C-Mannosylation: Previous studies and future research perspectives

Yuki Niwa, Siro Simizu

Research output: Contribution to journalShort surveypeer-review


C-linked glycosylation, one of the protein glycosylations, is a unique type of glycosylation in which an α-mannose is attached to the indole C2 carbon of a tryptophan residue via a C–C linkage and is so named C-mannosylation. C-mannosylation is enzymati-cally catalyzed in the endoplasmic reticulum (ER) lumen, and the N-terminal side Trp residue of the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys (Xaa represents any amino acid) is often C-mannosylated. It has been reported that about 30 proteins are C-mannosylated, and the functions of C-mannosylation are becoming clear. In 2013, C. elegans dumpy-19 (dpy-19) was identified as a C-mannosyltransferase, and we revealed that DPY19L3, one of the human homologs of dpy-19, has similar activity in 2016. In this review, we describe previous studies about C-mannosylation, including our results and future research perspectives.

Original languageEnglish
Pages (from-to)J191-J198 and E231-E238
JournalTrends in Glycoscience and Glycotechnology
Issue number177
Publication statusPublished - 2018 Nov


  • C-mannosylation
  • DPY19
  • Thrombospondin type-1 repeat
  • Tryptophan
  • Type-I cytokine receptor

ASJC Scopus subject areas

  • Biochemistry
  • Organic Chemistry


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