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Volumn 290, Issue 23, 2015, Pages 14556-14566

Contribution of the juxtatransmembrane intracellular regions to the time course and permeation of ATP-gated P2X7 Receptor Ion Channels

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELL DEATH;

EID: 84930624548     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.642033     Document Type: Article
Times cited : (28)

References (46)
  • 1
    • 84861526394 scopus 로고    scopus 로고
    • Molecular and functional properties of P2X receptors-recent progress and persisting challenges
    • Kaczmarek-Hájek, K., Lörinczi, E., Hausmann, R., and Nicke, A. (2012) Molecular and functional properties of P2X receptors-recent progress and persisting challenges. Purinergic Signal. 8, 375-417
    • (2012) Purinergic Signal. , vol.8 , pp. 375-417
    • Kaczmarek-Hájek, K.1    Lörinczi, E.2    Hausmann, R.3    Nicke, A.4
  • 2
    • 67649639047 scopus 로고    scopus 로고
    • Signaling at purinergic P2X receptors
    • Surprenant, A., and North, R. A. (2009) Signaling at purinergic P2X receptors. Annu. Rev. Physiol. 71, 333-359
    • (2009) Annu. Rev. Physiol. , vol.71 , pp. 333-359
    • Surprenant, A.1    North, R.A.2
  • 4
    • 84871504004 scopus 로고    scopus 로고
    • Moving through the gate in ATP-activated P2X receptors
    • Jiang, R., Taly, A., and Grutter, T. (2013) Moving through the gate in ATP-activated P2X receptors. Trends Biochem. Sci. 38, 20-29
    • (2013) Trends Biochem. Sci. , vol.38 , pp. 20-29
    • Jiang, R.1    Taly, A.2    Grutter, T.3
  • 5
    • 0036788971 scopus 로고    scopus 로고
    • Molecular physiology of P2X receptors
    • North, R. A. (2002) Molecular physiology of P2X receptors. Physiol. Rev. 82, 1013-1067
    • (2002) Physiol. Rev. , vol.82 , pp. 1013-1067
    • North, R.A.1
  • 10
    • 60549110083 scopus 로고    scopus 로고
    • Inhibition of P2X(7) receptors by divalent cations: Old action and new insight
    • Jiang, L. H. (2009) Inhibition of P2X(7) receptors by divalent cations: old action and new insight. Eur. Biophys. J. 38, 339-346
    • (2009) Eur. Biophys. J. , vol.38 , pp. 339-346
    • Jiang, L.H.1
  • 16
    • 84455161674 scopus 로고    scopus 로고
    • The intracellular amino terminus plays a dominant role in desensitisation of ATP gated P2X receptor ion channels
    • Allsopp, R. C., and Evans, R. J. (2011) The intracellular amino terminus plays a dominant role in desensitisation of ATP gated P2X receptor ion channels. J. Biol. Chem. 286, 44691-44701
    • (2011) J. Biol. Chem. , vol.286 , pp. 44691-44701
    • Allsopp, R.C.1    Evans, R.J.2
  • 17
    • 3142669217 scopus 로고    scopus 로고
    • Identification of a trafficking motif involved in the stabilization and polarization of P2X receptors
    • Chaumont, S., and Jiang, L. H., Penna, A., North, R. A., and Rassendren, F. (2004) Identification of a trafficking motif involved in the stabilization and polarization of P2X receptors. J. Biol. Chem. 279, 29628-29638
    • (2004) J. Biol. Chem. , vol.279 , pp. 29628-29638
    • Chaumont, S.1    Jiang, L.H.2    Penna, A.3    North, R.A.4    Rassendren, F.5
  • 18
    • 0029665112 scopus 로고    scopus 로고
    • The cytolytic P2Z receptor for extracellular ATP identifiedasaP2X receptor P2X7
    • Surprenant, A., Rassendren, F., Kawashima, E., North, R. A., and Buell, G. (1996) The cytolytic P2Z receptor for extracellular ATP identifiedasaP2X receptor P2X7. Science 272, 735-738
    • (1996) Science , vol.272 , pp. 735-738
