α-Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) and N-methyl-D-aspartate (NMDA) receptors adopt different subunit arrangements

Journal of Biological Chemistry

Volumn 288, Issue 30, 2013, Pages 21987-21998

  Balasuriya, Dilshan ^a   Goetze, Tom A ^a   Barrera, Nelson P ^b   Stewart, Andrew P ^a   Suzuki, Yuki ^c   Edwardson, J Michael ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b PONTIFICIA UNIVERSIDAD CATÓLICA DE CHILE   (Chile)

^c KYOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMPA-RECEPTOR; ATOMIC FORCE; IONOTROPIC GLUTAMATE RECEPTORS; N-METHYL-D-ASPARTATE; NMDA RECEPTOR;

BIOCHEMISTRY; BIOLOGY;

ATOMIC FORCE MICROSCOPY;

AMPA RECEPTOR; AMPA RECEPTOR A1; AMPA RECEPTOR A2; EPITOPE; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; N METHYL DEXTRO ASPARTIC ACID RECEPTOR 1; N METHYL DEXTRO ASPARTIC ACID RECEPTOR 2A; RECEPTOR ANTIBODY; UNCLASSIFIED DRUG;

ANIMAL CELL; ANTIBODY SPECIFICITY; ARTICLE; ATOMIC FORCE MICROSCOPY; CELL SURFACE; CONTROLLED STUDY; FEMALE; MOLECULAR IMAGING; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN ISOLATION; STRUCTURAL HOMOLOGY; STRUCTURE ACTIVITY RELATION;

ATOMIC FORCE MICROSCOPY; CELL SURFACE RECEPTOR; GLUTAMATE RECEPTORS, IONOTROPIC (AMPA, NMDA); PROTEIN COMPLEXES; SINGLE-PARTICLE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; CELL LINE; FLUORESCENT ANTIBODY TECHNIQUE; HUMANS; MICROSCOPY, ATOMIC FORCE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN MULTIMERIZATION; PROTEIN SUBUNITS; RATS; RECEPTORS, AMPA; RECEPTORS, N-METHYL-D-ASPARTATE; TRANSFECTION;

EID: 84881232191     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.469205     Document Type: Article

References (27)

