AMPA receptor tetramerization is mediated by Q/R editing

Neuron

Volumn 40, Issue 4, 2003, Pages 763-774

  Greger, Ingo H ^a,b   Khatri, Latika ^a   Kong, Xiangpeng ^a   Ziff, Edward B ^a  

^a NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMPA RECEPTOR; GLUTAMATE RECEPTOR; PROTEIN SUBUNIT;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; FEMALE; HUMAN; HUMAN CELL; ION CONDUCTANCE; NERVE CELL PLASTICITY; NONHUMAN; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FUNCTION; RNA EDITING; STOICHIOMETRY; SYNAPTIC TRANSMISSION; TETRAMERIZATION;

EID: 0242573188     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0896-6273(03)00668-8     Document Type: Article

References (53)

1. Abagyan R., Batalov S., Cardozo T., Totrov M., Webber J., Zhou Y. Homology modeling with internal coordinate mechanics. deformation zone mapping and improvements of models via conformational search Proteins Suppl. 1:1997;29-37.
2. Armstrong N., 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.
3. Ayalon G., Stern-Bach Y. Functional assembly of AMPA and kainate receptors is mediated by several discrete protein-protein interactions. Neuron. 31:2001;103-113.
4. Baeuerle P.A., Huttner W.B. Tyrosine sulfation is a trans-Golgi-specific protein modification. J. Cell Biol. 105:1987;2655-2664.
5. Barry M.F., Ziff E.B. Receptor trafficking and the plasticity of excitatory synapses. Curr. Opin. Neurobiol. 12:2002;279-286.
6. Boulter J., Hollmann M., O'Shea-Greenfield A., Hartley M., Deneris E., Maron C., Heinemann S. Molecular cloning and functional expression of glutamate receptor subunit genes. Science. 249:1990;1033-1037.
7. Burnashev N., Villarroel A., Sakmann B. Dimensions and ion selectivity of recombinant AMPA and kainate receptor channels and their dependence on Q/R site residues. J. Physiol. 496:1996;165-173.
8. Chen G.Q., Cui C., Mayer M.L., Gouaux E. Functional characterization of a potassium-selective prokaryotic glutamate receptor. Nature. 402:1999;817-821.
9. Creighton T.E. Proteins. Structures and Molecular Properties:1993;W.H. Freeman, New York.
10. Deutsch C. Potassium channel ontogeny. Annu. Rev. Physiol. 64:2002;19-46.
11. Dingledine R., Borges K., Bowie D., Traynelis S.F. The glutamate receptor ion channels. Pharmacol. Rev. 51:1999;7-61.
12. Doyle D.A., Morais Cabral J., Pfuetzner R.A., Kuo A., Gulbis J.M., Cohen S.L., Chait B.T., MacKinnon R. The structure of the potassium channel. molecular basis of K+ conduction and selectivity Science. 280:1998;69-77.
13. Ellgaard L., Helenius A. Quality control in the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol. 4:2003;181-191.
14. Engelman D.M. Electrostatic fasteners hold the T cell receptor-CD3 complex together. Mol. Cell. 11:2003;5-6.
15. Green W.N. Ion channel assembly. creating structures that function J. Gen. Physiol. 113:1999;163-170.
16. Green W.N., Claudio T. Acetylcholine receptor assembly. subunit folding and oligomerization occur sequentially Cell. 74:1993;57-69.
17. Greger I.H., Khatri L., Ziff E.B. RNA editing at arg607 controls AMPA receptor exit from the endoplasmic reticulum. Neuron. 34:2002;759-772.
18. Hayashi Y., Shi S.H., Esteban J.A., Piccini A., Poncer J.C., Malinow R. Driving AMPA receptors into synapses by LTP and CaMKII. requirement for GluR1 and PDZ domain interaction Science. 287:2000;2262-2267.
19. Heginbotham L., Odessey E., Miller C. Tetrameric stoichiometry of a prokaryotic K+ channel. Biochemistry. 36:1997;10335-10342.
20. Hollmann M., Heinemann S. Cloned glutamate receptors. Annu. Rev. Neurosci. 17:1994;31-108.
21. Jonas P., Burnashev N. Molecular mechanisms controlling calcium entry through AMPA-type glutamate receptor channels. Neuron. 15:1995;987-990.
22. Kuner T., Beck C., Sakmann B., Seeburg P.H. Channel-lining residues of the AMPA receptor M2 segment. structural environment of the Q/R site and identification of the selectivity filter J. Neurosci. 21:2001;4162-4172.
23. Kuner T., Seeburg P.H., Guy H.R. A common architecture for K+ channels and ionotropic glutamate receptors? Trends Neurosci. 26:2003;27-32.
24. Kuusinen A., Abele R., Madden D.R., Keinanen K. Oligomerization and ligand-binding properties of the ectodomain of the alpha-amino-3-hydroxy-5- methyl-4-isoxazole propionic acid receptor subunit GluRD. J. Biol. Chem. 274:1999;28937-28943.
25. Lee M.C., Hamamoto S., Schekman R. Ceramide biosynthesis is required for the formation of the oligomeric H+-ATPase Pma1p in the yeast endoplasmic reticulum. J. Biol. Chem. 277:2002;22395-22401.