    • Surprenant, A.1    Rassendren, F.2    Kawashima, E.3    North, R.A.4    Buell, G.5
  • 19
    • 84874195644 scopus 로고    scopus 로고
    • P2X7 receptor channels allow direct permeation of nanometer-sized dyes
    • Browne, L. E., Compan, V., Bragg, L., and North, R. A. (2013) P2X7 receptor channels allow direct permeation of nanometer-sized dyes. J. Neurosci. 33, 3557-3566
    • (2013) J. Neurosci. , vol.33 , pp. 3557-3566
    • Browne, L.E.1    Compan, V.2    Bragg, L.3    North, R.A.4
  • 20
    • 77952931867 scopus 로고    scopus 로고
    • C-terminal calmodulin-binding motif differentially controls human and rat P2X7 receptor current facilitation
    • Roger, S., Gillet, L., Baroja-Mazo, A., Surprenant, A., and Pelegrin, P. (2010) C-terminal calmodulin-binding motif differentially controls human and rat P2X7 receptor current facilitation. J. Biol. Chem. 285, 17514-17524
    • (2010) J. Biol. Chem. , vol.285 , pp. 17514-17524
    • Roger, S.1    Gillet, L.2    Baroja-Mazo, A.3    Surprenant, A.4    Pelegrin, P.5
  • 22
    • 0041845127 scopus 로고    scopus 로고
    • Mutation of a dibasic amino acid motif within the C terminus of the P2X7 nucleotide receptor results in trafficking defects and impaired function
    • Denlinger, L. C., and Sommer, J. A., Parker, K., Gudipaty, L., Fisette, P. L., and Watters, J. W., Proctor, R. A., Dubyak, G. R., and Bertics, P. J. (2003) Mutation of a dibasic amino acid motif within the C terminus of the P2X7 nucleotide receptor results in trafficking defects and impaired function. J. Immunol. 171, 1304-1311
    • (2003) J. Immunol. , vol.171 , pp. 1304-1311
    • Denlinger, L.C.1    Sommer, J.A.2    Parker, K.3    Gudipaty, L.4    Fisette, P.L.5    Watters, J.W.6    Proctor, R.A.7    Dubyak, G.R.8    Bertics, P.J.9
  • 23
    • 0037072748 scopus 로고    scopus 로고
    • Epithelial membrane proteins induce membrane blebbing and interact with the P2X7 receptor C terminus
    • Wilson, H. L., and Wilson, S. A., Surprenant, A., and North, R. A. (2002) Epithelial membrane proteins induce membrane blebbing and interact with the P2X7 receptor C terminus. J. Biol. Chem. 277, 34017-34023
    • (2002) J. Biol. Chem. , vol.277 , pp. 34017-34023
    • Wilson, H.L.1    Wilson, S.A.2    Surprenant, A.3    North, R.A.4
  • 24
    • 0034703055 scopus 로고    scopus 로고
    • The role of positively charged amino acids in ATP recognition by human P2X1 receptors
    • Ennion, S., Hagan, S., and Evans, R. J. (2000) The role of positively charged amino acids in ATP recognition by human P2X1 receptors. J. Biol. Chem. 275, 29361-29367
    • (2000) J. Biol. Chem. , vol.275 , pp. 29361-29367
    • Ennion, S.1    Hagan, S.2    Evans, R.J.3
  • 25
    • 0020000229 scopus 로고
    • A patch-clamp study of bovine chromaffin cells and of their sensitivity to acetylcholine
    • Fenwick, E. M., Marty, A., and Neher, E. (1982) A patch-clamp study of bovine chromaffin cells and of their sensitivity to acetylcholine. J. Physiol. 331, 577-597
    • (1982) J. Physiol. , vol.331 , pp. 577-597
    • Fenwick, E.M.1    Marty, A.2    Neher, E.3
  • 26
    • 84912090584 scopus 로고    scopus 로고
    • Kinetics of conformational changes revealed by voltage-clamp fluorometry give insight to desensitization at ATP-gated human P2X1 receptors
    • Fryatt, A. G., and Evans, R. J. (2014) Kinetics of conformational changes revealed by voltage-clamp fluorometry give insight to desensitization at ATP-gated human P2X1 receptors. Mol. Pharmacol. 86, 707-715
