P2X receptors: dawn of the post-structure era

Trends in Biochemical Sciences

Volumn 35, Issue 2, 2010, Pages 83-90

  Young, Mark T ^a  

^a CARDIFF UNIVERSITY   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ION CHANNEL; PURINERGIC P2X RECEPTOR;

ATOMIC FORCE MICROSCOPY; BINDING SITE; CRYSTAL STRUCTURE; DISULFIDE BOND; ELECTRON MICROSCOPY; HUMAN; MEMBRANE POTENTIAL; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; RECEPTOR BINDING; REVIEW; SIGNAL TRANSDUCTION; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; THREE DIMENSIONAL IMAGING;

ANIMALS; HUMANS; MODELS, MOLECULAR; PROTEIN CONFORMATION; RECEPTORS, PURINERGIC P2; SIGNAL TRANSDUCTION;

DANIO RERIO;

EID: 75749112926     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2009.09.006     Document Type: Review

References (64)

1. Burnstock G. Historical review: ATP as a neurotransmitter. Trends Pharmacol. Sci. 27 (2006) 166-176
2. Surprenant A., and North R.A. Signaling at purinergic P2X receptors. Ann. Rev. Physiol. 71 (2009) 333-359
3. Zimmermann H. Ectonucleotidases: some recent developments and a note on nomenclature. Drug. Dev. Res. 52 (2000) 44-56
4. Sim J.A., et al. Altered hippocampal synaptic potentiation in P2X4 knock-out mice. J. Neurosci. 26 (2006) 9006-9009
5. Finger T.E., et al. ATP signaling is crucial for communication from taste buds to gustatory nerves. Science 310 (2005) 1495-1499
6. Mulryan K., et al. Reduced vas deferens contraction and male infertility in mice lacking P2X1 receptors. Nature 403 (2000) 86-89
7. Yamamoto K., et al. Impaired flow-dependent control of vascular tone and remodeling in P2X4-deficient mice. Nat. Med. 12 (2006) 133-137
8. Brake A.J., et al. New structural motif for ligand-gated ion channels defined by an ionotropic ATP receptor. Nature 371 (1994) 519-523
9. Valera S., et al. A new class of ligand-gated ion channel defined by P2x receptor for extracellular ATP. Nature 371 (1994) 516-519
10. Diaz-Hernandez M., et al. Cloning and characterization of two novel zebrafish P2X receptor subunits. Biochem. Biophys. Res. Commun. 295 (2002) 849-853
11. Agboh K.C., et al. Functional characterization of a P2X receptor from Schistosoma mansoni. J. Biol. Chem. 279 (2004) 41650-41657
12. Fountain S.J., et al. An intracellular P2X receptor required for osmoregulation in Dictyostelium discoideum. Nature 448 (2007) 200-203
13. Fountain S.J., et al. Permeation properties of a P2X receptor in the green algae Ostreococcus tauri. J. Biol. Chem. 283 (2008) 15122-15126
14. Bavan S., et al. A P2X receptor from the tardigrade species Hypsibius dujardini with fast kinetics and sensitivity to zinc and copper. BMC Evol. Biol. 9 (2009) 17
15. Fountain S.J., and Burnstock G. An evolutionary history of P2X receptors. Purinergic. Signal 5 (2009) 269-272
16. North R.A. Molecular physiology of P2X receptors. Physiol. Rev. 82 (2002) 1013-1067
17. Young M.T., et al. Amino acid residues in the P2X7 receptor that mediate differential sensitivity to ATP and BzATP. Mol. Pharmacol. 71 (2007) 92-100
18. Barrera N.P., et al. Atomic force microscopy imaging demonstrates that P2X2 receptors are trimers but that P2X6 receptor subunits do not oligomerize. J. Biol. Chem. 280 (2005) 10759-10765
19. Nicke A., et al. P2X1 and P2X3 receptors form stable trimers: a novel structural motif of ligand-gated ion channels. EMBO J. 17 (1998) 3016-3028
20. Gonzales E.B., et al. Pore architecture and ion sites in acid-sensing ion channels and P2X receptors. Nature 460 (2009) 599-604
