N-glycosylation is not a prerequisite for glutamate receptor function but is essential for lectin modulation

Molecular Pharmacology

Volumn 52, Issue 5, 1997, Pages 861-873

  Everts, Inga ^a   Villmann, Carmen ^a   Hollmann, Michael ^a  

^a MAX PLANCK INSTITUTE OF EXPERIMENTAL MEDICINE   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA AMINO 3 HYDROXY 5 METHYL 4 ISOXAZOLEPROPIONIC ACID; CONCANAVALIN A; GLUTAMATE RECEPTOR; KAINIC ACID RECEPTOR; LECTIN; N METHYL DEXTRO ASPARTIC ACID; TUNICAMYCIN;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DESENSITIZATION; DRUG BINDING; ION TRANSPORT; LECTIN BINDING SITE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN GLYCOSYLATION; RECEPTOR BINDING;

EID: 0030729835     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: 10.1124/mol.52.5.861     Document Type: Article

References (38)

1. Monaghan, D. T., R. J. Bridges, and C. W. Cotman. The excitatory amino acid receptors: their classes, pharmacology, and distinct properties in the function of the central nervous system. Annu. Rev. Pharmacol. Toxicol. 29:365 (1989).
2. Hollmann, M., and S. Heinemann. Cloned glutamate receptors. Annu. Rev. Neurosci. 17:31-108 (1994).
3. Hollmann, M., C. Maron, and S. Heinemann. N-glycosylation site tagging suggests a 3-transmembrane domain topology for the glutamate receptor GluR1. Neuron 13:1331-1343 (1994).
4. Wo, Z. G. L., and R. E. Oswald. A topological analysis of goldfish kainate receptors predicts 3 transmembrane segments. J. Biol. Chem. 270:2000-2009 (1995).
5. Hullebroeck, M. F., and D. R. Hampson. Characterization of the oligosaccharide side chains on kainate binding proteins and AMPA receptors. Brain Res. 590:187-192 (1992).
6. Lis, H., and N. Sharon. Protein glycosylation: structural and functional aspects. Eur. J. Biochem. 218:1-27 (1993).
7. Mußhoff, U., M. Madeja, P. Bloms, K. Muschnittel, and E. J. Speckmann. Tunicamycin-induced inhibition of functional expression of glutamate receptors in Xenopus oocytes. Neurosci. Lett. 147:163-166 (1992).
8. Chazot, P. L., M. Cik, and F. A. Stephenson. An investigation into the role of N-glycosylation in the functional expression of a recombinant heteromeric NMDA receptor. Mol. Membr. Biol. 12:331-337 (1995).
9. Kawamoto, S., S. Hattori, I. Oiji, K. Hamajima, M. Mishina, and K. Okuda. Ligand binding properties and N-glycosylation of the 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. 223:665-673 (1994).
10. Kawamoto, S., S. Hattori, K. Sakimura, M. Mishina, and K. Okuda. 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. 64:1258-1266 (1995).
11. Kawamoto, S., S. Uchino, S. Hattori, K. Hamajima, M. Mishina, S. Nakajima-Iijima, and K. Okuda. Expression and characterization of the ζ-1 subunit of the N-methyl-D-aspartate (NMDA) receptor channel in a baculovirus system. Mol. Brain Res. 30:137-148 (1995).
12. Sumikawa, K., I. Parker, and R. Miledi. Effect of tunicamycin on the expression of functional brain neurotransmitter receptors and voltage-operated channels in Xenopus oocytes. Mol. Brain Res. 4:191-199 (1988).
13. Mathers, D. D., and P. N. R. Usherwood. Concanavalin A blocks desensitization of glutamate receptors on insect mucle fibers. Nature (Lond.) 259:409-411 (1976).
14. Mayer, M. L., and L. Vyklicky, Jr. Concanavalin A selectively reduces desensitization of mammalian neuronal quisqualate receptors. Proc. Natl. Acad. Sci. USA. 86:1411-1415 (1989).
15. Huettner, J. E. Glutamate receptor channels in rat DRG neurons: activation by kainate and quisqualate and blockade of desensitization by Con A. Neuron 5:255-266 (1990).
16. Wong, L. A., and M. L. Mayer. Differential modulation by cyclothiazide and concanavalin A of desensitization at native α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid-preferring and kainate-preferring glutamate receptors. Mol. Pharmacol. 44:504-510 (1993).
17. Thio, L. L., D. B. Clifford, and C. F. Zorumski. Concanavalin A enhances excitatory synaptic transmission in cultured rat hippocampal neurons. Synapse 13:94-97 (1993).
