메뉴 건너뛰기




Volumn 587, Issue 24, 2009, Pages 5801-5818

Functional and structural identification of amino acid residues of the P2X2 receptor channel critical for the voltage- and [ATP]-dependent gating

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ARGININE; CYSTEINE; LYSINE; PHENYLALANINE; PURINERGIC P2X2 RECEPTOR; SERINE; THREONINE;

EID: 72549108771     PISSN: 00223751     EISSN: 14697793     Source Type: Journal    
DOI: 10.1113/jphysiol.2009.182824     Document Type: Article
Times cited : (18)

References (51)
  • 1
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
    • Arnold K, Bordoli L, Kopp J, Schwede T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 2006, 22:195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 2
    • 4143136452 scopus 로고    scopus 로고
    • Trimeric architecture of homomeric P2X2 and heteromeric P2X1 + 2 receptor subtypes
    • Aschrafi A, Sadtler S, Niculescu C, Rettinger J, Schmalzing G. Trimeric architecture of homomeric P2X2 and heteromeric P2X1 + 2 receptor subtypes. J Mol Biol 2004, 342:333-343.
    • (2004) J Mol Biol , vol.342 , pp. 333-343
    • Aschrafi, A.1    Sadtler, S.2    Niculescu, C.3    Rettinger, J.4    Schmalzing, G.5
  • 3
    • 15444372454 scopus 로고    scopus 로고
    • Atomic force microscopy imaging demonstrates that P2X2 receptors are trimers but that P2X6 receptor subunits do not oligomerize
    • Barrera NP, Ormond SJ, Henderson RM, Murrell-Lagnado RD, Edwardson JM. Atomic force microscopy imaging demonstrates that P2X2 receptors are trimers but that P2X6 receptor subunits do not oligomerize. J Biol Chem 2005, 280:10759-10765.
    • (2005) J Biol Chem , vol.280 , pp. 10759-10765
    • Barrera, N.P.1    Ormond, S.J.2    Henderson, R.M.3    Murrell-Lagnado, R.D.4    Edwardson, J.M.5
  • 4
    • 33750580538 scopus 로고    scopus 로고
    • Movement of 'gating charge' is coupled to ligand binding in a G-protein-coupled receptor
    • Ben-Chaim Y, Chanda B, Dascal N, Bezanilla F, Parnas I, Parnas H. Movement of 'gating charge' is coupled to ligand binding in a G-protein-coupled receptor. Nature 2006, 444:106-109.
    • (2006) Nature , vol.444 , pp. 106-109
    • Ben-Chaim, Y.1    Chanda, B.2    Dascal, N.3    Bezanilla, F.4    Parnas, I.5    Parnas, H.6
  • 6
    • 0028025001 scopus 로고
    • New structural motif for ligand-gated ion channels defined by an ionotropic ATP receptor
    • Brake AJ, Wagenbach MJ, Julius D. New structural motif for ligand-gated ion channels defined by an ionotropic ATP receptor. Nature 1994, 371:519-523.
    • (1994) Nature , vol.371 , pp. 519-523
    • Brake, A.J.1    Wagenbach, M.J.2    Julius, D.3
  • 7
    • 34250719722 scopus 로고    scopus 로고
    • Purine and pyrimidine receptors
    • Burnstock G. Purine and pyrimidine receptors. Cell Mol Life Sci 2007, 64:1471-1483.
    • (2007) Cell Mol Life Sci , vol.64 , pp. 1471-1483
    • Burnstock, G.1
  • 8
    • 36348952111 scopus 로고    scopus 로고
    • Thr339-to-serine substitution in rat P2X2 receptor second transmembrane domain causes constitutive opening and indicates a gating role for Lys308
    • Cao L, Young MT, Broomhead HE, Fountain SJ, North RA. Thr339-to-serine substitution in rat P2X2 receptor second transmembrane domain causes constitutive opening and indicates a gating role for Lys308. J Neurosci 2007, 27:12916-12923.