21. Jasti J., et al. Structure of acid-sensing ion channel 1 at 1.9 A resolution and low pH. Nature 449 (2007) 316-323
22. Kawate T., et al. Crystal structure of the ATP-gated P2X4 ion channel in the closed state. Nature 460 (2009) 592-598
23. Silberberg S.D., and Swartz K.J. Structural biology: Trimeric ion-channel design. Nature 460 (2009) 580-581
24. Ennion S.J., and Evans R.J. Conserved cysteine residues in the extracellular loop of the human P2X(1) receptor form disulfide bonds and are involved in receptor trafficking to the cell surface. Mol. Pharmacol. 61 (2002) 303-311
25. Clyne J.D., et al. Mutational analysis of the conserved cysteines of the rat P2X2 purinoceptor. J. Neurosci. 22 (2002) 3873-3880
26. Jiang L.H., et al. Identification of amino acid residues contributing to the ATP-binding site of a purinergic P2X receptor. J. Biol. Chem. 275 (2000) 34190-34196
27. Marquez-Klaka B., et al. Identification of an intersubunit cross-link between substituted cysteine residues located in the putative ATP binding site of the P2X1 receptor. J. Neurosci. 27 (2007) 1456-1466
28. Roberts J.A., and Evans R.J. ATP binding at human P2X1 receptors. Contribution of aromatic and basic amino acids revealed using mutagenesis and partial agonists. J. Biol. Chem. 279 (2004) 9043-9055
29. Roberts J.A., and Evans R.J. Contribution of conserved polar glutamine, asparagine and threonine residues and glycosylation to agonist action at human P2X1 receptors for ATP. J. Neurochem. 96 (2006) 843-852
30. Wilkinson W.J., et al. Role of ectodomain lysines in the subunits of the heteromeric P2X2/3 receptor. Mol. Pharmacol. 70 (2006) 1159-1163
31. Nagaya N., et al. An intersubunit zinc binding site in rat P2X2 receptors. J Biol. Chem. 280 (2005) 25982-25993
32. Adriouch S., et al. ADP-ribosylation at R125 gates the P2X7 ion channel by presenting a covalent ligand to its nucleotide binding site. FASEB J. 22 (2008) 861-869
33. Jelinkova I., et al. Identification of P2X(4) receptor transmembrane residues contributing to channel gating and interaction with ivermectin. Pflugers Arch. 456 (2008) 939-950
34. Li M., et al. Gating the pore of P2X receptor channels. Nat. Neurosci. 11 (2008) 883-887
35. Migita K., et al. Polar residues of the second transmembrane domain influence cation permeability of the ATP-gated P2X(2) receptor. J. Biol. Chem. 276 (2001) 30934-30941
36. Rassendren F., et al. Identification of amino acid residues contributing to the pore of a P2X receptor. EMBO J. 16 (1997) 3446-3454
37. Samways D.S., et al. On the role of the first transmembrane domain in cation permeability and flux of the ATP-gated P2X2 receptor. J. Biol. Chem. 283 (2008) 5110-5117
38. Roberts J.A., and Evans R.J. Cysteine substitution mutants give structural insight and identify ATP binding and activation sites at P2X receptors. J. Neurosci. 27 (2007) 4072-4082
39. Yan Z., et al. Participation of the Lys313-Ile333 sequence of the purinergic P2X4 receptor in agonist binding and transduction of signals to the channel gate. J Biol. Chem. 281 (2006) 32649-32659
40. Young M.T., et al. Role of the domain encompassing Arg304 to Ile328 in rat P2X2 receptor conformation revealed by alterations in complex glycosylation at Asn298. Biochem. J. 416 (2008) 137-143
41. Cao L., et al. Thr339-to-serine substitution in rat P2X2 receptor second transmembrane domain causes constitutive opening and indicates a gating role for Lys308. J. Neurosci. 27 (2007) 12916-12923