18. Geoffroy, M., B. Lambolez, L. P. d. Calvalho, J. Rossier, and J. Stinnakre. Concanavalin A potentiates NMDA-evoked responses in the Xenopus oocyte expression system. Eur. J. Pharmacol. 166:355-356 (1989).
19. Yue, K. T., J. F. Macdonald, R. Pekhletski, and D. R. Hampson. Differential effects of lectins on recombinant glutamate receptors. Eur. J. Pharmacol. 291:229-235 (1995).
20. Partin, K. M., D. K. Patneau, C. A. Winters, M. L. Mayer, and A. Buonanno. Selective modulation of desensitization at AMPA versus kainate receptors by cyclothiazide and concanavalin A. Neuron 11:1069-1082 (1993).
21. Partin, K. M., D. Bowie, and M. L. Mayer. Structural determinants of allosteric regulation in alternatively spliced AMPA receptors. Neuron 14: 833-843 (1995).
22. Partin, K. M., D. K. Patneau, and M. L. Mayer. Cyclothiazide differentially modulates desensitization of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor splice variants. Mol. Pharmacol. 46:129-138 (1994).
23. Duksin, D., and W. C. Mahoney. Relationship of the structure and biological activity of the natural homologues of tunicamycin. J. Biol. Chem. 257:3105-3109 (1982).
24. Hume, R. I., R. Dingledine, and S. F. Heinemann. Identification of a site in glutamate receptor subunits that controls calcium permeability. Science (Washington D. C.) 253:1028-1031 (1991).
25. Burnashev, N., H. Monyer, P. H. Seeburg, and B. Sakmann. Divalent ion permeability of AMPA receptor channels is dominated by the edited form of a single subunit. Neuron 8:189-198 (1992).
26. Bettler, B., J. Egebjerg, G. Sharma, G. Pecht, I. Hermans-Borgmeyer, C. Moll, C. F. Stevens, and S. Heinemann. Cloning of a putative glutamate receptor: a low affinity kainate binding subunit. Neuron 8:257-265 (1992).
27. Lomeli, H., W. Wisden, M. Köhler, K. Keinänen, B. Sommer, and P. H. Seeburg. High-affinity kainate and domoate receptors in rat brain. FEBS Lett. 307:139-143 (1992).
28. Sugihara, H., K. Moriyoshi, T. Ishii, M. Masu, and S. Nakanishi. Structures and properties of 7 isoforms of the NMDA receptor generated by alternative splicing. Biochem. Biophys. Res. Commun. 185:826-832 (1992).
29. Hollmann, M., J. Boulter, C. Maron, L. Beasley, J. Sullivan, G. Pecht, and S. Heinemann. Zinc potentiates agonist-induced currents at certain splice variants of the NMDA receptor. Neuron 10:943-954 (1993).
30. Monyer, H., R. Sprengel, R. Schoepfer, A. Herb, M. Higuchi, H. Lomeli, N. Burnashev, B. Sakmann, and P. H. Seeburg. Heteromeric NMDA receptors: molecular and functional distinction of subtypes. Science (Washington D. C.) 256:1217-1221 (1992).
31. Partin, K. M., M. W. Fleck, and M. L. Mayer. AMPA receptor flip/flop mutants affecting deactivation, desensitization, and modulation by cyclothiazide, aniracetam, and thiocyanate. J. Neurosci. 16:6634-6647 (1996).
32. Merlie, J. P., R. Sebbane, S. Tzartos, and J. Lindstrom. Inhibition of glycosylation with tunicamycin blocks assembly of newly synthesized acetylcholine receptor subunits in muscle cells. J. Biol. Chem. 257:2694-2701 (1982).
33. Prives, J. M., and K. Olden. Carbohydrate requirement for expression and stability of acetylcholine receptor on the surface of embryonic muscle cells in culture. Proc. Natl. Acad. Sci. USA 77:5263-5267 (1980).
34. Sumikawa, K., and R. Miledi. Assembly and N-glycosylation of all ACh receptor subunits are required for their efficient insertion into plasma membranes. Mol. Brain Res. 5:183-192 (1989).
35. Schmidt, J. W., and W. A. Catterall. Biosynthesis and processing of the α subunit of the voltage-sensitive sodium channel in rat brain neurons. Cell 46:437-445 (1986).
36. +)-ATPase of chick sensory neurons: studies on biosynthesis and intracellular transport. J. Biol. Chem. 261:1009-1019 (1986).
37. Groves, J. D., and M. J. A. Tanner. Role of N-glycosylation in the expression of human band 3-mediated anion transport. Mol. Membr. Biol. 11: 31-38 (1994).
38. van Koppen, C. J., and N. M. Nathanson. Site-directed mutagenesis of the m2 muscarinic acetylcholine receptor. J. Biol. Chem. 265:20887-20892 (1990).