메뉴 건너뛰기




Volumn 143, Issue 3, 2014, Pages 377-386

Long α helices projecting from the membrane as the dimer interface in the voltage-gated H+ channel

Author keywords

[No Author keywords available]

Indexed keywords

HV1 PROTON CHANNEL, MOUSE; ION CHANNEL;

EID: 84894474220     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.201311082     Document Type: Article
Times cited : (21)

References (48)
  • 1
    • 36849015754 scopus 로고    scopus 로고
    • Probing the structure of the dimeric KtrB membrane protein
    • Albright, R.A., K. Joh, and J.H. Morais-Cabral. 2007. Probing the structure of the dimeric KtrB membrane protein. J. Biol. Chem. 282:35046-35055. http://dx.doi.org/10.1074/jbc.M704260200
    • (2007) J. Biol. Chem. , vol.282 , pp. 35046-35055
    • Albright, R.A.1    Joh, K.2    Morais-Cabral, J.H.3
  • 2
    • 0032031204 scopus 로고    scopus 로고
    • Voltage-gated ion channels and electrical excitability
    • Armstrong, C.M., and B. Hille. 1998. Voltage-gated ion channels and electrical excitability. Neuron. 20:371-380. http://dx.doi.org/ 10.1016/S0896-6273(00)80981-2
    • (1998) Neuron. , vol.20 , pp. 371-380
    • Armstrong, C.M.1    Hille, B.2
  • 3
    • 0034017867 scopus 로고    scopus 로고
    • The voltage sensor in voltage-dependent ion channels
    • Bezanilla, F. 2000. The voltage sensor in voltage-dependent ion channels. Physiol. Rev. 80:555-592.
    • (2000) Physiol. Rev. , vol.80 , pp. 555-592
    • Bezanilla, F.1
  • 4
    • 0035252931 scopus 로고    scopus 로고
    • Coiled coils: a highly versatile protein folding motif
    • Burkhard, P., J. Stetefeld, and S.V. Strelkov. 2001. Coiled coils: a highly versatile protein folding motif. Trends Cell Biol. 11:82-88. http://dx.doi.org/10.1016/S0962-8924(00)01898-5
    • (2001) Trends Cell Biol. , vol.11 , pp. 82-88
    • Burkhard, P.1    Stetefeld, J.2    Strelkov, S.V.3
  • 5
    • 0026489631 scopus 로고
    • Thermal motions of surface α-helices in the d-galactose chemosensory receptor. Detection by disulfide trapping.
    • Careaga, C.L., and J.J. Falke. 1992. Thermal motions of surface α-helices in the d-galactose chemosensory receptor. Detection by disulfide trapping. J. Mol. Biol. 226:1219-1235. http://dx.doi.org/ 10.1016/0022-2836(92)91063-U
    • (1992) J. Mol. Biol. , vol.226 , pp. 1219-1235
    • Careaga, C.L.1    Falke, J.J.2
  • 6
    • 0025804130 scopus 로고
    • Large differences in the helix propensities of alanine and glycine
    • Chakrabartty, A., J.A. Schellman, and R.L. Baldwin. 1991. Large differences in the helix propensities of alanine and glycine. Nature. 351:586-588. http://dx.doi.org/10.1038/351586a0
    • (1991) Nature. , vol.351 , pp. 586-588
    • Chakrabartty, A.1    Schellman, J.A.2    Baldwin, R.L.3
  • 7
    • 0023645034 scopus 로고
    • Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins
