메뉴 건너뛰기




Volumn 1, Issue 4, 2010, Pages

Pore-opening mechanism in trimeric P2X receptor channels

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CADMIUM; CATION CHANNEL; CYSTEINE; PURINERGIC P2X RECEPTOR; SILVER;

EID: 84880308941     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms1048     Document Type: Article
Times cited : (78)

References (47)
  • 1
    • 0033516494 scopus 로고    scopus 로고
    • +-channel activation gating
    • DOI 10.1126/science.285.5424.73
    • Perozo, E., Cortes, D.M. & Cuello, L.G. Structural rearrangements underlying K+-channel activation gating. Science 2 85, 73-78 (1999). (Pubitemid 29307565)
    • (1999) Science , vol.285 , Issue.5424 , pp. 73-78
    • Perozo, E.1    Cortes, D.M.2    Cuello, L.G.3
  • 2
    • 0034817286 scopus 로고    scopus 로고
    • Structure of the KcsA channel intracellular gate in the open state
    • DOI 10.1038/nsb1001-883
    • Liu, Y.S., Sompornpisut, P. & Perozo, E. Structure of the KcsA channel intracellular gate in the open state. Nat. Struct. Biol. 8, 883-887 (2001). (Pubitemid 32923609)
    • (2001) Nature Structural Biology , vol.8 , Issue.10 , pp. 883-887
    • Liu, Y.-S.1    Sompornpisut, P.2    Perozo, E.3
  • 3
    • 0037026489 scopus 로고    scopus 로고
    • The voltage-gated potassium channels and their relatives
    • DOI 10.1038/nature00978
    • Yellen, G. The voltage-gated potassium channels and their relatives. Nature 4 19, 35-42 (2002). (Pubitemid 34987863)
    • (2002) Nature , vol.419 , Issue.6902 , pp. 35-42
    • Yellen, G.1
  • 4
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • DOI 10.1038/417515a
    • Jiang, Y. et al. Crystal structure and mechanism of a calcium-gated potassium channel. Nature 4 17, 515-522 (2002). (Pubitemid 34595912)
    • (2002) Nature , vol.417 , Issue.6888 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 6
    • 0037387189 scopus 로고    scopus 로고
    • Potassium channel gating observed with site-directed mass tagging
    • DOI 10.1038/nsb908
    • Kelly, B.L. & Gross, A. Potassium channel gating observed with site-directed mass tagging. Nat. Struct. Biol. 10, 280-284 (2003). (Pubitemid 36418752)
    • (2003) Nature Structural Biology , vol.10 , Issue.4 , pp. 280-284
    • Kelly, B.L.1    Gross, A.2
  • 7
    • 58149250085 scopus 로고    scopus 로고
    • High-resolution structure of the open NaK channel
    • Alam, A. & Jiang, Y. High-resolution structure of the open NaK channel. Nat. Struct. Mol. Biol. 1 6, 30-34 (2009).
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 30-34
    • Alam, A.1    Jiang, Y.2
  • 9
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • DOI 10.1126/science.282.5397.2220
    • Chang, G., Spencer, R.H., Lee, A.T., Barclay, M.T. & Rees, D.C. Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel. Science 2 82, 2220-2226 (1998). (Pubitemid 29004063)
    • (1998) Science , vol.282 , Issue.5397 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5
  • 10
    • 0034910316 scopus 로고    scopus 로고
    • Structural models of the MscL gating mechanism
    • Sukharev, S., Durell, S.R. & Guy, H.R. Structural models of the MscL gating mechanism. Biophys.J. 8 1, 917-936 (2001). (Pubitemid 32721462)
