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Volumn 113, Issue 17, 2016, Pages 4741-4746

Conductance of P2X4 purinergic receptor is determined by conformational equilibrium in the transmembrane region

Author keywords

Insect cell expression system; Ligand gated ion channels; Membrane proteins; NMR; Purinergic receptors

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALANINE; HIGH DENSITY LIPOPROTEIN; METHIONINE; PURINERGIC P2X4 RECEPTOR; MEMBRANE PROTEIN; PROTEIN BINDING;

EID: 84964703042     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1600519113     Document Type: Article
Times cited : (22)

References (50)
  • 1
    • 84888353305 scopus 로고    scopus 로고
    • Introduction and perspective, historical note
    • Burnstock G (2013) Introduction and perspective, historical note. Front Cell Neurosci 7:227.
    • (2013) Front Cell Neurosci , vol.7 , pp. 227
    • Burnstock, G.1
  • 2
    • 84875222862 scopus 로고    scopus 로고
    • GLYX-13, a NMDA receptor glycine-site functional partial agonist, induces antidepressant-like effects without ketamine-like side effects
    • Burgdorf J, et al. (2013) GLYX-13, a NMDA receptor glycine-site functional partial agonist, induces antidepressant-like effects without ketamine-like side effects. Neuropsychopharmacology 38(5):729-742.
    • (2013) Neuropsychopharmacology , vol.38 , Issue.5 , pp. 729-742
    • Burgdorf, J.1
  • 3
    • 20844441945 scopus 로고    scopus 로고
    • Varenicline: An alpha4beta2 nicotinic receptor partial agonist for smoking cessation
    • Coe JW, et al. (2005) Varenicline: An alpha4beta2 nicotinic receptor partial agonist for smoking cessation. J Med Chem 48(10):3474-3477.
    • (2005) J Med Chem , vol.48 , Issue.10 , pp. 3474-3477
    • Coe, J.W.1
  • 4
    • 0043033172 scopus 로고    scopus 로고
    • Structural basis for partial agonist action at ionotropic glutamate receptors
    • Jin R, Banke TG, Mayer ML, Traynelis SF, Gouaux E (2003) Structural basis for partial agonist action at ionotropic glutamate receptors. Nat Neurosci 6(8):803-810.
    • (2003) Nat Neurosci , vol.6 , Issue.8 , pp. 803-810
    • Jin, R.1    Banke, T.G.2    Mayer, M.L.3    Traynelis, S.F.4    Gouaux, E.5
  • 5
    • 20444408992 scopus 로고    scopus 로고
    • Mechanism of partial agonist action at the NR1 subunit of NMDA receptors
    • Inanobe A, Furukawa H, Gouaux E (2005) Mechanism of partial agonist action at the NR1 subunit of NMDA receptors. Neuron 47(1):71-84.
    • (2005) Neuron , vol.47 , Issue.1 , pp. 71-84
    • Inanobe, A.1    Furukawa, H.2    Gouaux, E.3
  • 6
    • 2342462388 scopus 로고    scopus 로고
    • Structure and function of glutamate receptor ion channels
    • Mayer ML, Armstrong N (2004) Structure and function of glutamate receptor ion channels. Annu Rev Physiol 66:161-181.
    • (2004) Annu Rev Physiol , vol.66 , pp. 161-181
    • Mayer, M.L.1    Armstrong, N.2
  • 7
    • 0022178232 scopus 로고
    • Is there a basis for distinguishing two types of P2-purinoceptor?
    • Burnstock G, Kennedy C (1985) Is there a basis for distinguishing two types of P2-purinoceptor? Gen Pharmacol 16(5):433-440.
    • (1985) Gen Pharmacol , vol.16 , Issue.5 , pp. 433-440
    • Burnstock, G.1    Kennedy, C.2
  • 8
    • 0028030797 scopus 로고
    • A new class of ligand-gated ion channel defined by P2x receptor for extracellular ATP
    • Valera S, et al. (1994) A new class of ligand-gated ion channel defined by P2x receptor for extracellular ATP. Nature 371(6497):516-519.