26. Leuschner W.D., Hoch W. Subtype-specific assembly of alpha-amino-3- hydroxy-5-methyl-4-isoxazole propionic acid receptor subunits is mediated by their n-terminal domains. J. Biol. Chem. 274:1999;16907-16916.
27. Liu S.Q., Cull-Candy S.G. Synaptic activity at calcium-permeable AMPA receptors induces a switch in receptor subtype. Nature. 405:2000;454-458.
28. MacKinnon R. Pore loops. an emerging theme in ion channel structure Neuron. 14:1995;889-892.
29. Madden D.R. The structure and function of glutamate receptor ion channels. Nat. Rev. Neurosci. 3:2002;91-101.
30. Malinow R. AMPA receptor trafficking and long-term potentiation. Philos. Trans. R. Soc. Lond. B Biol. Sci. 358:2003;707-714.
31. Mano I., Teichberg V.I. A tetrameric subunit stoichiometry for a glutamate receptor-channel complex. Neuroreport. 9:1998;327-331.
32. Mansour M., Nagarajan N., Nehring R.B., Clements J.D., Rosenmund C. Heteromeric AMPA receptors assemble with a preferred subunit stoichiometry and spatial arrangement. Neuron. 32:2001;841-853.
33. Osten P., Khatri L., Perez J.L., Köhr G., Giese G., Daly C., Schulz T.W., Wensky A., Lee L.M., Ziff E.B. Mutagenesis reveals a role for ABP/GRIP binding to GluR2 in synaptic surface accumulation of the AMPA receptor. Neuron. 27:2000;313-325.
34. Ozawa S., Kamiya H., Tsuzuki K. Glutamate receptors in the mammalian central nervous system. Prog. Neurobiol. 54:1998;581-618.
35. Panchenko V.A., Glasser C.R., Mayer M.L. Structural similarities between glutamate receptor channels and K(+) channels examined by scanning mutagenesis. J. Gen. Physiol. 117:2001;345-360.
36. Rosenmund C., Stern-Bach Y., Stevens C.F. The tetrameric structure of a glutamate receptor channel. Science. 280:1998;1596-1599.
37. Safferling M., Tichelaar W., Kummerle G., Jouppila A., Kuusinen A., Keinanen K., Madden D.R. First images of a glutamate receptor ion channel. oligomeric state and molecular dimensions of GluRB homomers Biochemistry. 40:2001;13948-13953.
38. Schägger H., Cramer W.A., von Jagow G. Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal. Biochem. 217:1994;220-230.
39. Seeburg P.H. The role of RNA editing in controlling glutamate receptor channel properties. J. Neurochem. 66:1996;1-5.
40. Seeburg P.H. A-to-I editing. new and old sites, functions, and speculations Neuron. 35:2002;17-20.
41. Seeburg P.H., Single F., Kuner T., Higuchi M., Sprengel R. Genetic manipulation of key determinants of ion flow in glutamate receptor channels in the mouse. Brain Res. 907:2001;233-243.
42. Shi S., Hayashi Y., Esteban J.A., Malinow R. Subunit-specific rules governing AMPA receptor trafficking to synapses in hippocampal pyramidal neurons. Cell. 105:2001;331-343.
43. Sommer B., Köhler M., Sprengel R., Seeburg P.H. RNA editing in brain controls a determinant of ion flow in glutamate-gated channels. Cell. 67:1991;11-19.
44. Sun Y., Olson R., Horning M., Armstrong N., Mayer M., Gouaux E. Mechanism of glutamate receptor desensitization. Nature. 417:2002;245-253.
45. Swanson G.T., Kamboj S.K., Cull-Candy S.G. Single-channel properties of recombinant AMPA receptors depend on RNA editing, splice variation, and subunit composition. J. Neurosci. 17:1997;58-69.
46. Tanaka H., Grooms S.Y., Bennett M.V., Zukin R.S. The AMPAR subunit GluR2. still front and center-stage Brain Res. 886:2000;190-207.
47. Tatu U., Helenius A. Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum. J. Cell Biol. 136:1997;555-565.
48. + channel and binding of channel blockers Biophys. J. 82:2002;1884-1893.
49. Washburn M.S., Numberger M., Zhang S., Dingledine R. Differential dependence on GluR2 expression of three characteristic features of AMPA receptors. J. Neurosci. 17:1997;9393-9406.
50. Wenthold R.J., Petralia R.S., Blahos J. II, Niedzielski A.S. Evidence for multiple AMPA receptor complexes in hippocampal CA1/CA2 neurons. J. Neurosci. 16:1996;1982-1989.
51. Wo Z.G., Oswald R.E. Unraveling the modular design of glutamate-gated ion channels. Trends Neurosci. 18:1995;161-168.
52. Wood M.W., VanDongen H.M., VanDongen A.M. Structural conservation of ion conduction pathways in K channels and glutamate receptors. Proc. Natl. Acad. Sci. USA. 92:1995;4882-4886.
53. Zamanillo D., Sprengel R., Hvalby O., Jensen V., Burnashev N., Rozov A., Kaiser K.M., Koster H.J., Borchardt T., Worley P., et al. Importance of AMPA receptors for hippocampal synaptic plasticity but not for spatial learning. Science. 284:1999;1805-1811.