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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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O-mannosylation precedes and potentially controls the N-glycosylation of a yeast cell wall glycoprotein.

Secretory proteins in yeast are N- and O-glycosylated while they enter the endoplasmic reticulum. N-glycosylation is initiated by the oligosaccharyl transferase complex and O-mannosylation is initiated by distinct O-mannosyltransferase complexes of the protein mannosyl transferase Pmt1/Pmt2 and Pmt4 families. Using covalently linked cell-wall protein 5 (Ccw5) as a model, we show that the Pmt4 and Pmt1/Pmt2 mannosyltransferases glycosylate different domains of the Ccw5 protein, thereby mannosylating several consecutive serine and threonine residues. In addition, it is shown that O-mannosylation by Pmt4 prevents N-glycosylation by blocking the hydroxy amino acid of the single N-glycosylation site present in Ccw5. These data prove that the O- and N-glycosylation machineries compete for Ccw5; therefore O-mannosylation by Pmt4 precedes N-glycosylation.[1]

References

  1. O-mannosylation precedes and potentially controls the N-glycosylation of a yeast cell wall glycoprotein. Ecker, M., Mrsa, V., Hagen, I., Deutzmann, R., Strahl, S., Tanner, W. EMBO Rep. (2003) [Pubmed]
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