Complex Oligosaccharides Are N-linked to Kv3 Voltage-gated K+ Channels in Rat Brain.
From: Department of Biochemistry and Molecular Biology, Brody School of Medicine at East Carolina University, 600 Moye Boulevard, Greenville, NC 27834, USA.
Biochimica et biophysica acta
- Publish Date: Apr 2007
- ISSN: 0006-3002
- Volume: 1770
- Issue: 4
- Pages: 666-71
- Medium: Print
- Language: English
- Citation (JAMA): Cartwright Tara A, Corey Melissa J, Schwalbe Ruth A, et al. Complex Oligosaccharides Are N-linked to Kv3 Voltage-gated K+ Channels in Rat Brain.. Biochim. Biophys. Acta Apr 2007;1770:666-71
Abstract
Neuronal Kv3 voltage-gated K(+) channels have two absolutely conserved N-glycosylation sites. Here, it is shown that Kv3.1, 3.3, and 3.4 channels are N-glycosylated in rat brain. Digestion of total brain membranes with peptide N glycosidase F (PNGase F) produced faster migrating immunobands than those of undigested membranes. Additionally, partial PNGase F digests showed that both sites are occupied by oligosaccharides. Neuraminidase treatment produced a smaller immunoband shift relative to PNGase F treatment. These results indicate that both sites are highly available and occupied by N-linked oligosaccharides for Kv3.1, 3.3, and 3.4 in rat brain, and furthermore that at least one oligosaccharide is of complex type. Additionally, these results point to an extracytoplasmic S1-S2 linker in Kv3 proteins expressed in native membranes. We suggest that N-glycosylation processing of Kv3 channels is critical for the expression of K(+) currents at the surface of neurons, and perhaps contributes to the pathophysiology of congenital disorders of glycosylation.
Mesh Headings (Keywords): Amino Acid Sequence, Animals, Blotting, Western, Brain, Carbohydrate Conformation, Cell Membrane, Female, Glycosylation, Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase, Molecular Sequence Data, Nerve Tissue Proteins, Neuraminidase, Neurons, Oligosaccharides, Potassium Channels, Voltage-Gated, Protein Conformation, Protein Processing, Post-Translational, Rats, Shaw Potassium Channels
Check for Full Text / PubMed Unique Identifier (PMID): 17197096
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