Ataxin-10 Interacts with O-linked Beta-n-acetylglucosamine Transferase in the Brain.
From: Institute of Physiology, Pestalozzistr. 20, University of Basel, CH-4056 Basel, Switzerland.
The Journal of biological chemistry
- Publish Date: Jul 2006
- ISSN: 0021-9258
- Volume: 281
- Issue: 29
- Pages: 20263-70
- Medium: Print
- Language: English
- Citation (JAMA): März Pia, Stetefeld Jörg, Bendfeldt Kerstin, et al. Ataxin-10 Interacts with O-linked Beta-n-acetylglucosamine Transferase in the Brain.. J. Biol. Chem. Jul 2006;281:20263-70
Abstract
Modification by O-GlcNAc involves a growing number of eucaryotic nuclear and cytosolic proteins. Glycosylation of intracellular proteins is a dynamic process that in several cases competes with and acts as a reciprocal modification system to phosphorylation. O-Linked beta-N-acetylglucosamine transferase (OGT) levels are highest in the brain, and neurodegenerative disorders such as Alzheimer disease have been shown to involve abnormally phosphorylated key proteins, probably as a result of hypoglycosylation. Here, we show that the neurodegenerative disease protein ataxin-10 (Atx-10) is associated with cytoplasmic OGT p110 in the brain. In PC12 cells and pancreas, this association is competed by the shorter OGT p78 splice form, which is down-regulated in brain. Overexpression of Atx-10 in PC12 cells resulted in the reconstitution of the Atx-10-OGT p110 complex and enhanced intracellular glycosylation activity. Moreover, in an in vitro enzyme assay using PC12 cell extracts, Atx-10 increased OGT activity 2-fold. These data indicate that Atx-10 might be essential for the maintenance of a critical intracellular glycosylation level and homeostasis in the brain.
Mesh Headings (Keywords): Acetylglucosamine, Acetylglucosaminidase, Animals, Blotting, Western, Brain, Chromatography, Gel, Cytosol, Glycosylation, Histone Acetyltransferases, Multienzyme Complexes, Nerve Tissue Proteins, PC12 Cells, Pheochromocytoma, Rats, Recombinant Proteins, Transfection, beta-N-Acetylhexosaminidases
Check for Full Text / PubMed Unique Identifier (PMID): 16714295
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