    • (2007) J Neurosci , vol.27 , pp. 12916-12923
    • Cao, L.1    Young, M.T.2    Broomhead, H.E.3    Fountain, S.J.4    North, R.A.5
  • 9
    • 0026773023 scopus 로고
    • Pharmacological and kinetic properties of α4β2 neuronal nicotinic acetylcholine receptors expressed in Xenopus oocytes
    • Charnet P, Labarca C, Cohen BN, Davidson N, Lester HA, Pilar G. Pharmacological and kinetic properties of α4β2 neuronal nicotinic acetylcholine receptors expressed in Xenopus oocytes. J Physiol 1992, 450:375-394.
    • (1992) J Physiol , vol.450 , pp. 375-394
    • Charnet, P.1    Labarca, C.2    Cohen, B.N.3    Davidson, N.4    Lester, H.A.5    Pilar, G.6
  • 10
    • 0032940264 scopus 로고    scopus 로고
    • Single channel properties of P2X2 purinoceptors
    • Ding S, Sachs F. Single channel properties of P2X2 purinoceptors. J Gen Physiol 1999, 113:695-720.
    • (1999) J Gen Physiol , vol.113 , pp. 695-720
    • Ding, S.1    Sachs, F.2
  • 12
    • 0032053981 scopus 로고    scopus 로고
    • A domain contributing to the ion channel of ATP-gated P2X2 receptors identified by the substituted cysteine accessibility method
    • Egan TM, Haines WR, Voigt MM. A domain contributing to the ion channel of ATP-gated P2X2 receptors identified by the substituted cysteine accessibility method. J Neurosci 1998, 18:2350-2359.
    • (1998) J Neurosci , vol.18 , pp. 2350-2359
    • Egan, T.M.1    Haines, W.R.2    Voigt, M.M.3
  • 13
    • 0034703055 scopus 로고    scopus 로고
    • The role of positively charged amino acids in ATP recognition by human P2X1 receptors
    • Ennion S, Hagan S, Evans RJ. The role of positively charged amino acids in ATP recognition by human P2X1 receptors. J Biol Chem 2000, 275:29361-29367.
    • (2000) J Biol Chem , vol.275 , pp. 29361-29367
    • Ennion, S.1    Hagan, S.2    Evans, R.J.3
  • 14
    • 0029872192 scopus 로고    scopus 로고
    • Voltage-jump relaxation kinetics for wild-type and chimeric beta subunits of neuronal nicotinic receptors
    • Figl A, Labarca C, Davidson N, Lester HA, Cohen BN. Voltage-jump relaxation kinetics for wild-type and chimeric beta subunits of neuronal nicotinic receptors. J Gen Physiol 1996, 107:369-379.
    • (1996) J Gen Physiol , vol.107 , pp. 369-379
    • Figl, A.1    Labarca, C.2    Davidson, N.3    Lester, H.A.4    Cohen, B.N.5
  • 15
    • 59649098673 scopus 로고    scopus 로고
    • Voltage- and [ATP]-dependent gating of the P2X2 ATP receptor channel
    • Fujiwara Y, Keceli B, Nakajo K, Kubo Y. Voltage- and [ATP]-dependent gating of the P2X2 ATP receptor channel. J Gen Physiol 2009, 133:93-109.
    • (2009) J Gen Physiol , vol.133 , pp. 93-109
    • Fujiwara, Y.1    Keceli, B.2    Nakajo, K.3    Kubo, Y.4
  • 16
    • 4043062112 scopus 로고    scopus 로고
    • Density-dependent changes of the pore properties of the P2X2 receptor channel
    • Fujiwara Y, Kubo Y. Density-dependent changes of the pore properties of the P2X2 receptor channel. J Physiol 2004, 558:31-43.
