Measurement of Conformational Changes accompanying Desensitization in an Ionotropic Glutamate Receptor

Cell

Volumn 127, Issue 1, 2006, Pages 85-97

  Armstrong, Neali ^a   Jasti, Jaysankar ^a   Beich Frandsen, Mads ^a   Gouaux, Eric ^a  

^a Och Spine at New York Presbyterian Hospitals   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

IONOTROPIC RECEPTOR;

ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; CRYSTALLOGRAPHY; DESENSITIZATION; HUMAN; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; RECEPTOR BINDING;

EID: 33749059766     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2006.08.037     Document Type: Article

References (41)

1. Akabas M.H., Stauffer D.A., Xu M., and Karlin A. Acetylcholine receptor channel structure probed in cysteine-substitution mutants. Science 258 (1992) 307-310
2. Akabas M.H., Kaufmann C., Archdeacon P., and Karlin A. Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the alpha subunit. Neuron 13 (1994) 919-927
3. Armstrong N., and Gouaux E. Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: Crystal structures of the GluR2 ligand binding core. Neuron 28 (2000) 165-181
4. Armstrong N., Sun Y., Chen G.-Q., and Gouaux E. Structure of a glutamate-receptor ligand-binding core in complex with kainate. Nature 395 (1998) 913-917
5. Armstrong N., Mayer M., and Gouaux E. Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes. Proc. Natl. Acad. Sci. USA 100 (2003) 5736-5741
6. Bowie D., and Smart T.G. Thiocyanate ions selectively antagonize AMPA-evoked responses in Xenopus laevis oocytes microinjected with rat brain mRNA. Br. J. Pharmacol. 109 (1993) 779-787
7. Brunger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J.S., Kuszewski J., Nilges M., Pannu N.S., et al. Crystallography and NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54 (1998) 905-921
8. CCP4 (Collaborative Computational Project, Number 4). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. D50 (1994) 760-763
9. Dingledine R., Borges K., Bowie D., and Traynelis S.F. The glutamate receptor ion channels. Pharmacol. Rev. 51 (1999) 7-61
10. Donevan S.D., and Rogawski M.A. Allosteric regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole-propionate receptors by thiocyanate and cyclothiazide at a common modulatory site distinct from that of 2,3-benzodiazepines. Neuroscience 87 (1998) 615-629
11. Furukawa H., and Gouaux E. Mechanisms of activation, inhibition, and specificity: crystal structures of the NMDA receptor NR1 ligand-binding core. EMBO J. 22 (2003) 2873-2885
12. Hall R.A., Kessler M., Quan A., Ambros-Ingerson J., and Lynch G. Cyclothiazide decreases [3H]AMPA binding to rat brain membranes: evidence that AMPA receptor desensitization increases agonist affinity. Brain Res. 628 (1993) 345-348
13. Honoré T., Davies S.N., Drejer J., Fletcher E.J., Jacobsen P., Lodge D., and Nielsen F.E. Quinoxalinediones: Potent competitive non-NMDA glutamate receptor antagonists. Science 241 (1988) 701-703
14. Horning M.S., and Mayer M.L. Regulation of AMPA receptor gating by ligand binding core dimers. Neuron 41 (2004) 379-388
15. Jin R., Horning M., Mayer M.L., and Gouaux E. Mechanism of activation and selectivity in a ligand-gated ion channel: Structural and functional studies of GluR2 and quisqualate. Biochemistry 41 (2002) 15635-15643
16. Jin R., Banke T.G., Mayer M.L., Traynelis S.F., and Gouaux E. Structural basis for partial agonist action at ionotropic glutamate receptors. Nat. Neurosci. 6 (2003) 803-810
17. Jones T.A., Zou J.-Y., Cowan S.W., and Kjeldgaard. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47 (1991) 110-119
18. Kessler M., Arai A., Quan A., and Lynch G. Effect of cyclothiazide on binding properties of AMPA-type glutamate receptors: lack of competition between cyclothiazide and GYKI 52466. Mol. Pharmacol. 49 (1996) 123-131
