A conserved mechanism for gating in an ionotropic glutamate receptor

Journal of Biological Chemistry

Volumn 288, Issue 26, 2013, Pages 18842-18852

  Moore, Bryn S ^a   Mirshahi, Uyenlinh L ^a   Ebersole, Tonya L ^a   Mirshahi, Tooraj ^a  

^a WEIS CENTER FOR RESEARCH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BASAL ACTIVITIES; CHANNEL ACTIVITY; CHANNELS CONTROL; CRYSTALLOGRAPHIC STRUCTURE; IONOTROPIC GLUTAMATE RECEPTORS; LIGAND BINDING DOMAIN; POTASSIUM CHANNELS; SURFACE EXPRESSION;

LIGANDS; POTASSIUM;

AMINO ACIDS;

6 CYANO 7 NITRO 2,3 QUINOXALINEDIONE; 6,7 DINITRO 2,3 QUINOXALINEDIONE; ALANINE; GLUTAMIC ACID; GLYCINE; IONOTROPIC RECEPTOR; KAINIC ACID; POTASSIUM CHANNEL;

AMINO ACID COMPOSITION; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CELL SURFACE; CHANNEL GATING; CONTROLLED STUDY; EMBRYO; HINGE REGION; HUMAN; HUMAN CELL; LIGAND BINDING; MOLECULAR MECHANICS; NONHUMAN; POROSITY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION;

DESENSITIZATION; GATING; GLUTAMATE; GLUTAMATE RECEPTORS IONOTROPIC (AMPA, NMDA); ION CHANNELS; KAINATE; PHARMACOLOGY;

ALANINE; ANIMALS; CELL MEMBRANE; GLYCINE; HEK293 CELLS; HUMANS; ION CHANNEL GATING; KAINIC ACID; LIGANDS; NEURONS; OOCYTES; PATCH-CLAMP TECHNIQUES; POTASSIUM CHANNELS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, AMPA; RECEPTORS, GLUTAMATE; RECOMBINANT PROTEINS; XENOPUS LAEVIS;

EID: 84879564438     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.465187     Document Type: Article

References (34)

