Recognition of a glycosylation substrate by the O-GlcNAc transferase TPR repeats

Karim Rafie, Olawale Raimi, Andrew T. Ferenbach, Vladimir S. Borodkin, Vaibhav Kapuria, Daan M. F. van Aalten (Lead / Corresponding author)

Research output: Contribution to journalArticlepeer-review

40 Citations (Scopus)
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O-linked N-acetylglucosamine (O-GlcNAc) is an essential and dynamic post-translational modification found on hundreds of nucleocytoplasmic proteins in metazoa. Although a single enzyme, O-GlcNAc transferase (OGT), generates the entire cytosolic O-GlcNAc proteome, it is not understood how it recognises its protein substrates, targeting only a fraction of serines/threonines in the metazoan proteome for glycosylation. We describe a trapped complex of human OGT with the C-terminal domain of TAB1, a key innate immunity signalling O-GlcNAc protein, revealing extensive interactions with the tetratricopeptide repeats of OGT. Confirmed by mutagenesis, this interaction suggests that glycosylation substrate specificity is achieved by recognition of a degenerate sequon in the active site combined with an extended conformation C-terminal of the O-GlcNAc target site.
Original languageEnglish
Article number70078
Pages (from-to)1-9
Number of pages9
JournalOpen Biology
Publication statusPublished - 28 Jun 2017


  • Glycosylation
  • Signalling
  • O-GlcNAc
  • O-GlcNAc transferase
  • Substrate recognition


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