N-glycosylation sites on the nicotinic ACh receptor subunits regulate receptor channel desensitization and conductance

Molecular Brain Research

Volumn 114, Issue 2, 2003, Pages 172-176

  Nishizaki, Tomoyuki ^a  

^a HYOGO COLLEGE OF MEDICINE   (Japan)

Author keywords

Desensitization; N glycosylation; Nicotinic ACh receptor; Patch clamp; Single channel conductance; Two electrode voltage clamp

Indexed keywords

CONCANAVALIN A; LECTIN; NICOTINIC RECEPTOR;

ARTICLE; CELL MEMBRANE CONDUCTANCE; CONTROLLED STUDY; DESENSITIZATION; GLYCOSYLATION; ION PERMEABILITY; MEMBRANE CURRENT; MUTATION; NEUROTRANSMISSION; NONHUMAN; OOCYTE; PRIORITY JOURNAL; VOLTAGE CLAMP; WILD TYPE; XENOPUS;

TORPEDO;

EID: 0038800049     PISSN: 0169328X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0169-328X(03)00171-2     Document Type: Article

References (14)

1. Chazot P.L., Cik M., Stephenson F.A. An investigation into the role of N-glycosylation in the functional expression of a recombinant heteromeric NMDA receptor. Mol. Membr. Biol. 12:1995;331-337.
2. Everts I., Villmann C., Hollmann M. N-Glycosylation is not a prerequisite for glutamate receptor function but Is essential for lectin modulation. Mol. Pharmacol. 52:1997;861-873.
3. Gehle V.M., Sumikawa K. Site-directed mutagenesis of the conserved N-glycosylation site on the nicotinic acetylcholine receptor subunits. Mol. Brain Res. 11:1991;17-25.
4. Gehle V.M., Walcott E.C., Nishizaki T., Sumikawa K. N-glycosylation at the conserved sites ensures the expression of properly folded functional ACh receptors. Mol. Brain Res. 45:1997;219-229.
5. Huganir R.L., Greengard P. Regulation of neurotransmitter receptor desensitization by protein phosphorylation. Neuron. 5:1990;555-567.
6. Kawamoto S., Hattori S., Oiji I., Hamajima K., Mishina M., Okuda K. Ligand-binding properties and N-glycosylation of α1 subunit of the α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate(AMPA)-selective glutamate receptor channel expressed in a baculovirus system. Eur. J. Biochem. 223:1994;665-673.
7. Kawamoto S., Hattori S., Sakimura K., Mishina M., Okuda K. N-linked glycosylation of the α-amino-3-hydroxy-5-methylisoxazole-4-propionate (AMPA)-selective glutamate receptor channel α2 subunit is essential for the acquisition of ligand-binding activity. J. Neurochem. 64:1995;1258-1266.
8. Kawamoto S., Uchino S., Hattori S., Hamajima K., Mishina M., Nakajima-Iijima S., Okuda K. Expression and characterization of the ζ1 subunit of the N-methyl-D-aspartate (NMDA) receptor channel in a baculovirus system. Mol. Brain Res. 30:1995;137-148.
9. Lis H., Sharon N. Protein glycosylation. Structural and functional aspects. Eur. J. Biochem. 218:1993;1-27.
10. Merlie J.P., Sebbane R., Tzartos S., Lindstrom J. Inhibition of glycosylation with tunicamycin blocks assembly of newly synthesized acetylcholine receptor subunits in muscle cells. J. Biol. Chem. 257:1982;2694-2701.
11. Musshoff U., Madeja M., Bloms P., Musch-Nittel K., Speckmann E.J. Tunicamycin-induced inhibition of functional expression of glutamate receptors in Xenopus oocytes. Neurosci. Lett. 147:1992;163-166.
12. Nishizaki T., Sumikawa K. Tunicamycin increases desensitization of junctional and extrajunctional acetylcholine receptors expressed in Xenopus oocytes by a mechanism independent of N-glycosylation blocking. Mol. Pharmacol. 42:1992;152-156.
13. Ramanathan V.K., Hall Z.W. Altered glycosylation sites of the δ subunit of the acetylcholine receptor (AChR) reduce αδ association and receptor assembly. J. Biol. Chem. 274:1999;20513-20520.
14. Sumikawa K., Miledi R. Assembly and N-glycosylation of all ACh receptor subunits are required for their efficient insertion into plasma membranes. Mol. Brain Res. 1989;183-192.