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Sorting out glycosylation enzymes in the Golgi apparatus
Author(s) -
Nilsson Tommy,
Au Catherine E.,
Bergeron John J.M.
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.10.064
Subject(s) - glycosylation , golgi apparatus , enzyme , microbiology and biotechnology , n linked glycosylation , biochemistry , glycobiology , secretory pathway , biology , chemistry , glycan , cell , glycoprotein
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.