    • (2014) Mol. Pharmacol. , vol.86 , pp. 707-715
    • Fryatt, A.G.1    Evans, R.J.2
  • 27
    • 0037625979 scopus 로고    scopus 로고
    • Activation and desensitization of the recombinant P2X1 receptor atnanomolar ATP concentrations
    • Rettinger, J., and Schmalzing, G. (2003) Activation and desensitization of the recombinant P2X1 receptor atnanomolar ATP concentrations. J. Gen. Physiol. 121, 451-461
    • (2003) J. Gen. Physiol. , vol.121 , pp. 451-461
    • Rettinger, J.1    Schmalzing, G.2
  • 29
    • 0031567594 scopus 로고    scopus 로고
    • P2X7 purinoceptor expression in xenopus oocytes is not sufficient to produce a pore-forming P2Z-like phenotype
    • Petrou, S., Ugur, M., Drummond, R. M., and Singer, J. J., Walsh, J. V., Jr. (1997) P2X7 purinoceptor expression in Xenopus oocytes is not sufficient to produce a pore-forming P2Z-like phenotype. FEBS Lett. 411, 339-345
    • (1997) FEBS Lett. , vol.411 , pp. 339-345
    • Petrou, S.1    Ugur, M.2    Drummond, R.M.3    Singer, J.J.4    Walsh, J.V.5
  • 30
  • 32
    • 84911059063 scopus 로고    scopus 로고
    • Plasma membrane cholesterol as a regulator of human and rodent P2X7 receptor activation and sensitization
    • Robinson, L. E., Shridar, M., Smith, P., and Murrell-Lagnado, R. D. (2014) Plasma membrane cholesterol as a regulator of human and rodent P2X7 receptor activation and sensitization. J. Biol. Chem. 289, 31983-31994
    • (2014) J. Biol. Chem. , vol.289 , pp. 31983-31994
    • Robinson, L.E.1    Shridar, M.2    Smith, P.3    Murrell-Lagnado, R.D.4
  • 33
    • 59449086148 scopus 로고    scopus 로고
    • The P2X7 receptor channel pore dilates under physiological ion conditions
    • Yan, Z., Li, S., Liang, Z., Tomić, M., and Stojilkovic, S. S. (2008) The P2X7 receptor channel pore dilates under physiological ion conditions. J. Gen. Physiol. 132, 563-573
    • (2008) J. Gen. Physiol. , vol.132 , pp. 563-573
    • Yan, Z.1    Li, S.2    Liang, Z.3    Tomić, M.4    Stojilkovic, S.S.5
  • 34
    • 34547824501 scopus 로고    scopus 로고
    • Influence of extracellular monovalent cations on pore and gating properties of P2X7 receptor-operated single-channel currents
    • Riedel, T., Schmalzing, G., and Markwardt, F. (2007) Influence of extracellular monovalent cations on pore and gating properties of P2X7 receptor-operated single-channel currents. Biophys. J. 93, 846-858
    • (2007) Biophys. J. , vol.93 , pp. 846-858
    • Riedel, T.1    Schmalzing, G.2    Markwardt, F.3
  • 35
    • 0026610465 scopus 로고
    • The ATP4-receptor-operated ion channel of human lymphocytes: Inhibition of ion fluxes by amiloride analogs and by extracellular sodium ions
    • Wiley, J. S., Chen, R., Wiley, M. J., and Jamieson, G. P. (1992) The ATP4-receptor-operated ion channel of human lymphocytes: inhibition of ion fluxes by amiloride analogs and by extracellular sodium ions. Arch. Biochem. Biophys. 292, 411-418
    • (1992) Arch. Biochem. Biophys. , vol.292 , pp. 411-418
    • Wiley, J.S.1    Chen, R.2    Wiley, M.J.3    Jamieson, G.P.4
  • 36
    • 84881594236 scopus 로고    scopus 로고
    • Cellular fluorescent high-throughput screening assays of the ATP-gated P2X7 receptor
    • YaQin, J., Qi, Y., and ShiYou, L. (2013) Cellular fluorescent high-throughput screening assays of the ATP-gated P2X7 receptor. Chin. Sci. Bull. 58, 2812-2819
    • (2013) Chin. Sci. Bull. , vol.58 , pp. 2812-2819
    • Yaqin, J.1    Qi, Y.2    Shiyou, L.3
  • 37
    • 77958530854 scopus 로고    scopus 로고