    • (1994) Nature , vol.371 , Issue.6497 , pp. 516-519
    • Valera, S.1
  • 9
    • 0028025001 scopus 로고
    • New structural motif for ligand-gated ion channels defined by an ionotropic ATP receptor
    • Brake AJ, Wagenbach MJ, Julius D (1994) New structural motif for ligand-gated ion channels defined by an ionotropic ATP receptor. Nature 371(6497):519-523.
    • (1994) Nature , vol.371 , Issue.6497 , pp. 519-523
    • Brake, A.J.1    Wagenbach, M.J.2    Julius, D.3
  • 11
    • 84861526394 scopus 로고    scopus 로고
    • Molecular and functional properties of P2X receptors: Recent progress and persisting challenges
    • Kaczmarek-Hájek K, Lörinczi E, Hausmann R, Nicke A (2012) Molecular and functional properties of P2X receptors: Recent progress and persisting challenges. Purinergic Signal 8(3):375-417.
    • (2012) Purinergic Signal , vol.8 , Issue.3 , pp. 375-417
    • Kaczmarek-Hájek, K.1    Lörinczi, E.2    Hausmann, R.3    Nicke, A.4
  • 12
    • 0031033013 scopus 로고    scopus 로고
    • Characterization of recombinant human P2X4 receptor reveals pharmacological differences to the rat homologue
    • Garcia-Guzman M, Soto F, Gomez-Hernandez JM, Lund PE, Stühmer W (1997) Characterization of recombinant human P2X4 receptor reveals pharmacological differences to the rat homologue. Mol Pharmacol 51(1):109-118.
    • (1997) Mol Pharmacol , vol.51 , Issue.1 , pp. 109-118
    • Garcia-Guzman, M.1    Soto, F.2    Gomez-Hernandez, J.M.3    Lund, P.E.4    Stühmer, W.5
  • 13
    • 0036788971 scopus 로고    scopus 로고
    • Molecular physiology of P2X receptors
    • North RA (2002) Molecular physiology of P2X receptors. Physiol Rev 82(4):1013-1067.
    • (2002) Physiol Rev , vol.82 , Issue.4 , pp. 1013-1067
    • North, R.A.1
  • 14
    • 79955957628 scopus 로고    scopus 로고
    • P2X receptors in health and disease
    • Burnstock G, Kennedy C (2011) P2X receptors in health and disease. Adv Pharmacol 61:333-372.
    • (2011) Adv Pharmacol , vol.61 , pp. 333-372
    • Burnstock, G.1    Kennedy, C.2
  • 16
    • 0033985726 scopus 로고    scopus 로고
    • Functional characterization of the P2X(4) receptor orthologues
    • Jones CA, et al. (2000) Functional characterization of the P2X(4) receptor orthologues. Br J Pharmacol 129(2):388-394.
    • (2000) Br J Pharmacol , vol.129 , Issue.2 , pp. 388-394
    • Jones, C.A.1
  • 17
    • 0032988572 scopus 로고    scopus 로고
    • Pharmacological characterization of recombinant human and rat P2X receptor subtypes
    • Bianchi BR, et al. (1999) Pharmacological characterization of recombinant human and rat P2X receptor subtypes. Eur J Pharmacol 376(1-2):127-138.
    • (1999) Eur J Pharmacol , vol.376 , Issue.1-2 , pp. 127-138
    • Bianchi, B.R.1
  • 18
    • 84860785529 scopus 로고    scopus 로고
    • Molecular mechanism of ATP binding and ion channel activation in P2X receptors
    • Hattori M, Gouaux E (2012) Molecular mechanism of ATP binding and ion channel activation in P2X receptors. Nature 485(7397):207-212.
