Ataxin-10 interacts with O-GlcNAc transferase OGT in pancreatic {beta} cells

Journal Article · Fri Nov 11 04:00:00 EST 2005 · Biochemical and Biophysical Research Communications

DOI:https://doi.org/10.1016/j.bbrc.2005.09.026· OSTI ID:20713431

Andrali, Sreenath S ^[1]; Maerz, Pia ^[2]; Oezcan, Sabire ^[1]

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1. Department of Molecular and Cellular Biochemistry, University of Kentucky, College of Medicine, 741 South Limestone Street, Lexington, KY 40536 (United States)
2. Institute for Physiology, University of Basel, 4051 Basel (Switzerland)

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 {beta} cells, which appears to interfere with {beta}-cell function. To obtain a better understanding of the role of O-linked GlcNAc modification in {beta} 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 {beta} cells.

• OSTI ID: 20713431
• Journal Information: Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 1 Vol. 337; ISSN BBRCA9; ISSN 0006-291X
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
GENES
GLUCOSE
HYPERGLYCEMIA
IN VIVO
MICE
MUTATIONS
PANCREAS
PHOSPHORYLATION
PROTEINS