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What can yeast tell us about N ‐linked glycosylation in the Golgi apparatus?
Author(s) -
Munro Sean
Publication year - 2001
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/s0014-5793(01)02488-7
Subject(s) - golgi apparatus , endoplasmic reticulum , glycosylation , yeast , glycoprotein , glycan , glycosyltransferase , secretory pathway , microbiology and biotechnology , chemistry , biochemistry , biology , enzyme
The N ‐glycans found on eukaryotic glycoproteins occur in a vast range of different structures. A universal N ‐glycan core is attached to proteins during synthesis in the endoplasmic reticulum, and then diversity is generated as the proteins pass through the Golgi apparatus. Many of the Golgi‐localised glycosyltransferases have now been identified in both yeast and mammalian cells, but it is still unclear how these enzymes are integrated into the Golgi and the rest of the cell so as to ensure efficient and specific processing of passing substrates. This review discusses the potential of the yeast system to address these issues.