    • (2012) Nature , vol.485 , Issue.7397 , pp. 207-212
    • Hattori, M.1    Gouaux, E.2
  • 19
    • 67949117176 scopus 로고    scopus 로고
    • Crystal structure of the ATP-gated P2X(4) ion channel in the closed state
    • Kawate T, Michel JC, Birdsong WT, Gouaux E (2009) Crystal structure of the ATP-gated P2X(4) ion channel in the closed state. Nature 460(7255):592-598.
    • (2009) Nature , vol.460 , Issue.7255 , pp. 592-598
    • Kawate, T.1    Michel, J.C.2    Birdsong, W.T.3    Gouaux, E.4
  • 20
    • 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 (1998) A domain contributing to the ion channel of ATP-gated P2X2 receptors identified by the substituted cysteine accessibility method. J Neurosci 18(7):2350-2359.
    • (1998) J Neurosci , vol.18 , Issue.7 , pp. 2350-2359
    • Egan, T.M.1    Haines, W.R.2    Voigt, M.M.3
  • 21
    • 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 (1997) Identification of amino acid residues contributing to the pore of a P2X receptor. EMBO J 16(12):3446-3454.
    • (1997) EMBO J , vol.16 , Issue.12 , pp. 3446-3454
    • Rassendren, F.1    Buell, G.2    Newbolt, A.3    North, R.A.4    Surprenant, A.5
  • 23
    • 84880308941 scopus 로고    scopus 로고
    • Pore-opening mechanism in trimeric P2X receptor channels
    • Li M, Kawate T, Silberberg SD, Swartz KJ (2010) Pore-opening mechanism in trimeric P2X receptor channels. Nat Commun 1:44.
    • (2010) Nat Commun , vol.1 , pp. 44
    • Li, M.1    Kawate, T.2    Silberberg, S.D.3    Swartz, K.J.4
  • 24
    • 77951213527 scopus 로고    scopus 로고
    • Gated access to the pore of a P2X receptor: Structural implications for closed-open transitions
    • Kracun S, Chaptal V, Abramson J, Khakh BS (2010) Gated access to the pore of a P2X receptor: Structural implications for closed-open transitions. J Biol Chem 285(13): 10110-10121.
    • (2010) J Biol Chem , vol.285 , Issue.13 , pp. 10110-10121
    • Kracun, S.1    Chaptal, V.2    Abramson, J.3    Khakh, B.S.4
  • 25
    • 0029955763 scopus 로고    scopus 로고
    • Ionic permeability of, and divalent cation effects on, two ATP-gated cation channels (P2X receptors) expressed inmammalian cells
    • Evans RJ, et al. (1996) Ionic permeability of, and divalent cation effects on, two ATP-gated cation channels (P2X receptors) expressed inmammalian cells. J Physiol 497(Pt 2):413-422.
    • (1996) J Physiol , vol.497 , pp. 413-422
    • Evans, R.J.1
  • 26
    • 0035878883 scopus 로고    scopus 로고
    • Ionic selectivity of native ATP-activated (P2X) receptor channels in dissociated neurones from rat parasympathetic ganglia
    • Liu DM, Adams DJ (2001) Ionic selectivity of native ATP-activated (P2X) receptor channels in dissociated neurones from rat parasympathetic ganglia. J Physiol 534(Pt. 2):423-435.
    • (2001) J Physiol , vol.534 , pp. 423-435
    • Liu, D.M.1    Adams, D.J.2
  • 27
    • 0032089620 scopus 로고    scopus 로고
    • P2X1 and P2X3 receptors form stable trimers: A novel structural motif of ligand-gated ion channels
    • Nicke A, et al. (1998) P2X1 and P2X3 receptors form stable trimers: A novel structural motif of ligand-gated ion channels. EMBO J 17(11):3016-3028.
    • (1998) EMBO J , vol.17 , Issue.11 , pp. 3016-3028
    • Nicke, A.1
  • 28
    • 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 (2004) Trimeric architecture of homomeric P2X2 and heteromeric P2X1+2 receptor subtypes. J Mol Biol 342(1):333-343.