    • (2004) J Physiol , vol.558 , pp. 31-43
    • Fujiwara, Y.1    Kubo, Y.2
  • 17
    • 33748893444 scopus 로고    scopus 로고
    • Regulation of the desensitization and ion selectivity of ATP-gated P2X2 channels by phosphoinositides
    • Fujiwara Y, Kubo Y. Regulation of the desensitization and ion selectivity of ATP-gated P2X2 channels by phosphoinositides. J Physiol 2006, 576:135-149.
    • (2006) J Physiol , vol.576 , pp. 135-149
    • Fujiwara, Y.1    Kubo, Y.2
  • 20
    • 0035805612 scopus 로고    scopus 로고
    • Amino acid residues involved in gating identified in the first membrane-spanning domain of the rat P2X2 receptor
    • Jiang LH, Rassendren F, Spelta V, Surprenant A, North RA. Amino acid residues involved in gating identified in the first membrane-spanning domain of the rat P2X2 receptor. J Biol Chem 2001, 276:14902-14908.
    • (2001) J Biol Chem , vol.276 , pp. 14902-14908
    • Jiang, L.H.1    Rassendren, F.2    Spelta, V.3    Surprenant, A.4    North, R.A.5
  • 21
    • 0034602169 scopus 로고    scopus 로고
    • Identification of amino acid residues contributing to the ATP-binding site of a purinergic P2X receptor
    • Jiang LH, Rassendren F, Surprenant A, North RA. Identification of amino acid residues contributing to the ATP-binding site of a purinergic P2X receptor. J Biol Chem 2000, 275:34190-34196.
    • (2000) J Biol Chem , vol.275 , pp. 34190-34196
    • Jiang, L.H.1    Rassendren, F.2    Surprenant, A.3    North, R.A.4
  • 22
    • 64149112159 scopus 로고    scopus 로고
    • Functional relevance of aromatic residues in the first transmembrane domain of P2X receptors
    • Jindrichova M, Vavra V, Obsil T, Stojilkovic SS, Zemkova H. Functional relevance of aromatic residues in the first transmembrane domain of P2X receptors. J Neurochem 2009, 109:923-934.
    • (2009) J Neurochem , vol.109 , pp. 923-934
    • Jindrichova, M.1    Vavra, V.2    Obsil, T.3    Stojilkovic, S.S.4    Zemkova, H.5
  • 23
    • 67949117176 scopus 로고    scopus 로고
    • Crystal structure of the ATP-gated P2X4 ion channel in the closed state
    • Kawate T, Michel JC, Birdsong WT, Gouaux E. Crystal structure of the ATP-gated P2X4 ion channel in the closed state. Nature 2009, 460:592-598.
    • (2009) Nature , vol.460 , pp. 592-598
    • Kawate, T.1    Michel, J.C.2    Birdsong, W.T.3    Gouaux, E.4
  • 24
    • 0035287474 scopus 로고    scopus 로고
    • Molecular physiology of P2X receptors and ATP signalling at synapses
    • Khakh BS. Molecular physiology of P2X receptors and ATP signalling at synapses. Nat Rev Neurosci 2001, 2:165-174.
    • (2001) Nat Rev Neurosci , vol.2 , pp. 165-174
    • Khakh, B.S.1
  • 25
    • 14044274324 scopus 로고    scopus 로고
    • Contribution of transmembrane regions to ATP-gated P2X2 channel permeability dynamics
    • Khakh BS, Egan TM. Contribution of transmembrane regions to ATP-gated P2X2 channel permeability dynamics. J Biol Chem 2005, 280:6118-6129.
    • (2005) J Biol Chem , vol.280 , pp. 6118-6129
    • Khakh, B.S.1    Egan, T.M.2
  • 26
    • 23744495788 scopus 로고    scopus 로고
    • Regulation of cell-to-cell communication mediated by astrocytic ATP in the CNS
    • Koizumi S, Fujishita K, Inoue K. Regulation of cell-to-cell communication mediated by astrocytic ATP in the CNS. Purinergic Signal 2005, 1:211-217.