    • Cornette, J.L., K.B. Cease, H. Margalit, J.L. Spouge, J.A. Berzofsky, and C. DeLisi. 1987. Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins. J. Mol. Biol. 195:659-685. http://dx.doi.org/10.1016/0022-2836(87)90189-6
    • (1987) J. Mol. Biol. , vol.195 , pp. 659-685
    • Cornette, J.L.1    Cease, K.B.2    Margalit, H.3    Spouge, J.L.4    Berzofsky, J.A.5    DeLisi, C.6
  • 8
    • 0000920828 scopus 로고
    • The packing of ?-helices: simple coiledcoils
    • Crick, F.H.C. 1953. The packing of ?-helices: simple coiledcoils. Acta Crystallogr. 6:689-697. http://dx.doi.org/10.1107/ S0365110X53001964
    • (1953) Acta Crystallogr. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 9
    • 77954644773 scopus 로고    scopus 로고
    • Structural dynamics of the magnesium-bound conformation of CorA in a lipid bilayer
    • Dalmas, O., L.G. Cuello, V. Jogini, D.M. Cortes, B. Roux, and E. Perozo. 2010. Structural dynamics of the magnesium-bound conformation of CorA in a lipid bilayer. Structure. 18:868-878. http:// dx.doi.org/10.1016/j.str.2010.04.009
    • (2010) Structure. , vol.18 , pp. 868-878
    • Dalmas, O.1    Cuello, L.G.2    Jogini, V.3    Cortes, D.M.4    Roux, B.5    Perozo, E.6
  • 10
    • 0037379781 scopus 로고    scopus 로고
    • Voltage-gated proton channels and other proton transfer pathways
    • Decoursey, T.E. 2003. Voltage-gated proton channels and other proton transfer pathways. Physiol. Rev. 83:475-579.
    • (2003) Physiol. Rev. , vol.83 , pp. 475-579
    • Decoursey, T.E.1
  • 11
    • 0032983519 scopus 로고    scopus 로고
    • Structure of the membrane domain of subunit b of the Escherichia coli F0F1 ATP synthase
    • Dmitriev, O., P.C. Jones, W. Jiang, and R.H. Fillingame. 1999. Structure of the membrane domain of subunit b of the Escherichia coli F0F1 ATP synthase. J. Biol. Chem. 274:15598-15604. http:// dx.doi.org/10.1074/jbc.274.22.15598
    • (1999) J. Biol. Chem. , vol.274 , pp. 15598-15604
    • Dmitriev, O.1    Jones, P.C.2    Jiang, W.3    Fillingame, R.H.4
  • 12
    • 76149085162 scopus 로고    scopus 로고
    • VSOP/Hv1 proton channels sustain calcium entry, neutrophil migration, and superoxide production by limiting cell depolarization and acidification
    • El Chemaly, A., Y. Okochi, M. Sasaki, S. Arnaudeau, Y. Okamura, and N. Demaurex. 2010. VSOP/Hv1 proton channels sustain calcium entry, neutrophil migration, and superoxide production by limiting cell depolarization and acidification. J. Exp. Med. 207:129-139. http://dx.doi.org/10.1084/jem.20091837
    • (2010) J. Exp. Med. , vol.207 , pp. 129-139
    • El Chemaly, A.1    Okochi, Y.2    Sasaki, M.3    Arnaudeau, S.4    Okamura, Y.5    Demaurex, N.6
  • 13
    • 64549106513 scopus 로고    scopus 로고
    • Disruption of the IS6-AID linker affects voltage-gated calcium channel inactivation and facilitation