    • (2004) J Mol Biol , vol.342 , Issue.1 , pp. 333-343
    • Aschrafi, A.1    Sadtler, S.2    Niculescu, C.3    Rettinger, J.4    Schmalzing, G.5
  • 29
    • 0043007514 scopus 로고    scopus 로고
    • Self-assembly of discoidal phospholipid bilayer nanoparticles with membrane scaffold proteins
    • Bayburt TH, Grinkova YV, Sligar SG (2002) Self-assembly of discoidal phospholipid bilayer nanoparticles with membrane scaffold proteins. Nano Lett 2(8):853-856.
    • (2002) Nano Lett , vol.2 , Issue.8 , pp. 853-856
    • Bayburt, T.H.1    Grinkova, Y.V.2    Sligar, S.G.3
  • 30
    • 77952355281 scopus 로고    scopus 로고
    • NMR analyses of the interaction between CCR5 and its ligand using functional reconstitution of CCR5 in lipid bilayers
    • Yoshiura C, et al. (2010) NMR analyses of the interaction between CCR5 and its ligand using functional reconstitution of CCR5 in lipid bilayers. J Am Chem Soc 132(19):6768-6777.
    • (2010) J Am Chem Soc , vol.132 , Issue.19 , pp. 6768-6777
    • Yoshiura, C.1
  • 31
    • 0347985761 scopus 로고    scopus 로고
    • Phospholipid phase transitions in homogeneous nanometer scale bilayer discs
    • Shaw AW, McLean MA, Sligar SG (2004) Phospholipid phase transitions in homogeneous nanometer scale bilayer discs. FEBS Lett 556(1-3):260-264.
    • (2004) FEBS Lett , vol.556 , Issue.1-3 , pp. 260-264
    • Shaw, A.W.1    McLean, M.A.2    Sligar, S.G.3
  • 32
    • 84915756175 scopus 로고    scopus 로고
    • Functional dynamics of deuterated ?2-adrenergic receptor in lipid bilayers revealed by NMR spectroscopy
    • Kofuku Y, et al. (2014) Functional dynamics of deuterated ?2-adrenergic receptor in lipid bilayers revealed by NMR spectroscopy. Angew Chem Int Ed Engl 53(49):13376-13379.
    • (2014) Angew Chem Int Ed Engl , vol.53 , Issue.49 , pp. 13376-13379
    • Kofuku, Y.1
  • 33
    • 84872202933 scopus 로고    scopus 로고
    • Functional equilibrium of the KcsA structure revealed by NMR
    • Imai S, et al. (2012) Functional equilibrium of the KcsA structure revealed by NMR. J Biol Chem 287(47):39634-39641.
    • (2012) J Biol Chem , vol.287 , Issue.47 , pp. 39634-39641
    • Imai, S.1
  • 34
    • 84866976467 scopus 로고    scopus 로고
    • Efficacy of the β2-adrenergic receptor is determined by conformational equilibrium in the transmembrane region
    • Kofuku Y, et al. (2012) Efficacy of the β2-adrenergic receptor is determined by conformational equilibrium in the transmembrane region. Nat Commun 3:1045.
    • (2012) Nat Commun , vol.3 , pp. 1045
    • Kofuku, Y.1
  • 35
    • 0036374146 scopus 로고    scopus 로고
    • Cloning and characterization of two novel zebrafish P2X receptor subunits
    • Diaz-Hernandez M, et al. (2002) Cloning and characterization of two novel zebrafish P2X receptor subunits. Biochem Biophys Res Commun 295(4):849-853.
    • (2002) Biochem Biophys Res Commun , vol.295 , Issue.4 , pp. 849-853
    • Diaz-Hernandez, M.1
  • 36
    • 0142247460 scopus 로고    scopus 로고
    • Molecular characterization of the zebrafish P2X receptor subunit gene family
    • Kucenas S, Li Z, Cox JA, Egan TM, Voigt MM (2003) Molecular characterization of the zebrafish P2X receptor subunit gene family. Neuroscience 121(4):935-945.