    • (2001) Biophysical Journal , vol.81 , Issue.2 , pp. 917-936
    • Sukharev, S.1    Durell, S.R.2    Guy, H.R.3
  • 11
    • 0037194760 scopus 로고    scopus 로고
    • Open channel structure of MscL and the gating mechanism of mechanosensitive channels
    • DOI 10.1038/nature00992
    • Perozo, E., Cortes, D.M., Sompornpisut, P., Kloda, A. & Martinac, B. Open channel structure of MscL and the gating mechanism of mechanosensitive channels. Nature 4 18, 942-948 (2002). (Pubitemid 34976024)
    • (2002) Nature , vol.418 , Issue.6901 , pp. 942-948
    • Perozo, E.1    Cortes, D.M.2    Sompornpisut, P.3    Kloda, A.4    Martinac, B.5
  • 12
    • 0036728233 scopus 로고    scopus 로고
    • A large iris-like expansion of a mechanosensitive channel protein induced by membrane tension
    • DOI 10.1038/nsb828
    • Betanzos, M., Chiang, C.S., Guy, H.R. & Sukharev, S. A large iris-like expansion of a mechanosensitive channel protein induced by membrane tension. Nat. Struct. Biol. 9, 704-710 (2002). (Pubitemid 34977305)
    • (2002) Nature Structural Biology , vol.9 , Issue.9 , pp. 704-710
    • Betanzos, M.1    Chiang, C.-S.2    Guy, H.R.3    Sukharev, S.4
  • 13
    • 0036725152 scopus 로고    scopus 로고
    • Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating
    • DOI 10.1038/nsb827
    • Perozo, E., Kloda, A., Cortes, D.M. & Martinac, B. Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating. Nat. Struct. Biol. 9, 696-703 (2002). (Pubitemid 34977304)
    • (2002) Nature Structural Biology , vol.9 , Issue.9 , pp. 696-703
    • Perozo, E.1    Kloda, A.2    Cortes, D.M.3    Martinac, B.4
  • 14
    • 69949160755 scopus 로고    scopus 로고
    • Structure of a tetrameric MscL in an expanded intermediate state
    • Liu, Z., Gandhi, C.S. & Rees, D.C. Structure of a tetrameric MscL in an expanded intermediate state. Nature 4 61, 120-124 (2009).
    • (2009) Nature , vol.461 , pp. 120-124
    • Liu, Z.1    Gandhi, C.S.2    Rees, D.C.3
  • 15
    • 67949117176 scopus 로고    scopus 로고
    • Crystal structure of the ATP-gated P2X4 ion channel in the closed state
    • Kawate, T., Michel, J.C., Birdsong, W.T. & Gouaux, E. Crystal structure of the ATP-gated P2X4 ion channel in the closed state. Nature 4 60, 592-598 (2009).
    • (2009) Nature , vol.460 , pp. 592-598
    • Kawate, T.1    Michel, J.C.2    Birdsong, W.T.3    Gouaux, E.4
  • 16
    • 34548813656 scopus 로고    scopus 로고
    • Structure of acid-sensing ion channel 1 at 1.9 A resolution and low pH
    • DOI 10.1038/nature06163, PII NATURE06163
    • Jasti, J., Furukawa, H., Gonzales, E.B. & Gouaux, E. Structure of acid-sensing ion channel 1 at 1.9 A resolution and low pH. Nature 4 49, 316-323 (2007). (Pubitemid 47443482)
    • (2007) Nature , vol.449 , Issue.7160 , pp. 316-323
    • Jasti, J.1    Furukawa, H.2    Gonzales, E.B.3    Gouaux, E.4
  • 17
    • 67949092829 scopus 로고    scopus 로고
    • Pore architecture and ion sites in acid-sensing ion channels and P2X receptors
    • Gonzales, E.B., Kawate, T. & Gouaux, E. Pore architecture and ion sites in acid-sensing ion channels and P2X receptors. Nature 460, 599-604 (2009).
