title: Sorting out glycosylation enzymes in the Golgi apparatus.
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.
authors.affiliation: The Research Institute of the McGill University Health Centre, Department of Medicine, McGill University, 687 Pine Avenue West, Montreal, Quebec, Canada H3A 1A1. tommy.nilsson@mcgill.ca
authors.forename: Tommy
authors.initials: T
authors.lastname: Nilsson
authors.forename: Catherine E
authors.initials: CE
authors.lastname: Au
authors.forename: John J M
authors.initials: JJ
authors.lastname: Bergeron
mesh_terms: D000818:Animals; D006031:Glycosylation; D006056:Golgi Apparatus / Q000201:enzymology / Q000378:metabolism* / Q000648:ultrastructure; D006801:Humans; D013379:Substrate Specificity