42. Duckwitz W., et al. P2X5 subunit assembly requires scaffolding by the second transmembrane domain and a conserved aspartate. J. Biol. Chem. 281 (2006) 39561-39572
43. Mio K., et al. Reconstruction of the P2X(2) receptor reveals a vase-shaped structure with lateral tunnels above the membrane. Structure 17 (2009) 266-275
44. Young M.T., et al. Molecular shape, architecture and size of P2X4 receptors determined using fluorescence resonance energy transfer and electron microscopy. J. Biol. Chem. 283 (2008) 26241-26251
45. Evans R. Orthosteric and allosteric binding sites of P2X receptors. Eur. Biophys. J. 38 (2009) 319-327
46. Fischer W., et al. Conserved lysin and arginin residues in the extracellular loop of P2X3 receptors are involved in agonist binding. Eur. J. Pharmacol. 576 (2007) 7-17
47. Yan Z., et al. Molecular determinants of the agonist binding domain of a P2X receptor channel. Mol. Pharmacol. 67 (2005) 1078-1088
48. Guerlet G., et al. Comparative models of P2X2 receptor support inter-subunit ATP-binding sites. Biochem. Biophys. Res. Commun. 375 (2008) 405-409
49. Nakazawa K., et al. Purification and aqueous phase atomic force microscopic observation of recombinant P2X2 receptor. Eur. J. Pharmacol. 518 (2005) 107-110
50. Shinozaki Y., et al. Direct Observation of ATP-Induced Conformational Changes in Single P2X4 Receptors. PLoS Biol. 7 (2009) e103
51. Frank, J. (2006) Three-dimensional electron microscopy of macromolecular assemblies. Oxford University Press, p. 31
52. Mio K., et al. Visualization of the trimeric P2X2 receptor with a crown-capped extracellular domain. Biochem. Biophys. Res. Commun. 337 (2005) 998-1005
53. Eifler N., et al. Functional expression of mammalian receptors and membrane channels in different cells. J. Struct. Biol. 159 (2007) 179-193
54. Radford K.M., et al. Baculovirus expression provides direct evidence for heteromeric assembly of P2X2 and P2X3 receptors. J. Neurosci. 17 (1997) 6529-6533
55. Kawate T., and Gouaux E. Fluorescence-detection size-exclusion chromatography for precrystallization screening of integral membrane proteins. Structure 14 (2006) 673-681
56. Hamilton S.G., et al. ATP in human skin elicits a dose-related pain response which is potentiated under conditions of hyperalgesia. Brain 123 Pt 6 (2000) 1238-1246
57. Tsuda M., et al. P2X4 receptors induced in spinal microglia gate tactile allodynia after nerve injury. Nature 424 (2003) 778-783
58. Chessell I.P., et al. Disruption of the P2X7 purinoceptor gene abolishes chronic inflammatory and neuropathic pain. Pain 114 (2005) 386-396
59. Honore P., et al. A-740003 [N-(1-{[(cyanoimino)(5-quinolinylamino) methyl]amino}-2,2-dimethylpropyl)-2-(3,4-dimethoxyphenyl)acetamide], a novel and selective P2X7 receptor antagonist, dose-dependently reduces neuropathic pain in the rat. J. Pharmacol. Exp. Ther. 319 (2006) 1376-1385
60. Di Virgilio F. Liaisons dangereuses: P2X(7) and the inflammasome. Trends Pharmacol. Sci. 28 (2007) 465-472
61. Ferrari D., et al. The P2X7 receptor: a key player in IL-1 processing and release. J. Immunol. 176 (2006) 3877-3883
62. Solle M., et al. Altered cytokine production in mice lacking P2X(7) receptors. J. Biol. Chem. 276 (2001) 125-132
63. King B.F. Novel P2X7 receptor antagonists ease the pain. Br. J. Pharmacol. 151 (2007) 565-567
64. McInnes, I.B. et al. (2007) Results of a Phase II clinical trial of a novel P2X7 receptor antagonist, AZD9056, in patients with active rheumatiod arthritis (CREATE study). ACR/ARHP Annual Scientific Meeting, presentation 2085 (Abstract)