    • (2009) Nature , vol.460 , pp. 599-604
    • Gonzales, E.B.1    Kawate, T.2    Gouaux, E.3
  • 18
    • 0030962404 scopus 로고    scopus 로고
    • Identification of amino acid residues contributing to the pore of a P2X receptor
    • DOI 10.1093/emboj/16.12.3446
    • Rassendren, F., Buell, G., Newbolt, A., North, R.A. & Surprenant, A. Identification of amino acid residues contributing to the pore of a P2X receptor. EMBO J. 1 6, 3446-3454 (1997). (Pubitemid 27250040)
    • (1997) EMBO Journal , vol.16 , Issue.12 , pp. 3446-3454
    • Rassendren, F.1    Buell, G.2    Newbolt, A.3    North, R.A.4    Surprenant, A.5
  • 19
    • 0032053981 scopus 로고    scopus 로고
    • 2 receptors identified by the substituted cysteine accessibility method
    • Egan, T.M., Haines, W.R. & Voigt, M.M. A domain contributing to the ion channel of ATP-gated P2X2 receptors identified by the substituted cysteine accessibility method.J. Neurosci. 1 8, 2350-2359 (1998). (Pubitemid 28141784)
    • (1998) Journal of Neuroscience , vol.18 , Issue.7 , pp. 2350-2359
    • Egan, T.M.1    Haines, W.R.2    Voigt, M.M.3
  • 20
    • 0032540197 scopus 로고    scopus 로고
    • 2 receptor/channels
    • DOI 10.1016/S0014-2999(98)00207-6, PII S0014299998002076
    • Nakazawa, K., Inoue, K. & Ohno, Y. An asparagine residue regulating conductance through P2X2 receptor/channels. Eur.J. Pharmacol. 347, 141-144 (1998). (Pubitemid 28238098)
    • (1998) European Journal of Pharmacology , vol.347 , Issue.1 , pp. 141-144
    • Nakazawa, K.1    Inoue, K.2    Ohno, Y.3
  • 21
    • 0035903169 scopus 로고    scopus 로고
    • Polar residues of the second transmembrane domain influence cation permeability of the ATP-gated P2X(2) receptor
    • Migita, K., Haines, W.R., Voigt, M.M. & Egan, T.M. Polar residues of the second transmembrane domain influence cation permeability of the ATP-gated P2X(2) receptor.J. Biol. Chem. 2 76, 30934-30941 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 30934-30941
    • Migita, K.1    Haines, W.R.2    Voigt, M.M.3    Egan, T.M.4
  • 22
    • 0037047678 scopus 로고    scopus 로고
    • Size of side-chain at channel pore mouth affects Ca(2+) block of P2X(2) receptor
    • Nakazawa, K. et al. Size of side-chain at channel pore mouth affects Ca(2+) block of P2X(2) receptor. Eur. J. Pharmacol. 4 49, 207-211 (2002).
    • (2002) Eur. J. Pharmacol. , vol.449 , pp. 207-211
    • Nakazawa, K.1
  • 23
    • 7244261780 scopus 로고    scopus 로고
    • 2 receptor
    • DOI 10.1523/JNEUROSCI.1423-04.2004
    • Li, Z., Migita, K., Samways, D.S., Voigt, M.M. & Egan, T.M. Gain and loss of channel function by alanine substitutions in the transmembrane segments of the rat ATP-gated P2X2 receptor.J. Neurosci. 2 4, 7378-7386 (2004). (Pubitemid 39100706)
    • (2004) Journal of Neuroscience , vol.24 , Issue.33 , pp. 7378-7386
    • Li, Z.1    Migita, K.2    Samways, D.S.K.3    Voigt, M.M.4    Egan, T.M.5
  • 24
    • 1842558753 scopus 로고    scopus 로고
    • Contribution of Calcium Ions to P2X Channel Responses
    • DOI 10.1523/JNEUROSCI.5429-03.2004
    • Egan, T.M. & Khakh, B.S. Contribution of calcium ions to P2X channel responses.J. Neurosci. 2 4, 3413-3420 (2004). (Pubitemid 38451907)
    • (2004) Journal of Neuroscience , vol.24 , Issue.13 , pp. 3413-3420
    • Egan, T.M.1    Khakh, B.S.2
  • 25
    • 36348952111 scopus 로고    scopus 로고
    • 308
    • DOI 10.1523/JNEUROSCI.4036-07.2007
    • Cao, L., Young, M.T., Broomhead, H.E., Fountain, S.J. & N orth, R.A. Thr339-to-serine substitution in rat P2X2 receptor second transmembrane domain causes constitutive opening and indicates a gating role for Lys308.J. Neurosci. 2 7, 12916-12923 (2007). (Pubitemid 350159573)
    • (2007) Journal of Neuroscience , vol.27 , Issue.47 , pp. 12916-12923
    • Cao, L.1    Young, M.T.2    Broomhead, H.E.3    Fountain, S.J.4    North, R.A.5
  • 26
    • 34147179943 scopus 로고    scopus 로고
    • Ivermectin Interaction with Transmembrane Helices Reveals Widespread Rearrangements during Opening of P2X Receptor Channels
    • DOI 10.1016/j.neuron.2007.03.020, PII S0896627307002425
    • Silberberg, S.D., Li, M. & Swartz, K.J. Ivermectin Interaction with transmembrane helices reveals widespread rearrangements during opening of P2X receptor channels. Neuron 5 4, 263-274 (2007). (Pubitemid 46561201)
    • (2007) Neuron , vol.54 , Issue.2 , pp. 263-274
    • Silberberg, S.D.1    Li, M.2    Swartz, K.J.3
  • 27
    • 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, D.S., Migita, K., Li, Z. & Egan, T.M. On the role of the first transmembrane domain in cation permeability and flux of the ATP-gated P2X2 receptor.J. Biol. Chem. 283, 5110-5117 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 5110-5117
    • Samways, D.S.1    Migita, K.2    Li, Z.3    Egan, T.M.4
  • 29
    • 70449635974 scopus 로고    scopus 로고
    • Polar residues in the second transmembrane domain of the rat P2X2 receptor that affect spontaneous gating, unitary conductance, and rectification
    • Cao, L., Broomhead, H.E., Young, M.T. & North, R.A. P olar residues in the second transmembrane domain of the rat P2X2 receptor that affect spontaneous gating, unitary conductance, and rectification. J. Neurosci. 29, 14257-14264 (2009).
