Amino terminal domains of the NMDA receptor are organized as local heterodimers

PLoS ONE

Volumn 6, Issue 4, 2011, Pages

  Lee, Chia Hsueh ^a   Gouaux, Eric ^a  

^a OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; DIMER; HETERODIMER; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PROTEIN GLUA2; PROTEIN GLUK2; PROTEIN GLUN1; PROTEIN GLUN2A; PROTEIN GLUN2B; UNCLASSIFIED DRUG; PROTEIN SUBUNIT;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DISULFIDE BOND; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN BINDING; PROTEIN CROSS LINKING; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; RAT; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS; ANIMAL; CHEMISTRY; GENETICS; METABOLISM; PROTEIN MULTIMERIZATION; PROTEIN TERTIARY STRUCTURE; WESTERN BLOTTING;

RATTUS;

ANIMALS; BLOTTING, WESTERN; MUTAGENESIS, SITE-DIRECTED; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; RATS; RECEPTORS, N-METHYL-D-ASPARTATE;

EID: 79955525364     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0019180     Document Type: Article

References (38)

1. Dingledine R, Borges K, Bowie D, Traynelis SF, (1999) The glutamate receptor ion channels. Pharmacol Rev 51: 7-61.
2. Paoletti P, Neyton J, (2007) NMDA receptor subunits: function and pharmacology. Curr Opin Pharmacol 7: 39-47.
3. Collingridge GL, Olsen RW, Peters J, Spedding M, (2009) A nomenclature for ligand-gated ion channels. Neuropharmacology 56: 2-5.
4. Schorge S, Colquhoun D, (2003) Studies of NMDA receptor function and stoichiometry with truncated and tandem subunits. J Neurosci 23: 1151-1158.
5. Papadakis M, Hawkins LM, Stephenson FA, (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.
6. Qiu S, Hua YL, Yang F, Chen YZ, Luo JH, (2005) Subunit assembly of N-methyl-d-aspartate receptors analyzed by fluorescence resonance energy transfer. J Biol Chem 280: 24923-24930.
7. Furukawa H, Singh SK, Mancusso R, Gouaux E, (2005) Subunit arrangement and function in NMDA receptors. Nature 438: 185-192.
8. Rambhadran A, Gonzalez J, Jayaraman V, (2010) Subunit arrangement in N-methyl-D-aspartate (NMDA) receptors. J Biol Chem 285: 15296-15301.
9. Schuler T, Mesic I, Madry C, Bartholomaus I, Laube B, (2008) Formation of NR1/NR2 and NR1/NR3 heterodimers constitutes the initial step in N-methyl-D-aspartate receptor assembly. J Biol Chem 283: 37-46.
10. Kunishima N, Shimada Y, Tsuji Y, Sato T, Yamamoto M, et al. (2000) Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor. Nature 407: 971-977.
11. Jin R, Singh SK, Gu S, Furukawa H, Sobolevsky AI, et al. (2009) Crystal structure and association behaviour of the GluR2 amino-terminal domain. EMBO J 28: 1812-1823.
12. Kumar J, Schuck P, Jin R, Mayer ML, (2009) The N-terminal domain of GluR6-subtype glutamate receptor ion channels. Nat Struct Mol Biol 16: 631-638.
13. Clayton A, Siebold C, Gilbert RJ, Sutton GC, Harlos K, et al. (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.
14. Sobolevsky AI, Rosconi MP, Gouaux E, (2009) X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor. Nature 462: 745-756.
15. Karakas E, Simorowski N, Furukawa H, (2009) Structure of the zinc-bound amino-terminal domain of the NMDA receptor NR2B subunit. EMBO J 28: 3910-3920.
16. Hansen KB, Furukawa H, Traynelis SF, (2010) Control of assembly and function of glutamate receptors by the amino-terminal domain. Mol Pharmacol 78: 535-549.
17. Gielen M, Siegler Retchless B, Mony L, Johnson JW, Paoletti P, (2009) Mechanism of differential control of NMDA receptor activity by NR2 subunits. Nature 459: 703-707.
18. Yuan H, Hansen KB, Vance KM, Ogden KK, Traynelis SF, (2009) Control of NMDA receptor function by the NR2 subunit amino-terminal domain. J Neurosci 29: 12045-12058.
