C-Mannosylation: Modification on Tryptophan in Cellular Proteins

Yoshito Ihara, Yoko Inai, Midori Ikezaki, In Sook L. Matsui, Shino Manabe, Yukishige Ito

Research output: Chapter in Book/Report/Conference proceedingChapter

15 Citations (Scopus)

Abstract

C-Mannosylation is a unique glycosylation in which an α-mannose attaches to the indole C2 carbon atom of a tryptophan (Trp) residue to produce C-mannosyltryptophan. C-Mannosylation usually occurs at the first Trp in the consensus amino acid sequence Trp-x-x-Trp (W-x-x-W) in proteins through an enzymatic reaction with a specific mannosyltransferase. Recently, Caenorhabditis elegans DPY-19 was identified as a C-mannosyltransferase. Most substrates for C-mannosylation are part of either the thrombospondin type-1 repeat (TSR) superfamily or the type I cytokine receptor family, suggesting a functional role for C-mannosylation in specific substrate proteins. Although the functions of C-mannosylation have not been fully clarified, site-directed mutagenesis of the C-mannosylation potential site in the W-x-x-W motif has revealed it to be important in the folding or targeting of substrate proteins, such as mucins and ADAMTS-like 1, in the cell. By using chemically synthesized C-mannosylated TSR-derived peptides, it was revealed that C-mannosylated peptides could modulate lipopolysaccharide-induced cellular signaling to produce tumor necrosis factor-α. These accumulated findings indicate that C-mannosylation plays important roles in modulating the functions of acceptor proteins in the cell.

Original languageEnglish
Title of host publicationGlycoscience
Subtitle of host publicationBiology and Medicine
PublisherSpringer Japan
Pages1091-1100
Number of pages10
ISBN (Electronic)9784431548416
ISBN (Print)9784431548409
DOIs
Publication statusPublished - 2015 Jan 1
Externally publishedYes

Keywords

  • C-Mannosyl-tryptophan
  • C-Mannosylation
  • Cytokine receptor
  • Thrombospondin

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine(all)

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