    • (2009) J. Neurosci. , vol.29 , pp. 14257-14264
    • Cao, L.1    Broomhead, H.E.2    Young, M.T.3    North, R.A.4
  • 30
    • 0035499892 scopus 로고    scopus 로고
    • + channel-Fab complex at 2.0 A resolution
    • DOI 10.1038/35102009
    • Zhou, Y., Morais-Cabral, J.H., Kaufman, A. & MacKinnon, R. Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution. Nature 4 14, 43-48 (2001). (Pubitemid 33041616)
    • (2001) Nature , vol.414 , Issue.6859 , pp. 43-48
    • Zhou, Y.1    Morais-Cabral, J.H.2    Kaufman, A.3    Mackinnon, R.4
  • 31
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4 A resolution
    • DOI 10.1016/j.jmb.2004.12.031
    • Unwin, N. Refined structure of the nicotinic acetylcholine receptor at 4Aresolution. J. Mol. Biol. 3 46, 967-989 (2005). (Pubitemid 40215523)
    • (2005) Journal of Molecular Biology , vol.346 , Issue.4 , pp. 967-989
    • Unwin, N.1
  • 32
    • 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, B.S. Gated access to the pore of a P2X receptor: structural implications for closed-open transitions.J. Biol. Chem. 2 85, 10110-10121 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 10110-10121
    • Kracun, S.1    Chaptal, V.2    Abramson, J.3    Khakh, B.S.4
  • 33
    • 0028960949 scopus 로고
    • Silver as a probe of pore-forming residues in a potassium channel
    • Lu, Q. & Miller, C. Silver as a probe of pore-forming residues in a potassium channel. Science 2 68, 304-307 (1995).
    • (1995) Science , vol.268 , pp. 304-307
    • Lu, Q.1    Miller, C.2
  • 34
    • 0035923745 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1016/S0896-6273(01)00487-1
    • del Camino, D. & Yellen, G. Tight steric closure at the intracellular activation gate of a voltage-gated k(+) channel. Neuron 3 2, 649-656 (2001). (Pubitemid 33145198)
    • (2001) Neuron , vol.32 , Issue.4 , pp. 649-656
    • Del Camino, D.1    Yellen, G.2
  • 35
    • 0036788971 scopus 로고    scopus 로고
    • Molecular physiology of P2X receptors
    • North, R.A. Molecular physiology of P2X receptors. Physiol. Rev. 82, 1013-1067 (2002).
    • (2002) Physiol. Rev. , vol.82 , pp. 1013-1067
    • North, R.A.1
  • 36
    • 0030795112 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1016/S0896-6273(00)80357-8
    • Liu, Y., Holmgren, M., Jurman, M.E. & Yellen, G. Gated access to the pore of a voltage-dependent K+ channel. Neuron 1 9, 175-184 (1997). (Pubitemid 27333003)
    • (1997) Neuron , vol.19 , Issue.1 , pp. 175-184
    • Liu, Y.1    Holmgren, M.2    Jurman, M.E.3    Yellen, G.4
  • 37
    • 0032168179 scopus 로고    scopus 로고
    • + channel can be trapped in the open state by an intersubunit metal bridge
    • DOI 10.1016/S0896-6273(00)80571-1
    • Holmgren, M., Shin, K.S. & Yellen, G. The activation gate of a voltage-gated K+ channel can be trapped in the open state by an intersubunit metal bridge. Neuron 2 1, 617-621 (1998). (Pubitemid 28475512)
    • (1998) Neuron , vol.21 , Issue.3 , pp. 617-621
    • Holmgren, M.1    Shin, K.S.2    Yellen, G.3
  • 38
    • 0038452402 scopus 로고    scopus 로고
    • Coordination geometries of selected transition metal ions (Co2+, Ni2+, Cu2+, Zn2+, Cd2+, and Hg2+) in metalloproteins
    • Rulisek, L. & Vondrasek, J. Coordination geometries of selected transition metal ions (Co2+, Ni2+, Cu2+, Zn2+, Cd2+, and Hg2+) in metalloproteins.J. Inorg. Biochem. 71, 115-127 (1998).