1. Traynelis, S. F., Wollmuth, L. P., McBain, C. J., Menniti, F. S., Vance, K. M., Ogden, K. K., Hansen, K. B., Yuan, H., Myers, S. J., and Dingledine, R. (2010) Glutamate receptor ion channels: structure, regulation, and function. Pharmacol. Rev. 62, 405-496
2. Sobolevsky, A. I., Rosconi, M. P., and Gouaux, E. (2009) X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor. Nature 462, 745-756
3. Armstrong, N., Sun, Y., Chen, G. Q., and Gouaux, E. (1998) Structure of a glutamate receptor ligand-binding core in complex with kainate. Nature 395, 913-917 (Pubitemid 28503434)
4. Armstrong, N., and Gouaux, E. (2000) Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core. Neuron 28, 165-181
5. Bennett, J. A., and Dingledine, R. (1995) Topology profile for a glutamate receptor: three transmembrane domains and a channel-lining reentrant membrane loop. Neuron 14, 373-384
6. Jiang, Y., Lee, A., Chen, J., Cadene, M., Chait, B. T., and MacKinnon, R. (2002) The open pore conformation of potassium channels. Nature 417, 523-526 (Pubitemid 34595913)
7. + channel by pivoted bending of a transmembrane segment. Mol. Cell 10, 469-481
8. Rosenhouse-Dantsker, A., and Logothetis, D. E. (2006) New roles for a key glycine and its neighboring residue in potassium channel gating. Biophys. J. 91, 2860-2873 (Pubitemid 44526476)
9. Rosenhouse-Dantsker, A., and Logothetis, D. E. (2007) Potassium channel gating in the absence of the highly conserved glycine of the inner transmembrane helix. Channels 1, 189-197
10. Kohda, K., Wang, Y., and Yuzaki, M. (2000) Mutation of a glutamate receptor motif reveals its role in gating and δ2 receptor channel properties. Nat. Neurosci. 3, 315-322 (Pubitemid 30185480)
11. Taverna, F., Xiong, Z. G., Brandes, L., Roder, J. C., Salter, M. W., and MacDonald, J. F. (2000) The lurcher mutation of an α-amino-3-hydroxy-5- methyl-4-isoxazolepropionic acid receptor subunit enhances potency of glutamate and converts an antagonist to an agonist. J. Biol. Chem. 275, 8475-8479 (Pubitemid 30180193)
12. Klein, R. M., and Howe, J. R. (2004) Effects of the lurcher mutation on GluR1 desensitization and activation kinetics. J. Neurosci. 24, 4941-4951 (Pubitemid 38697827)
13. Chang, H. R., and Kuo, C. C. (2008) The activation gate and gating mechanism of the NMDA receptor. J. Neurosci. 28, 1546-1556
14. Sobolevsky, A. I., Yelshansky, M. V., and Wollmuth, L. P. (2003) Different gating mechanisms in glutamate receptor and K+channels. J. Neurosci. 23, 7559-7568 (Pubitemid 37034072)
15. + channel determined by construction of multimeric cDNAs. Neuron 9, 861-871
16. Man, H. Y., Lin, J. W., Ju, W. H., Ahmadian, G., Liu, L., Becker, L. E., Sheng, M., and Wang, Y. T. (2000) Regulation of AMPA receptor-mediated synaptic transmission by clathrin-dependent receptor internalization. Neuron 25, 649-662
17. Stern-Bach, Y., Russo, S., Neuman, M., and Rosenmund, C. (1998) A point mutation in the glutamate binding site blocks desensitization of AMPA receptors. Neuron 21, 907-918 (Pubitemid 28498797)
18. Greger, I. H., Khatri, L., and Ziff, E. B. (2002) RNA editing at Arg-607 controls AMPA receptor exit from the endoplasmic reticulum. Neuron 34, 759-772 (Pubitemid 34628738)
19. Mirshahi, T., Robillard, L., Zhang, H., Hébert, T. E., and Logothetis, D. E. (2002) Gβ residues that do not interact with Gα underlie agonist-independent activity of K+channels. J. Biol. Chem. 277, 7348-7355 (Pubitemid 34953130)
20. Schreibmayer, W., Lester, H. A., and Dascal, N. (1994) Voltage clamping of Xenopus laevis oocytes utilizing agarose-cushion electrodes. Pflugers Arch. 426, 453-458 (Pubitemid 24088000)
21. Chen, G. Q., Sun, Y., Jin, R., and Gouaux, E. (1998) Probing the ligand binding domain of the GluR2 receptor by proteolysis and deletion mutagenesis defines domain boundaries and yields a crystallizable construct. Protein Sci. 7, 2623-2630 (Pubitemid 28565704)
22. Schlesinger, F., Tammena, D., Krampfl, K., and Bufler, J. (2005) Two mechanisms of action of the adamantane derivative IEM-1460 at human AMPA-type glutamate receptors. Br. J. Pharmacol. 145, 656-663 (Pubitemid 41032637)
23. Menuz, K., Stroud, R. M., Nicoll, R. A., and Hays, F. A. (2007) TARP auxiliary subunits switch AMPA receptor antagonists into partial agonists. Science 318, 815-817 (Pubitemid 351411776)
24. Zuo, J., De Jager, P. L., Takahashi, K. A., Jiang, W., Linden, D. J., and Heintz, N. (1997) Neurodegeneration in lurcher mice caused by mutation in δ2 glutamate receptor gene. Nature 388, 769-773 (Pubitemid 27375155)
25. Wollmuth, L. P., Kuner, T., Jatzke, C., Seeburg, P. H., Heintz, N., and Zuo, J. (2000) The lurcher mutation identifies δ2 as an AMPA/kainate receptor-like channel that is potentiated by Ca2+. J. Neurosci. 20, 5973-5980 (Pubitemid 30658389)
26. Mayer, M. L. (2011) Emerging models of glutamate receptor ion channel structure and function. Structure 19, 1370-1380
27. Javadpour, M. M., Eilers, M., Groesbeek, M., and Smith, S. O. (1999) Helix packing in polytopic membrane proteins: role of glycine in transmembrane helix association. Biophys. J. 77, 1609-1618 (Pubitemid 29407334)
28. Eilers, M., Shekar, S. C., Shieh, T., Smith, S. O., and Fleming, P. J. (2000) Internal packing of helical membrane proteins. Proc. Natl. Acad. Sci. U.S.A. 97, 5796-5801 (Pubitemid 30367478)
29. Dong, H., Sharma, M., Zhou, H. X., and Cross, T. A. (2012) Glycines: role in α-helical membrane protein structures and a potential indicator of native conformation. Biochemistry 51, 4779-4789
30. Doyle, D. A., Morais Cabral, J., Pfuetzner, R. A., Kuo, A., Gulbis, J. M., Cohen, S. L., Chait, B. T., and MacKinnon, R. (1998) The structure of the potassium channel: molecular basis of K+ conduction and selectivity [see comments]. Science 280, 69-77 (Pubitemid 28169082)
31. Hardman, R. M., Stansfeld, P. J., Dalibalta, S., Sutcliffe, M. J., and Mitcheson, J. S. (2007) Activation gating of hERG potassium channels: S6 glycines are not required as gating hinges. J. Biol. Chem. 282, 31972-31981 (Pubitemid 350106442)
32. Ding, S., Ingleby, L., Ahern, C. A., and Horn, R. (2005) Investigating the putative glycine hinge in Shaker potassium channel. J. Gen. Physiol. 126, 213-226 (Pubitemid 41252783)
33. Deupi, X., Olivella, M., Sanz, A., Dölker, N., Campillo, M., and Pardo, L. (2010) Influence of the G-conformation of Ser and Thr on the structure of transmembrane helices. J. Struct. Biol. 169, 116-123
34. Armstrong, N., Jasti, J., Beich-Frandsen, M., and Gouaux, E. (2006) Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor. Cell 127, 85-97 (Pubitemid 44466635)