    • Findeisen, F., and D.L. Minor Jr. 2009. Disruption of the IS6-AID linker affects voltage-gated calcium channel inactivation and facilitation. J. Gen. Physiol. 133:327-343. http://dx.doi.org/10.1085/jgp.200810143
    • (2009) J. Gen. Physiol. , vol.133 , pp. 327-343
    • Findeisen, F.1    Minor, D.L.2
  • 17
    • 77449143196 scopus 로고    scopus 로고
    • Strong cooperativity between subunits in voltage-gated proton channels
    • Gonzalez, C., H.P. Koch, B.M. Drum, and H.P. Larsson. 2010. Strong cooperativity between subunits in voltage-gated proton channels. Nat. Struct. Mol. Biol. 17:51-56. http://dx.doi.org/10.1038/nsmb.1739
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 51-56
    • Gonzalez, C.1    Koch, H.P.2    Drum, B.M.3    Larsson, H.P.4
  • 19
    • 84861653161 scopus 로고    scopus 로고
    • Voltage-gated potassium channels and the diversity of electrical signalling
    • Jan, L.Y., and Y.N. Jan. 2012. Voltage-gated potassium channels and the diversity of electrical signalling. J. Physiol. 590:2591-2599. http://dx.doi.org/10.1113/jphysiol.2011.224212
    • (2012) J. Physiol. , vol.590 , pp. 2591-2599
    • Jan, L.Y.1    Jan, Y.N.2
  • 21
    • 84887919690 scopus 로고    scopus 로고
    • Mapping of sites facing aqueous environment of voltage-gated proton channel at resting state: A study with PEGylation protection
    • Kurokawa, T., and Y. Okamura. 2014. Mapping of sites facing aqueous environment of voltage-gated proton channel at resting state: A study with PEGylation protection. Biochim. Biophys. Acta. 1838:382- 387. http://dx.doi.org/10.1016/j.bbamem.2013.10.001
    • (2014) Biochim. Biophys. Acta. , vol.1838
    • Kurokawa, T.1    Okamura, Y.2
  • 22
    • 0042697277 scopus 로고    scopus 로고
    • Atomic proximity between S4 segment and pore domain in Shaker potassium channels
    • Lainé, M., M.C. Lin, J.P. Bannister, W.R. Silverman, A.F. Mock, B. Roux, and D.M. Papazian. 2003. Atomic proximity between S4 segment and pore domain in Shaker potassium channels. Neuron. 39:467-481. http://dx.doi.org/10.1016/S0896-6273(03)00468-9
    • (2003) Neuron. , vol.39 , pp. 467-481
    • Lainé, M.1    Lin, M.C.2    Bannister, J.P.3    Silverman, W.R.4    Mock, A.F.5    Roux, B.6    Papazian, D.M.7
  • 23
    • 27344442574 scopus 로고    scopus 로고
    • Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane
    • USA.
    • Lee, S.Y., A. Lee, J. Chen, and R. MacKinnon. 2005. Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane. Proc. Natl. Acad. Sci. USA. 102:15441-15446. http://dx.doi.org/10.1073/pnas.0507651102
    • (2005) Proc. Natl. Acad. Sci. , vol.102 , pp. 15441-15446
    • Lee, S.Y.1    Lee, A.2    Chen, J.3    MacKinnon, R.4
  • 24
    • 45549106075 scopus 로고    scopus 로고
    • Dimeric subunit stoichiometry of the human voltage-dependent proton channel Hv1
    • USA.