    • (1998) J. Inorg. Biochem. , vol.71 , pp. 115-127
    • Rulisek, L.1    Vondrasek, J.2
  • 39
    • 0043264239 scopus 로고    scopus 로고
    • Ab initio study of Cd-thiol complexes: Application to the modelling of the metallothionein active site
    • Enescu, M., Renault, J., Pommeret, S., Mialocq, J. & Pin, S. Ab initio study of Cd-thiol complexes: application to the modelling of the metallothionein active site. Phys. Chem. Chem. Phys. 5, 3762-3767 (2003).
    • (2003) Phys. Chem. Chem. Phys. , vol.5 , pp. 3762-3767
    • Enescu, M.1    Renault, J.2    Pommeret, S.3    Mialocq, J.4    Pin, S.5
  • 41
    • 17044400916 scopus 로고    scopus 로고
    • Secondary structure and gating rearrangements of transmembrane segments in rat P2X4 receptor channels
    • Silberberg, S.D., Chang, T.H. & Swartz, K.J. Secondary structure and gating rearrangements of transmembrane segments in rat P2X4 receptor channels.J. Gen. Physiol. 125, 347-359 (2005).
    • (2005) J. Gen. Physiol. , vol.125 , pp. 347-359
    • Silberberg, S.D.1    Chang, T.H.2    Swartz, K.J.3
  • 42
    • 0033366463 scopus 로고    scopus 로고
    • Neuronal P2X transmitter-gated cation channels change their ion selectivity in seconds
    • DOI 10.1038/7233
    • Khakh, B.S., Bao, X.R., Labarca, C. & Lester, H.A. Neuronal P2X transmittergated cation channels change their ion selectivity in seconds. Nat. Neurosci. 2, 322-330 (1999). (Pubitemid 30491274)
    • (1999) Nature Neuroscience , vol.2 , Issue.4 , pp. 322-330
    • Khakh, B.S.1    Bao, X.R.2    Labarca, C.3    Lester, H.A.4
  • 44
    • 14044274324 scopus 로고    scopus 로고
    • 2 channel permeability dynamics
    • DOI 10.1074/jbc.M411324200
    • Khakh, B.S. & Egan, T.M. Contribution of transmembrane regions to ATPgated P2X2 channel permeability dynamics.J. Biol. Chem. 2 80, 6118-6129 (2005). (Pubitemid 40280097)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.7 , pp. 6118-6129
    • Khakh, B.S.1    Egan, T.M.2
  • 45
    • 0028025001 scopus 로고
    • New structural motif for ligand-gated ion channels defined by an ionotropic ATP receptor
    • DOI 10.1038/371519a0
    • Brake, A.J., Wagenbach, M.J. & Julius, D. New structural motif for ligandgated ion channels defined by an ionotropic ATP receptor. Nature 3 71, 519-523 (1994). (Pubitemid 24306610)
    • (1994) Nature , vol.371 , Issue.6497 , pp. 519-523
    • Brake, A.J.1    Wagenbach, M.J.2    Julius, D.3
  • 46
    • 0032705299 scopus 로고    scopus 로고
    • Contribution of individual subunits to the multimeric P2X(2) receptor: Estimates based on methanethiosulfonate block at T336C
    • Stoop, R. et al. Contribution of individual subunits to the multimeric P2X(2) receptor: estimates based on methanethiosulfonate block at T336C. Mol. Pharmacol. 5 6, 973-981 (1999).
    • (1999) Mol. Pharmacol. , vol.56 , pp. 973-981
    • Stoop, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.