UDP-GlcNAc:Glycoprotein N-acetylglucosamine-1-phosphotransferase mediates the initial step in the formation of the methylphosphomannosyl residues on the high mannose oligosaccharides of Dictyostelium discoideum glycoproteins

Yi Qian, Christopher M. West, Stuart Kornfeld

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

Abstract

The Dictyostelium discoideum gene gpt1 encodes a protein XP_638036 with sequence similarity to the α/β subunits of mammalian UDP-GlcNAc:Glycoprotein N-acetylglucosamine-1-phosphotransferase. We now demonstrate that extracts of D. discoideum clones with mutations in this gene transfer GlcNAc-P from UDP-GlcNAc to mannose residues at less than 5% the wild type value. Further, the lysosomal hydrolases of these mutant clones fail to bind to a cation-independent mannose 6-phosphate receptor affinity column, indicating a lack of methylphosphomannosyl residues on the high mannose oligosaccharides of these proteins. We conclude that the gpt1 gene product catalyzes the initial step in the formation of methylphosphomannosyl residues on D. discoideum lysosomal hydrolases.

Original languageEnglish
Pages (from-to)678-681
Number of pages4
JournalBiochemical and Biophysical Research Communications
Volume393
Issue number4
DOIs
StatePublished - Mar 19 2010

Keywords

  • Dictyostelium discoideum
  • GlcNAc-1-phosphotransferase
  • Lysosomal hydrolases
  • Methylphosphomannosyl residues

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