19. Koike M., Tsukada S., Tsuzuki K., Kijima H., and Ozawa S. Regulation of kinetic properties of GluR2 AMPA receptor channels by alternative splicing. J. Neurosci. 20 (2000) 2166-2174
20. Krampfl K., Schlesinger F., Zorner A., Kappler M., Dengler R., and Bufler J. Control of kinetic properties of GluR2 flop AMPA-type channels: impact of R/G nuclear editing. Eur. J. Neurosci. 15 (2002) 51-62
21. Kuusinen A., Arvola M., and Keinänen K. Molecular dissection of the agonist binding site of an AMPA receptor. EMBO J. 14 (1995) 6327-6332
22. Madden D.R. The structure and function of glutamate receptor ion channels. Nat. Rev. Neurosci. 3 (2002) 91-101
23. Mayer M. Glutamate receptors at atomic resolution. Nature 440 (2006) 456-462
24. Mayer M.L. Crystal structures of the GluR5 and GluR6 ligand binding cores: molecular mechanisms underlying kainate receptor selectivity. Neuron 45 (2005) 539-552
25. Mayer M.L., and Armstrong N. Structure and function of glutamate receptor ion channels. Annu. Rev. Physiol. 66 (2004) 161-181
26. Miyazawa A., Fujiyoshi Y., and Unwin N. Structure and gating mechanism of the acetylcholine receptor pore. Nature 423 (2003) 949-955
27. Nakagawa T., Cheng Y., Ramm E., Sheng M., and Walz T. Structure and different conformational states of native AMPA receptor complexes. Nature 433 (2005) 545-549
28. Navaza J. AMoRe: An automated package for molecular replacement. Acta Crystallogr. A50 (1994) 157-163
29. Oswald R.E. Ionotropic glutamate receptor recognition and activation. Adv. Protein Chem. 68 (2004) 313-349
30. Partin K.M., Patneau D.K., Winters C.A., Mayer M.L., and Buonanno A. Selective modulation of desensitization at AMPA versus kainate receptors by cyclothiazide and concanavalin A. Neuron 11 (1993) 1069-1082
31. Partin K.M., Fleck M.W., and Mayer M.L. AMPA receptor flip/flop mutants affecting deactivation, desensitization, and modulation by cyclothiazide, aniracetam, and thiocyanate. J. Neurosci. 16 (1996) 6634-6647
32. Pasternack A., Coleman S.K., Jouppila A., Mottershead D.G., Lindfors M., Pasternack M., and Keinanen K. Alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor channels lacking the N-terminal domain. J. Biol. Chem. 277 (2002) 49662-49667 10.1074/jbc.M208349200 Published online October 21, 2001
33. Ren H., Honse Y., Karp B.J., Lipsky R.H., and Peoples R.W. A site in the fourth membrane-associated domain of the N-methyl-D-aspartate receptor regulates desensitization and ion channel gating. J. Biol. Chem. 278 (2003) 276-283
34. Robert A., and Howe J.R. How AMPA receptor desensitization depends on receptor occupancy. J. Neurosci. 23 (2003) 847-858
35. Robert A., Armstrong N., Gouaux J.E., and Howe J.R. AMPA receptor binding cleft mutations that alter affinity, efficacy, and recovery from desensitization. J. Neurosci. 25 (2005) 3752-3762
36. Sommer B., Keinänen K., Verdoorn T.A., Wisden W., Burnashev N., Herb A., Köhler M., Takagi T., Sakmann B., and Seeburg P.H. Flip and flop: A cell-specific functional switch in glutamate-operated channels of the CNS. Science 249 (1990) 1580-1585
37. Stern-Bach Y., Bettler B., Hartley M., Sheppard P.O., O'Hara P.J., and Heinemann S.F. Agonist selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid-binding proteins. Neuron 13 (1994) 1345-1357
38. Stern-Bach Y., Russo S., Neuman M., and Rosenmund C. A point mutation in the glutamate binding site blocks desensitization of AMPA receptors. Neuron 21 (1998) 907-918
39. Sun Y., Olson R., Horning M., Armstrong N., Mayer M., and Gouaux E. Mechanism of glutamate receptor desensitization. Nature 417 (2002) 245-253
40. Yamada K.A., and Tang C.-M. Benzothiadiazines inhibit rapid glutamate receptor desensitization and enhance glutamatergic synaptic currents. J. Neurosci. 13 (1993) 3904-3915
41. Yelshansky M.V., Sobolevsky A.I., Jatzke C., and Wollmuth L.P. Block of AMPA receptor desensitization by a point mutation outside the ligand-binding domain. J. Neurosci. 24 (2004) 4728-4736