Protein O-Glycosylation in Fungi: Diverse Structures and Multiple Functions

@article{Goto2007ProteinOI,
  title={Protein O-Glycosylation in Fungi: Diverse Structures and Multiple Functions},
  author={Masatoshi Goto},
  journal={Bioscience, Biotechnology, and Biochemistry},
  year={2007},
  volume={71},
  pages={1415 - 1427}
}
  • M. Goto
  • Published 23 June 2007
  • Biology
  • Bioscience, Biotechnology, and Biochemistry
Protein glycosylation is essential for eukaryotic cells from yeasts to humans. When compared to N-glycosylation, O-glycosylation is variable in sugar components and the mode of linkages connecting the sugars. In fungi, secretory proteins are commonly mannosylated by protein O-mannosyltransferase (PMT) in the endoplasmic reticulum, and subsequently glycosylated by several glycosyltransferases in the Golgi apparatus to form glycoproteins with diverse O-glycan structures. Protein O-glycosylation… 

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