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. Mayer, M. L. (2011) Emerging models of glutamate receptor ion channel structure and function. Structure 19, 1370-1380
3. Mansour, M., Nagarajan, N., Nehring, R. B., Clements, J. D., and Rosenmund, C. (2001) Heteromeric AMPA receptors assemble with a preferred subunit stoichiometry and spatial arrangement. Neuron 32, 841-853
4. Kumar, J., Schuck, P., and Mayer, M. L. (2011) Structure and assembly mechanism for heteromeric kainate receptors. Neuron 71, 319-331
5. Schorge, S., and Colquhoun, D. (2003) Studies of NMDA receptor function and stoichiometry with truncated and tandem subunits. J. Neurosci. 23, 1151-1158
6. Qiu, S., Hua, Y. L., Yang, F., Chen, Y. Z., and Luo, J. H. (2005) Subunit assembly ofN-methyl-D-aspartate receptors analyzed by fluorescence resonance energy transfer. J. Biol. Chem. 280, 24923-24930
7. 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
8. Rambhadran, A., Gonzalez, J., and Jayaraman, V. (2010) Subunit arrangement in N-methyl-D-aspartate (NMDA) receptors. J. Biol. Chem. 285, 15296-15301
9. Salussolia, C. L., Prodromou, M. L., Borker, P., and Wollmuth, L. P. (2011) Arrangement of subunits in functional NMDA receptors. J. Neurosci. 31, 11295-11304
10. Riou, M., Stroebel, D., Edwardson, J. M., and Paoletti, P. (2012) An alternating GluN1-2-1-2 subunit arrangement in mature NMDA receptors. PLoS One 7, e35134
11. Barrera, N. P., Betts, J., You, H., Henderson, R. M., Martin, I. L., Dunn, S. M. J., and Edwardson, J. M. (2008) Atomic force microscopy reveals the stoichiometry and subunit arrangement of the α 43 GABAA receptor. Mol. Pharm. 73, 960-967
12. Barrera, N. P., Herbert, P., Henderson, R. M., Martin, I. L., Edwardson, J. M. (2005) Atomic force microscopy reveals the stoichiometry and subunit arrangement of 5-HT3 receptors. Proc. Natl. Acad. Sci. U.S.A. 102, 12595-12600
13. Barrera, N. P., Ormond, S. J., Henderson, R. M., Murrell-Lagnado, R. D., Edwardson, J. M. (2005) AFM imaging demonstrates that P2X2 receptors are trimers, but that P2X6 receptor subunits do not oligomerize. J. Biol. Chem. 280, 10759-10765
14. Schneider, S. W., Lärmer, J., Henderson, R. M., and Oberleithner, H. (1998) Molecular weights of individual proteins correlate with molecular volumes measured by atomic force microscopy. Pflügers Arch. 435, 362-367
15. Suzuki, Y., Goetze, T. A., Stroebel, D., Balasuriya, D., Yoshimura, S. H., Henderson, R. M., Paoletti, P., Takeyasu, K., and Edwardson, J. M. (2013) Visualization of structural changes accompanying activation of NMDA receptors using fast-scan AFM imaging. J. Biol. Chem. 288, 778-784
16. Neaves, K. J., Cooper, L. P., White, J. H., Carnally, S. M., Dryden, D. T., Edwardson, J. M., and Henderson, R. M. (2009) Atomic force microscopy of the EcoKI type IDNArestriction enzyme bound toDNAshows enzyme dimerisation and DNA looping. Nucleic Acids Res. 37, 2053-2063
17. Scott, D. W. (1979) On optimal and data-based histograms. Biometrika 66, 605-610
18. Welch, B. L. (1947) The generalisation of Student's problems when several different population variances are involved. Biometrika 34, 28-35
19. Farina, A. N., Blain, K. Y., Maruo, T., Kwiatkowski, W., Choe, S., and Nakagawa, T. (2011) Separation of domain contacts is required for heterotetrameric assembly of functional NMDA receptors. J. Neurosci. 31, 3565-3579
20. Carnally, S. M., Johannessen, M., Henderson, R. M., Jackson, M. B., and Edwardson, J. M. (2010) Demonstration of a direct interaction between-1 receptors and acid-sensing ion channels. Biophys. J. 98, 1182-1191
21. Meddows, E., Le Bourdellès, B., Grimwood, S., Wafford, K., Sandhu, S., Whiting, P., and McIlhinney, R. A. J. (2001) Identification of molecular determinants that are important in the assembly of N-methyl-D-aspartate receptors. J. Biol. Chem. 276, 18795-18803
22. Papadakis, M., Hawkins, L. M., and Stephenson, F. A. (2004) Appropriate NR1-NR1 disulfide-linked homodimer formation is requisite for efficient expression of functional, cell surface N-methyl-D-aspartate NR1/NR2 receptors. J. Biol. Chem. 279, 14703-14712
23. Clayton, A., Siebold, C., Gilbert, R. J., Sutton, G. C., Harlos, K., McIlhinney, R. A., Jones, E. Y., and Aricescu, A. R. (2009) Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors. J. Mol. Biol. 392, 1125-1132
24. Jin, R., Singh, S. K., Gu, S., Furukawa, H., Sobolevsky, A. I., Zhou, J., Jin, Y., and Gouaux, E. (2009) Crystal structure and association behaviour of the GluR2 amino-terminal domain. EMBO J. 28, 1812-1923
25. Stroebel, D., Carvalho, S., and Paoletti, P. (2011) Functional evidence for a twisted conformation of the NMDA receptor GluN2A subunit N-terminal domain. Neuropharmacology 60, 151-158
26. Lee, C. H., and Gouaux, E. (2011) Amino-terminal domains of theNMDA receptor are organized as local heterodimers. PLoS One 6, e19180
27. Karakas, E., Simorowski, N., and Furukawa, H. (2011) Subunit arrangement and phenylethanolamine binding in GluN1/GluN2B NMDA receptors. Nature 475, 249-253