    • Lee, S.Y., J.A. Letts, and R. Mackinnon. 2008. Dimeric subunit stoichiometry of the human voltage-dependent proton channel Hv1. Proc. Natl. Acad. Sci. USA. 105:7692-7695. http://dx.doi.org/ 10.1073/pnas.0803277105
    • (2008) Proc. Natl. Acad. Sci. , vol.105 , pp. 7692-7695
    • Lee, S.Y.1    Letts, J.A.2    Mackinnon, R.3
  • 25
    • 0033981341 scopus 로고    scopus 로고
    • α-helical structural elements within the voltage-sensing domains of a K+ channel
    • Li-Smerin, Y., D.H. Hackos, and K.J. Swartz. 2000. α-helical structural elements within the voltage-sensing domains of a K+ channel. J. Gen. Physiol. 115:33-50. http://dx.doi.org/10.1085/jgp.115.1.33
    • (2000) J. Gen. Physiol. , vol.115 , pp. 33-50
    • Li-Smerin, Y.1    Hackos, D.H.2    Swartz, K.J.3
  • 26
    • 75749122696 scopus 로고    scopus 로고
    • Acid extrusion from human spermatozoa is mediated by flagellar voltage-gated proton channel
    • Lishko, P.V., I.L. Botchkina, A. Fedorenko, and Y. Kirichok. 2010. Acid extrusion from human spermatozoa is mediated by flagellar voltage-gated proton channel. Cell. 140:327-337. http://dx.doi.org/10.1016/j.cell.2009.12.053
    • (2010) Cell. , vol.140 , pp. 327-337
    • Lishko, P.V.1    Botchkina, I.L.2    Fedorenko, A.3    Kirichok, Y.4
  • 27
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
    • Long, S.B., E.B. Campbell, and R. Mackinnon. 2005. Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science. 309:897-903. http://dx.doi.org/10.1126/science.1116269
    • (2005) Science. , vol.309 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 28
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: new structures and new functions
    • Lupas, A. 1996. Coiled coils: new structures and new functions. Trends Biochem. Sci. 21:375-382.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 375-382
    • Lupas, A.1
  • 29
    • 0033582936 scopus 로고    scopus 로고
    • Transmembrane structure of an inwardly rectifying potassium channel
    • Minor, D.L., Jr., S.J. Masseling, Y.N. Jan, and L.Y. Jan. 1999. Transmembrane structure of an inwardly rectifying potassium channel. Cell. 96:879-891. http://dx.doi.org/10.1016/S0092-8674(00)80597-8
    • (1999) Cell. , vol.96 , pp. 879-891
    • Minor, D.L.1    Masseling, S.J.2    Jan, Y.N.3    Jan, L.Y.4
  • 30
    • 77952939105 scopus 로고    scopus 로고
    • Zinc inhibition of monomeric and dimeric proton channels suggests cooperative gating
    • Musset, B., S.M. Smith, S. Rajan, V.V. Cherny, S. Sujai, D. Morgan, and T.E. DeCoursey. 2010. Zinc inhibition of monomeric and dimeric proton channels suggests cooperative gating. J. Physiol. 588:1435- 1449. http://dx.doi.org/10.1113/jphysiol.2010.188318
    • (2010) J. Physiol. , vol.588
    • Musset, B.1    Smith, S.M.2    Rajan, S.3    Cherny, V.V.4    Sujai, S.5    Morgan, D.6    DeCoursey, T.E.7
  • 31
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
    • O'Neil, K.T., and W.F. DeGrado. 1990. A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids. Science. 250:646-651. http://dx.doi.org/10.1126/science.2237415
    • (1990) Science. , vol.250 , pp. 646-651
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 32
    • 63349109185 scopus 로고    scopus 로고
    • Voltage-gated proton channel is expressed on phagosomes
    • Okochi, Y., M. Sasaki, H. Iwasaki, and Y. Okamura. 2009. Voltage-gated proton channel is expressed on phagosomes. Biochem. Biophys. Res. Commun. 382:274-279. http://dx.doi.org/10.1016/j.bbrc.2009.03.036