    • (2005) Purinergic Signal , vol.1 , pp. 211-217
    • Koizumi, S.1    Fujishita, K.2    Inoue, K.3
  • 28
    • 63249117189 scopus 로고    scopus 로고
    • Interaction of the aromatics Tyr-72/Trp-288 in the interface of the extracellular and transmembrane domains is essential for proton gating of acid-sensing ion channels
    • Li T, Yang Y, Canessa CM. Interaction of the aromatics Tyr-72/Trp-288 in the interface of the extracellular and transmembrane domains is essential for proton gating of acid-sensing ion channels. J Biol Chem 2009, 284:4689-4694.
    • (2009) J Biol Chem , vol.284 , pp. 4689-4694
    • Li, T.1    Yang, Y.2    Canessa, C.M.3
  • 29
    • 7244261780 scopus 로고    scopus 로고
    • Gain and loss of channel function by alanine substitutions in the transmembrane segments of the rat ATP-gated P2X2 receptor
    • Li Z, Migita K, Samways DS, Voigt MM, Egan TM. Gain and loss of channel function by alanine substitutions in the transmembrane segments of the rat ATP-gated P2X2 receptor. J Neurosci 2004, 24:7378-7386.
    • (2004) J Neurosci , vol.24 , pp. 7378-7386
    • Li, Z.1    Migita, K.2    Samways, D.S.3    Voigt, M.M.4    Egan, T.M.5
  • 30
    • 33846968794 scopus 로고    scopus 로고
    • Identification of an intersubunit cross-link between substituted cysteine residues located in the putative ATP binding site of the P2X1 receptor
    • Marquez-Klaka B, Rettinger J, Bhargava Y, Eisele T, Nicke A. Identification of an intersubunit cross-link between substituted cysteine residues located in the putative ATP binding site of the P2X1 receptor. J Neurosci 2007, 27:1456-1466.
    • (2007) J Neurosci , vol.27 , pp. 1456-1466
    • Marquez-Klaka, B.1    Rettinger, J.2    Bhargava, Y.3    Eisele, T.4    Nicke, A.5
  • 31
    • 59649088809 scopus 로고    scopus 로고
    • Reconstruction of the P2X2 receptor reveals a vase-shaped structure with lateral tunnels above the membrane
    • Mio K, Ogura T, Yamamoto T, Hiroaki Y, Fujiyoshi Y, Kubo Y, Sato C. Reconstruction of the P2X2 receptor reveals a vase-shaped structure with lateral tunnels above the membrane. Structure 2009, 17:266-275.
    • (2009) Structure , vol.17 , pp. 266-275
    • Mio, K.1    Ogura, T.2    Yamamoto, T.3    Hiroaki, Y.4    Fujiyoshi, Y.5    Kubo, Y.6    Sato, C.7
  • 32
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • Miyazawa A, Fujiyoshi Y, Unwin N. Structure and gating mechanism of the acetylcholine receptor pore. Nature 2003, 423:949-955.
    • (2003) Nature , vol.423 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 33
    • 0030757442 scopus 로고    scopus 로고
    • Voltage-dependent gating of ATP-activated channels in PC12 cells
    • Nakazawa K, Liu M, Inoue K, Ohno Y. Voltage-dependent gating of ATP-activated channels in PC12 cells. J Neurophysiol 1997, 78:884-890.
    • (1997) J Neurophysiol , vol.78 , pp. 884-890
    • Nakazawa, K.1    Liu, M.2    Inoue, K.3    Ohno, Y.4
  • 34
    • 12844263080 scopus 로고    scopus 로고
    • Characterization of voltage-dependent gating of P2X2 receptor/channel
    • Nakazawa K, Ohno Y. Characterization of voltage-dependent gating of P2X2 receptor/channel. Eur J Pharmacol 2005, 508:23-30.
