issue 23 , Pages 3764-3769, 3 December 2009

Sorting out glycosylation enzymes in the Golgi apparatus

Edited by Alberto Luini

The Research Institute of the McGill University Health Centre, Department of Medicine, McGill University, 687 Pine Avenue West, Montreal, Quebec, Canada H3A 1A1

Received 15 October 2009; accepted 20 October 2009. published online 28 October 2009.

Abstract 

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 anin vitrotransport 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.

Keywords: Golgi apparatus, Glycosylation, COPI, Protein transport, Protein sorting

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PII: S0014-5793(09)00852-7

doi:10.1016/j.febslet.2009.10.064

FEBS Letters
Volume 583, Issue 23 , Pages 3764-3769, 3 December 2009