    • (2009) Biochem. Biophys. Res. Commun. , vol.382 , pp. 274-279
    • Okochi, Y.1    Sasaki, M.2    Iwasaki, H.3    Okamura, Y.4
  • 33
    • 79960621367 scopus 로고    scopus 로고
    • The crystal structure of a voltage-gated sodium channel
    • Payandeh, J., T. Scheuer, N. Zheng, and W.A. Catterall. 2011. The crystal structure of a voltage-gated sodium channel. Nature. 475:353-358. http://dx.doi.org/10.1038/nature10238
    • (2011) Nature. , vol.475 , pp. 353-358
    • Payandeh, J.1    Scheuer, T.2    Zheng, N.3    Catterall, W.A.4
  • 34
    • 2642701712 scopus 로고    scopus 로고
    • Three-dimensional architecture and gating mechanism of a K+ channel studied by EPR spectroscopy
    • Perozo, E., D.M. Cortes, and L.G. Cuello. 1998. Three-dimensional architecture and gating mechanism of a K+ channel studied by EPR spectroscopy. Nat. Struct. Biol. 5:459-469. http://dx.doi.org/ 10.1038/nsb0698-459
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 459-469
    • Perozo, E.1    Cortes, D.M.2    Cuello, L.G.3
  • 35
    • 0033516494 scopus 로고    scopus 로고
    • Structural rearrangements underlying K+-channel activation gating
    • Perozo, E., D.M. Cortes, and L.G. Cuello. 1999. Structural rearrangements underlying K+-channel activation gating. Science. 285:73-78. http://dx.doi.org/10.1126/science.285.5424.73
    • (1999) Science. , vol.285 , pp. 73-78
    • Perozo, E.1    Cortes, D.M.2    Cuello, L.G.3
  • 36
    • 84872735785 scopus 로고    scopus 로고
    • Subunit interactions during cooperative opening of voltage-gated proton channels
    • Qiu, F., S. Rebolledo, C. Gonzalez, and H.P. Larsson. 2013. Subunit interactions during cooperative opening of voltage-gated proton channels. Neuron. 77:288-298. http://dx.doi.org/10.1016/j.neuron.2012.12.021
    • (2013) Neuron. , vol.77 , pp. 288-298
    • Qiu, F.1    Rebolledo, S.2    Gonzalez, C.3    Larsson, H.P.4
  • 37
    • 33646358260 scopus 로고    scopus 로고
    • A voltage-gated proton-selective channel lacking the pore domain
    • Ramsey, I.S., M.M. Moran, J.A. Chong, and D.E. Clapham. 2006. A voltage-gated proton-selective channel lacking the pore domain. Nature. 440:1213-1216. http://dx.doi.org/10.1038/nature04700
    • (2006) Nature. , vol.440 , pp. 1213-1216
    • Ramsey, I.S.1    Moran, M.M.2    Chong, J.A.3    Clapham, D.E.4
  • 38
    • 66149104077 scopus 로고    scopus 로고
    • Hv1 proton channels are required for high-level NADPH oxidasedependent superoxide production during the phagocyte respiratory burst
    • USA.
    • Ramsey, I.S., E. Ruchti, J.S. Kaczmarek, and D.E. Clapham. 2009. Hv1 proton channels are required for high-level NADPH oxidasedependent superoxide production during the phagocyte respiratory burst. Proc. Natl. Acad. Sci. USA. 106:7642-7647. http://dx.doi.org/10.1073/pnas.0902761106
    • (2009) Proc. Natl. Acad. Sci. , vol.106 , pp. 7642-7647
    • Ramsey, I.S.1    Ruchti, E.2    Kaczmarek, J.S.3    Clapham, D.E.4
  • 39
    • 0024346677 scopus 로고
    • Hydrophobic organization of membrane proteins
    • Rees, D.C., L. DeAntonio, and D. Eisenberg. 1989. Hydrophobic organization of membrane proteins. Science. 245:510-513. http:// dx.doi.org/10.1126/science.2667138
    • (1989) Science. , vol.245 , pp. 510-513
    • Rees, D.C.1    DeAntonio, L.2    Eisenberg, D.3
  • 41
    • 33646229810 scopus 로고    scopus 로고
    • A voltage sensordomain protein is a voltage-gated proton channel
    • Sasaki, M., M. Takagi, and Y. Okamura. 2006. A voltage sensordomain protein is a voltage-gated proton channel. Science. 312:589-592. http://dx.doi.org/10.1126/science.1122352