    • Experimental characterization and mathematical modeling of P2X7 receptor channel gating
    • Yan, Z., Khadra, A., Li, S., Tomic, M., Sherman, A., and Stojilkovic, S. S. (2010) Experimental characterization and mathematical modeling of P2X7 receptor channel gating. J. Neurosci. 30, 14213-14224
    • (2010) J. Neurosci. , vol.30 , pp. 14213-14224
    • Yan, Z.1    Khadra, A.2    Li, S.3    Tomic, M.4    Sherman, A.5    Stojilkovic, S.S.6
  • 39
    • 46749144924 scopus 로고    scopus 로고
    • Facilitation of P2X7 receptor currents and membrane blebbing via constitutive and dynamic calmodulin binding
    • Roger, S., Pelegrin, P., and Surprenant, A. (2008) Facilitation of P2X7 receptor currents and membrane blebbing via constitutive and dynamic calmodulin binding. J. Neurosci. 28, 6393-6401
    • (2008) J. Neurosci. , vol.28 , pp. 6393-6401
    • Roger, S.1    Pelegrin, P.2    Surprenant, A.3
  • 40
    • 0040609340 scopus 로고    scopus 로고
    • A protein kinase C site highly conservedin P2X subunits controls the desensitisation kinetics of P2X2 ATP-gated channels
    • Boué-Grabot, E., Archambault, V., and Séguéla, P. (2000) A protein kinase C site highly conservedin P2X subunits controls the desensitisation kinetics of P2X2 ATP-gated channels. J. Biol. Chem. 275, 10190-10195
    • (2000) J. Biol. Chem. , vol.275 , pp. 10190-10195
    • Boué-Grabot, E.1    Archambault, V.2    Séguéla, P.3
  • 41
    • 0036290377 scopus 로고    scopus 로고
    • P2X(1) receptor subunit contribution to gating revealed by a dominant negative PKC mutant
    • Ennion, S. J., and Evans, R. J. (2002) P2X(1) receptor subunit contribution to gating revealed by a dominant negative PKC mutant. Biochem. Biophys. Res. Commun. 291, 611-616
    • (2002) Biochem. Biophys. Res. Commun. , vol.291 , pp. 611-616
    • Ennion, S.J.1    Evans, R.J.2
  • 42
    • 0035805612 scopus 로고    scopus 로고
    • Amino acid residues involved in gating identified in the first membrane-spanning domain of the rat p2X2 receptor
    • Jiang, L.-H., Rassendren, F., Spelta, V., Surprenant, A., and North, R. A. (2001) Amino acid residues involved in gating identified in the first membrane-spanning domain of the rat p2X2 receptor. J. Biol. Chem. 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
  • 44
    • 0033366463 scopus 로고    scopus 로고
    • Neuronal P2X transmitter-gated cation channels change their ion selectivity in seconds
    • Khakh, B. S., and Bao, X. R., Labarca, C., and Lester, H. A.(1999) Neuronal P2X transmitter-gated cation channels change their ion selectivity in seconds. Nat. Neurosci. 2, 322-330
    • (1999) Nat. Neurosci. , vol.2 , pp. 322-330
    • Khakh, B.S.1    Bao, X.R.2    Labarca, C.3    Lester, H.A.4
  • 45
    • 67949117176 scopus 로고    scopus 로고
    • Crystal structure of the ATP-gated P2X(4) ion channel in the closed state
    • Kawate, T., and Michel, J. C., Birdsong, W. T., and Gouaux, E. (2009) Crystal structure of the ATP-gated P2X(4) ion channel in the closed state. Nature 460, 592-598
    • (2009) Nature , vol.460 , pp. 592-598
    • Kawate, T.1    Michel, J.C.2    Birdsong, W.T.3    Gouaux, E.4
  • 46
    • 84860785529 scopus 로고    scopus 로고
    • Molecular mechanism of ATP binding and ion channel activation in P2X receptors
    • Hattori, M., and Gouaux, E. (2012) Molecular mechanism of ATP binding and ion channel activation in P2X receptors. Nature 485, 207-212
    • (2012) Nature , vol.485 , pp. 207-212
    • Hattori, M.1    Gouaux, E.2


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