19. Das U, Kumar J, Mayer ML, Plested AJ, (2010) Domain organization and function in GluK2 subtype kainate receptors. Proc Natl Acad Sci U S A 107: 8463-8468.
20. Bass RB, Butler SL, Chervitz SA, Gloor SL, Falke JJ, (2007) Use of site-directed cysteine and disulfide chemistry to probe protein structure and dynamics: applications to soluble and transmembrane receptors of bacterial chemotaxis. Methods Enzymol 423: 25-51.
21. Careaga CL, Falke JJ, (1992) Structure and dynamics of Escherichia coli chemosensory receptors. Engineered sulfhydryl studies. Biophys J 62: 209-216; discussion 217-209.
22. + modulation of the NMDA receptor. J Neurosci 21: 392-400.
23. Stroebel D, Carvalho S, Paoletti P, (2011) Functional evidence for a twisted conformation of the NMDA receptor GluN2A subunit N-terminal domain. Neuropharmacology 60: 151-158.
24. Qiu S, Zhang XM, Cao JY, Yang W, Yan YG, et al. (2009) An endoplasmic reticulum retention signal located in the extracellular amino-terminal domain of the NR2A subunit of N-Methyl-D-aspartate receptors. J Biol Chem 284: 20285-20298.
25. Han X, Tomitori H, Mizuno S, Higashi K, Full C, et al. (2008) Binding of spermine and ifenprodil to a purified, soluble regulatory domain of the N-methyl-D-aspartate receptor. J Neurochem 107: 1566-1577.
26. Farina AN, Blain KY, Maruo T, Kwiatkowski W, Choe S, et al. (2011) Separation of Domain Contacts Is Required for Heterotetrameric Assembly of Functional NMDA Receptors. J Neurosci 31: 3565-3579.
27. Atlason PT, Garside ML, Meddows E, Whiting P, McIlhinney RA, (2007) N-Methyl-D-aspartate (NMDA) receptor subunit NR1 forms the substrate for oligomeric assembly of the NMDA receptor. J Biol Chem 282: 25299-25307.
28. Inanobe A, Furukawa H, Gouaux E, (2005) Mechanism of partial agonist action at the NR1 subunit of NMDA receptors. Neuron 47: 71-84.
29. Ivanovic A, Reilander H, Laube B, Kuhse J, (1998) Expression and initial characterization of a soluble glycine binding domain of the N-methyl-D-aspartate receptor NR1 subunit. J Biol Chem 273: 19933-19937.
30. Meddows E, Le Bourdelles B, Grimwood S, Wafford K, Sandhu S, et al. (2001) Identification of molecular determinants that are important in the assembly of N-methyl-D-aspartate receptors. J Biol Chem 276: 18795-18803.
31. Moriyoshi K, Masu M, Ishii T, Shigemoto R, Mizuno N, et al. (1991) Molecular cloning and characterization of the rat NMDA receptor. Nature 354: 31-37.
32. Monyer H, Sprengel R, Schoepfer R, Herb A, Higuchi M, et al. (1992) Heteromeric NMDA receptors: molecular and functional distinction of subtypes. Science 256: 1217-1221.
33. Hawkins LM, Prybylowski K, Chang K, Moussan C, Stephenson FA, et al. (2004) Export from the endoplasmic reticulum of assembled N-methyl-d-aspartic acid receptors is controlled by a motif in the c terminus of the NR2 subunit. J Biol Chem 279: 28903-28910.
34. Horak M, Chang K, Wenthold RJ, (2008) Masking of the endoplasmic reticulum retention signals during assembly of the NMDA receptor. J Neurosci 28: 3500-3509.
35. Horak M, Wenthold RJ, (2009) Different roles of C-terminal cassettes in the trafficking of full-length NR1 subunits to the cell surface. J Biol Chem 284: 9683-9691.
36. Puddifoot CA, Chen PE, Schoepfer R, Wyllie DJ, (2009) Pharmacological characterization of recombinant NR1/NR2A NMDA receptors with truncated and deleted carboxy termini expressed in Xenopus laevis oocytes. Br J Pharmacol 156: 509-518.
37. Yang W, Zheng C, Song Q, Yang X, Qiu S, et al. (2007) A three amino acid tail following the TM4 region of the N-methyl-D-aspartate receptor (NR) 2 subunits is sufficient to overcome endoplasmic reticulum retention of NR1-1a subunit. J Biol Chem 282: 9269-9278.
38. Layne E, (1957) [73] Spectrophotometric and turbidimetric methods for measuring proteins Methods in Enzymology: Academic Press pp. 447-454.