    • (2005) Eur J Pharmacol , vol.508 , pp. 23-30
    • Nakazawa, K.1    Ohno, Y.2
  • 36
    • 0036788971 scopus 로고    scopus 로고
    • Molecular physiology of P2X receptors
    • North RA. Molecular physiology of P2X receptors. Physiol Rev 2002, 82:1013-1067.
    • (2002) Physiol Rev , vol.82 , pp. 1013-1067
    • North, R.A.1
  • 37
    • 33747682900 scopus 로고    scopus 로고
    • The metabotropic glutamate G-protein-coupled receptors mGluR3 and mGluR1a are voltage-sensitive
    • Ohana L, Barchad O, Parnas I, Parnas H. The metabotropic glutamate G-protein-coupled receptors mGluR3 and mGluR1a are voltage-sensitive. J Biol Chem 2006, 281:24204-24215.
    • (2006) J Biol Chem , vol.281 , pp. 24204-24215
    • Ohana, L.1    Barchad, O.2    Parnas, I.3    Parnas, H.4
  • 38
    • 0030962404 scopus 로고    scopus 로고
    • Identification of amino acid residues contributing to the pore of a P2X receptor
    • Rassendren F, Buell G, Newbolt A, North RA, Surprenant A. Identification of amino acid residues contributing to the pore of a P2X receptor. EMBO J 1997, 16:3446-3454.
    • (1997) EMBO J , vol.16 , pp. 3446-3454
    • Rassendren, F.1    Buell, G.2    Newbolt, A.3    North, R.A.4    Surprenant, A.5
  • 39
    • 34247120710 scopus 로고    scopus 로고
    • Cysteine substitution mutants give structural insight and identify ATP binding and activation sites at P2X receptors
    • Roberts JA, Evans RJ. Cysteine substitution mutants give structural insight and identify ATP binding and activation sites at P2X receptors. J Neurosci 2007, 27:4072-4082.
    • (2007) J Neurosci , vol.27 , pp. 4072-4082
    • Roberts, J.A.1    Evans, R.J.2
  • 41
    • 41949101239 scopus 로고    scopus 로고
    • On the role of the first transmembrane domain in cation permeability and flux of the ATP-gated P2X2 receptor
    • Samways DS, Migita K, Li Z, Egan TM. On the role of the first transmembrane domain in cation permeability and flux of the ATP-gated P2X2 receptor. J Biol Chem 2008, 283:5110-5117.
    • (2008) J Biol Chem , vol.283 , pp. 5110-5117
    • Samways, D.S.1    Migita, K.2    Li, Z.3    Egan, T.M.4
  • 42
    • 17044400916 scopus 로고    scopus 로고
    • Secondary structure and gating rearrangements of transmembrane segments in rat P2X4 receptor channels
    • Silberberg SD, Chang TH, Swartz KJ. Secondary structure and gating rearrangements of transmembrane segments in rat P2X4 receptor channels. J Gen Physiol 2005, 125:347-359.
    • (2005) J Gen Physiol , vol.125 , pp. 347-359
    • Silberberg, S.D.1    Chang, T.H.2    Swartz, K.J.3
  • 43
    • 34147179943 scopus 로고    scopus 로고
    • Ivermectin interaction with transmembrane helices reveals widespread rearrangements during opening of P2X receptor channels
    • Silberberg SD, Li M, Swartz KJ. Ivermectin interaction with transmembrane helices reveals widespread rearrangements during opening of P2X receptor channels. Neuron 2007, 54:263-274.
    • (2007) Neuron , vol.54 , pp. 263-274
    • Silberberg, S.D.1    Li, M.2    Swartz, K.J.3
  • 44
    • 0032705299 scopus 로고    scopus 로고
    • Contribution of individual subunits to the multimeric P2X2 receptor: estimates based on methanethiosulfonate block at T336C
    • Stoop R, Thomas S, Rassendren F, Kawashima E, Buell G, Surprenant A, North RA. Contribution of individual subunits to the multimeric P2X2 receptor: estimates based on methanethiosulfonate block at T336C. Mol Pharmacol 1999, 56:973-981.