    • (2006) Science. , vol.312 , pp. 589-592
    • Sasaki, M.1    Takagi, M.2    Okamura, Y.3
  • 42
    • 0036445512 scopus 로고    scopus 로고
    • Analysis of α-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation
    • Strelkov, S.V., and P. Burkhard. 2002. Analysis of α-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation. J. Struct. Biol. 137:54-64. http://dx.doi.org/ 10.1006/jsbi.2002.4454
    • (2002) J. Struct. Biol. , vol.137 , pp. 54-64
    • Strelkov, S.V.1    Burkhard, P.2
  • 43
    • 84868194771 scopus 로고    scopus 로고
    • Proton channels in algae: reasons to be excited
    • Taylor, A.R., C. Brownlee, and G.L. Wheeler. 2012. Proton channels in algae: reasons to be excited. Trends Plant Sci. 17:675-684. http://dx.doi.org/10.1016/j.tplants.2012.06.009
    • (2012) Trends Plant Sci. , vol.17 , pp. 675-684
    • Taylor, A.R.1    Brownlee, C.2    Wheeler, G.L.3
  • 44
    • 43449139690 scopus 로고    scopus 로고
    • The voltage-gated proton channel Hv1 has two pores, each controlled by one voltage sensor
    • Tombola, F., M.H. Ulbrich, and E.Y. Isacoff. 2008. The voltage-gated proton channel Hv1 has two pores, each controlled by one voltage sensor. Neuron. 58:546-556. http://dx.doi.org/10.1016/j.neuron.2008.03.026
    • (2008) Neuron. , vol.58 , pp. 546-556
    • Tombola, F.1    Ulbrich, M.H.2    Isacoff, E.Y.3
  • 45
    • 77449091709 scopus 로고    scopus 로고
    • The opening of the two pores of the Hv1 voltage-gated proton channel is tuned by cooperativity
    • Tombola, F., M.H. Ulbrich, S.C. Kohout, and E.Y. Isacoff. 2010. The opening of the two pores of the Hv1 voltage-gated proton channel is tuned by cooperativity. Nat. Struct. Mol. Biol. 17:44-50. http://dx.doi.org/10.1038/nsmb.1738
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 44-50
    • Tombola, F.1    Ulbrich, M.H.2    Kohout, S.C.3    Isacoff, E.Y.4
  • 46
    • 55049100031 scopus 로고    scopus 로고
    • S4-based voltage sensors have three major conformations
    • USA.
    • Villalba-Galea, C.A., W. Sandtner, D.M. Starace, and F. Bezanilla. 2008. S4-based voltage sensors have three major conformations. Proc. Natl. Acad. Sci. USA. 105:17600-17607. http://dx.doi.org/10.1073/pnas.0807387105
    • (2008) Proc. Natl. Acad. Sci. , vol.105 , pp. 17600-17607
    • Villalba-Galea, C.A.1    Sandtner, W.2    Starace, D.M.3    Bezanilla, F.4
  • 47
    • 0030747620 scopus 로고    scopus 로고
    • Helix proximity and ligand-induced conformational changes in the lactose permease of Escherichia coli determined by site-directed chemical crosslinking
    • Wu, J., and H.R. Kaback. 1997. Helix proximity and ligand-induced conformational changes in the lactose permease of Escherichia coli determined by site-directed chemical crosslinking. J. Mol. Biol. 270:285-293. http://dx.doi.org/10.1006/jmbi.1997.1099
    • (1997) J. Mol. Biol. , vol.270 , pp. 285-293
    • Wu, J.1    Kaback, H.R.2
  • 48
    • 0032506162 scopus 로고    scopus 로고
    • Tilting of helix I and ligand-induced changes in the lactose permease determined by site-directed chemical cross-linking in situ
    • Wu, J., D. Hardy, and H.R. Kaback. 1998. Tilting of helix I and ligand-induced changes in the lactose permease determined by site-directed chemical cross-linking in situ. Biochemistry. 37:15785-15790. http://dx.doi.org/10.1021/bi981501o
    • (1998) Biochemistry. , vol.37 , pp. 15785-15790
    • Wu, J.1    Hardy, D.2    Kaback, H.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.