    • (2003) Neuroscience , vol.121 , Issue.4 , pp. 935-945
    • Kucenas, S.1    Li, Z.2    Cox, J.A.3    Egan, T.M.4    Voigt, M.M.5
  • 37
    • 1642382983 scopus 로고    scopus 로고
    • Directed self-assembly of monodisperse phospholipid bilayer Nanodiscs with controlled size
    • Denisov IG, Grinkova YV, Lazarides AA, Sligar SG (2004) Directed self-assembly of monodisperse phospholipid bilayer Nanodiscs with controlled size. J Am Chem Soc 126(11):3477-3487.
    • (2004) J Am Chem Soc , vol.126 , Issue.11 , pp. 3477-3487
    • Denisov, I.G.1    Grinkova, Y.V.2    Lazarides, A.A.3    Sligar, S.G.4
  • 38
    • 0033366463 scopus 로고    scopus 로고
    • Neuronal P2X transmitter-gated cation channels change their ion selectivity in seconds
    • Khakh BS, Bao XR, Labarca C, Lester HA (1999) Neuronal P2X transmitter-gated cation channels change their ion selectivity in seconds. Nat Neurosci 2(4):322-330.
    • (1999) Nat Neurosci , vol.2 , Issue.4 , pp. 322-330
    • Khakh, B.S.1    Bao, X.R.2    Labarca, C.3    Lester, H.A.4
  • 39
    • 0031866948 scopus 로고    scopus 로고
    • Trinitrophenyl-substituted nucleotides are potent antagonists selective for P2X1, P2X3, and heteromeric P2X2/3 receptors
    • Virginio C, Robertson G, Surprenant A, North RA (1998) Trinitrophenyl-substituted nucleotides are potent antagonists selective for P2X1, P2X3, and heteromeric P2X2/3 receptors. Mol Pharmacol 53(6):969-973.
    • (1998) Mol Pharmacol , vol.53 , Issue.6 , pp. 969-973
    • Virginio, C.1    Robertson, G.2    Surprenant, A.3    North, R.A.4
  • 40
    • 0033664106 scopus 로고    scopus 로고
    • Competitive antagonism of recombinant P2X(2/3) receptors by 2', 3'-O-2,4,6-trinitrophenyl) adenosine 5?-triphosphate (TNP-ATP)
    • Burgard EC, et al. (2000) Competitive antagonism of recombinant P2X(2/3) receptors by 2', 3'-O-(2,4,6-trinitrophenyl) adenosine 5?-triphosphate (TNP-ATP). Mol Pharmacol 58(6):1502-1510.
    • (2000) Mol Pharmacol , vol.58 , Issue.6 , pp. 1502-1510
    • Burgard, E.C.1
  • 41
    • 30144445197 scopus 로고    scopus 로고
    • Inhibition mechanism of the recombinant rat P2X(2) receptor in glial cells by suramin and TNP-ATP
    • Trujillo CA, et al. (2006) Inhibition mechanism of the recombinant rat P2X(2) receptor in glial cells by suramin and TNP-ATP. Biochemistry 45(1):224-233.
    • (2006) Biochemistry , vol.45 , Issue.1 , pp. 224-233
    • Trujillo, C.A.1
  • 42
    • 79958024000 scopus 로고    scopus 로고
    • Ion access pathway to the transmembrane pore in P2X receptor channels
    • Kawate T, Robertson JL, Li M, Silberberg SD, Swartz KJ (2011) Ion access pathway to the transmembrane pore in P2X receptor channels. J Gen Physiol 137(6):579-590.
