A missense mutation in the catalytic domain of O-GlcNAc transferase links perturbations in protein O-GlcNAcylation to X-linked intellectual disability

FEBS Lett. 2020 Feb;594(4):717-727. doi: 10.1002/1873-3468.13640. Epub 2019 Nov 7.

Abstract

X-linked intellectual disabilities (XLID) are common developmental disorders. The enzyme O-GlcNAc transferase encoded by OGT, a recently discovered XLID gene, attaches O-GlcNAc to nuclear and cytoplasmic proteins. As few missense mutations have been described, it is unclear what the aetiology of the patient phenotypes is. Here, we report the discovery of a missense mutation in the catalytic domain of OGT in an XLID patient. X-ray crystallography reveals that this variant leads to structural rearrangements in the catalytic domain. The mutation reduces in vitro OGT activity on substrate peptides/protein. Mouse embryonic stem cells carrying the mutation reveal reduced O-GlcNAcase (OGA) and global O-GlcNAc levels. These data suggest a direct link between changes in the O-GlcNAcome and intellectual disability observed in patients carrying OGT mutations.

Keywords: O-GlcNAc; OGT; OGlcNAC transferase; XLID; intellectual disability; neurodevelopment.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Catalytic Domain*
  • Cell Line
  • Glycosylation
  • Humans
  • Intellectual Disability / enzymology*
  • Intellectual Disability / genetics*
  • Intellectual Disability / metabolism
  • Mice
  • Models, Molecular
  • Mutation, Missense*
  • N-Acetylglucosaminyltransferases / chemistry*
  • N-Acetylglucosaminyltransferases / genetics*
  • N-Acetylglucosaminyltransferases / metabolism

Substances

  • N-Acetylglucosaminyltransferases
  • O-GlcNAc transferase