    • (1999) Mol Pharmacol , vol.56 , pp. 973-981
    • Stoop, R.1    Thomas, S.2    Rassendren, F.3    Kawashima, E.4    Buell, G.5    Surprenant, A.6    North, R.A.7
  • 45
    • 67649639047 scopus 로고    scopus 로고
    • Signalling at purinergic P2X receptors
    • Surprenant A, North RA. Signalling at purinergic P2X receptors. Annu Rev Physiol 2008, 71:333-359.
    • (2008) Annu Rev Physiol , vol.71 , pp. 333-359
    • Surprenant, A.1    North, R.A.2
  • 46
    • 0032549559 scopus 로고    scopus 로고
    • Topological analysis of the ATP-gated ionotropic [correction of ionotrophic] P2X2 receptor subunit
    • Torres GE, Egan TM, Voigt MM. Topological analysis of the ATP-gated ionotropic [correction of ionotrophic] P2X2 receptor subunit. FEBS Lett 1998, 425:19-23.
    • (1998) FEBS Lett , vol.425 , pp. 19-23
    • Torres, G.E.1    Egan, T.M.2    Voigt, M.M.3
  • 47
    • 0028030797 scopus 로고
    • A new class of ligand-gated ion channel defined by P2X receptor for extracellular ATP
    • Valera S, Hussy N, Evans RJ, Adami N, North RA, Surprenant A, Buell G. A new class of ligand-gated ion channel defined by P2X receptor for extracellular ATP. Nature 1994, 371:516-519.
    • (1994) Nature , vol.371 , pp. 516-519
    • Valera, S.1    Hussy, N.2    Evans, R.J.3    Adami, N.4    North, R.A.5    Surprenant, A.6    Buell, G.7
  • 48
    • 0032966623 scopus 로고    scopus 로고
    • Selectivity of diadenosine polyphosphates for rat P2X receptor subunits
    • Wildman SS, Brown SG, King BF, Burnstock G. Selectivity of diadenosine polyphosphates for rat P2X receptor subunits. Eur J Pharmacol 1999, 367:119-123.
    • (1999) Eur J Pharmacol , vol.367 , pp. 119-123
    • Wildman, S.S.1    Brown, S.G.2    King, B.F.3    Burnstock, G.4
  • 49
    • 33845940887 scopus 로고    scopus 로고
    • Participation of the Lys313-Ile333 sequence of the purinergic P2X4 receptor in agonist binding and transduction of signals to the channel gate
    • Yan Z, Liang Z, Obsil T, Stojilkovic SS. 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 2006, 281:32649-32659.
    • (2006) J Biol Chem , vol.281 , pp. 32649-32659
    • Yan, Z.1    Liang, Z.2    Obsil, T.3    Stojilkovic, S.S.4
  • 50
    • 34848839244 scopus 로고    scopus 로고
    • Yeast screens show aromatic residues at the end of the sixth helix anchor transient receptor potential channel gate
    • Zhou X, Su Z, Anishkin A, Haynes WJ, Friske EM, Loukin SH, Kung C, Saimi Y. Yeast screens show aromatic residues at the end of the sixth helix anchor transient receptor potential channel gate. Proc Natl Acad Sci U S A 2007, 104:15555-15559.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 15555-15559
    • Zhou, X.1    Su, Z.2    Anishkin, A.3    Haynes, W.J.4    Friske, E.M.5    Loukin, S.H.6    Kung, C.7    Saimi, Y.8
  • 51
    • 0032031676 scopus 로고    scopus 로고
    • Two mechanisms for inward rectification of current flow through the purinoceptor P2X2 class of ATP-gated channels
    • Zhou Z, Hume RI. Two mechanisms for inward rectification of current flow through the purinoceptor P2X2 class of ATP-gated channels. J Physiol 1998, 507:353-364.
    • (1998) J Physiol , vol.507 , pp. 353-364
    • Zhou, Z.1    Hume, R.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.