    • (2011) J Gen Physiol , vol.137 , Issue.6 , pp. 579-590
    • Kawate, T.1    Robertson, J.L.2    Li, M.3    Silberberg, S.D.4    Swartz, K.J.5
  • 43
    • 80051959810 scopus 로고    scopus 로고
    • Preferential use of unobstructed lateral portals as the access route to the pore of human ATP-gated ion channels (P2X receptors
    • Samways DS, Khakh BS, Dutertre S, Egan TM (2011) Preferential use of unobstructed lateral portals as the access route to the pore of human ATP-gated ion channels (P2X receptors). Proc Natl Acad Sci USA 108(33):13800-13805.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.33 , pp. 13800-13805
    • Samways, D.S.1    Khakh, B.S.2    Dutertre, S.3    Egan, T.M.4
  • 44
    • 0027331059 scopus 로고
    • The use of cystathionine gamma-synthase in the production of alpha and chiral beta deuterated amino acids
    • Homer RJ, Kim MS, LeMaster DM (1993) The use of cystathionine gamma-synthase in the production of alpha and chiral beta deuterated amino acids. Anal Biochem 215(2):211-215.
    • (1993) Anal Biochem , vol.215 , Issue.2 , pp. 211-215
    • Homer, R.J.1    Kim, M.S.2    LeMaster, D.M.3
  • 45
    • 37849041010 scopus 로고    scopus 로고
    • A new labeling method for methyl transverse relaxationoptimized spectroscopy NMR spectra of alanine residues
    • Isaacson RL, et al. (2007) A new labeling method for methyl transverse relaxationoptimized spectroscopy NMR spectra of alanine residues. J Am Chem Soc 129(50): 15428-15429.
    • (2007) J Am Chem Soc , vol.129 , Issue.50 , pp. 15428-15429
    • Isaacson, R.L.1
  • 46
    • 0015861774 scopus 로고
    • Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction
    • Cheng Y, Prusoff WH (1973) Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction. Biochem Pharmacol 22(23):3099-3108.
    • (1973) Biochem Pharmacol , vol.22 , Issue.23 , pp. 3099-3108
    • Cheng, Y.1    Prusoff, W.H.2
  • 47
    • 0041930989 scopus 로고    scopus 로고
    • Cross-correlated relaxation enhanced 1H[bond]13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes
    • Tugarinov V, Hwang PM, Ollerenshaw JE, Kay LE (2003) Cross-correlated relaxation enhanced 1H[bond]13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes. J Am Chem Soc 125(34):10420-10428.
    • (2003) J Am Chem Soc , vol.125 , Issue.34 , pp. 10420-10428
    • Tugarinov, V.1    Hwang, P.M.2    Ollerenshaw, J.E.3    Kay, L.E.4
  • 48
    • 0026485457 scopus 로고
    • Subunit stoichiometry of a mammalian K+ channel determined by construction of multimeric cDNAs
    • Liman ER, Tytgat J, Hess P (1992) Subunit stoichiometry of a mammalian K+ channel determined by construction of multimeric cDNAs. Neuron 9(5):861-871.
    • (1992) Neuron , vol.9 , Issue.5 , pp. 861-871
    • Liman, E.R.1    Tytgat, J.2    Hess, P.3
  • 49
    • 84923079683 scopus 로고    scopus 로고
    • Amino acid coevolution reveals three-dimensional structure and functional domains of insect odorant receptors
    • Hopf TA, et al. (2015) Amino acid coevolution reveals three-dimensional structure and functional domains of insect odorant receptors. Nat Commun 6:6077.
    • (2015) Nat Commun , vol.6 , pp. 6077
    • Hopf, T.A.1
  • 50
    • 59649098673 scopus 로고    scopus 로고
    • Voltage-and [ATP]-dependent gating of the P2X(2) ATP receptor channel
    • Fujiwara Y, Keceli B, Nakajo K, Kubo Y (2009) Voltage-and [ATP]-dependent gating of the P2X(2) ATP receptor channel. J Gen Physiol 133(1):93-109.
    • (2009) J Gen Physiol , vol.133 , Issue.1 , pp. 93-109
    • Fujiwara, Y.1    Keceli, B.2    Nakajo, K.3    Kubo, Y.4


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