Ataxin-10 interacts with O-GlcNAc transferase OGT in pancreatic β cells

Sreenath S. Andrali, Pia März, Sabire Özcan

Research output: Contribution to journalArticlepeer-review

17 Scopus citations


Several nuclear and cytoplasmic proteins in metazoans are modified by O-linked N-acetylglucosamine (O-GlcNAc). This modification is dynamic and reversible similar to phosphorylation and is catalyzed by the O-linked GlcNAc transferase (OGT). Hyperglycemia has been shown to increase O-GlcNAc levels in pancreatic β cells, which appears to interfere with β-cell function. To obtain a better understanding of the role of O-linked GlcNAc modification in β cells, we have isolated OGT interacting proteins from a cDNA library made from the mouse insulinoma MIN6 cell line. We describe here the identification of Ataxin-10, encoded by the SCA10 (spinocerebellar ataxia type 10) gene as an OGT interacting protein. Mutations in the SCA10 gene cause progressive cerebellar ataxias and seizures. We demonstrate that SCA10 interacts with OGT in vivo and is modified by O-linked glycosylation in MIN6 cells, suggesting a novel role for the Ataxin-10 protein in pancreatic β cells.

Original languageEnglish
Pages (from-to)149-153
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - Nov 11 2005

Bibliographical note

Funding Information:
We thank Jessica Curry and John Hoben for their help with the Cytotrap screen, John Hanover (NIH) for the human cDNA clone. This work was supported by a grant from NIH (R21DK065730 to S.Ö) and a Postdoctoral fellowship from the American Heart Association, Ohio Valley, to S.S.A.


  • Ataxia
  • Ataxin-10
  • Diabetes
  • Glucose
  • MIN6
  • O-GlcNAc
  • OGT
  • SCA10
  • β cells

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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