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Volumn 108, Issue 44, 2011, Pages 18162-18167

Voltage-gated proton channel in a dinoflagellate

Author keywords

Action potential; Channel gating; Ion channel; Ion selectivity; Permeation

Indexed keywords

ASPARTIC ACID; COMPLEMENTARY DNA; ION CHANNEL; UNCLASSIFIED DRUG; VOLTAGE GATED PROTON CHANNEL;

EID: 81055126213     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1115405108     Document Type: Article
Times cited : (103)

References (61)
  • 1
    • 0014088645 scopus 로고
    • The subcellular origin of bioluminescence in Noctiluca miliaris
    • Eckert R, Reynolds GT (1967) The subcellular origin of bioluminescence in Noctiluca miliaris. J Gen Physiol 50:1429-1458.
    • (1967) J Gen Physiol , vol.50 , pp. 1429-1458
    • Eckert, R.1    Reynolds, G.T.2
  • 2
    • 3543002580 scopus 로고
    • Observations on Noctiluca
    • French
    • Quatrefages A (1850) Observations on Noctiluca. Ann Sci Natur Zool Ser, 3:226-235 French.
    • (1850) Ann Sci Natur Zool Ser , vol.3 , pp. 226-235
    • Quatrefages, A.1
  • 3
    • 0015366328 scopus 로고
    • On the physical identity of scintillons: Bioluminescent particles in Gonyaulax polyedra
    • Fogel M, Schmitter RE, Hastings JW (1972) On the physical identity of scintillons: Bioluminescent particles in Gonyaulax polyedra. J Cell Sci 11:305-317.
    • (1972) J Cell Sci , vol.11 , pp. 305-317
    • Fogel, M.1    Schmitter, R.E.2    Hastings, J.W.3
  • 4
    • 0023571887 scopus 로고
    • Characterization of the bioluminescent organelles in Gonyaulax polyedra (dinoflagellates) after fast-freeze fixation and antiluciferase immunogold staining
    • Nicolas MT, Nicolas G, Johnson CH, Bassot JM, Hastings JW (1987) Characterization of the bioluminescent organelles in Gonyaulax polyedra (dinoflagellates) after fastfreeze fixation and antiluciferase immunogold staining. J Cell Biol 105:723-735. (Pubitemid 18043835)
    • (1987) Journal of Cell Biology , vol.105 , Issue.2 , pp. 723-735
    • Nicolas, M.-T.1    Nicolas, G.2    Johnson, C.H.3    Bassot, J.-M.4    Woodland, H.J.5
  • 5
    • 38949093555 scopus 로고
    • Electrophysiological studies of a non-luminescent form of the dinoflagellate Noctiluca miliaris
    • Chang JJ (1960) Electrophysiological studies of a non-luminescent form of the dinoflagellate Noctiluca miliaris. J Cell Comp Physiol 56:33-42.
    • (1960) J Cell Comp Physiol , vol.56 , pp. 33-42
    • Chang, J.J.1
  • 6
    • 2642550001 scopus 로고
    • Membrane resting and action potentials from a protozoan, Noctiluca scintillans
    • Hisada M (1957) Membrane resting and action potentials from a protozoan, Noctiluca scintillans. J Cell Physiol 50:57-71.
    • (1957) J Cell Physiol , vol.50 , pp. 57-71
    • Hisada, M.1
  • 7
    • 37049242206 scopus 로고
    • II. Asynchronous flash initiation by a propagated triggering potential
    • Eckert R (1965) II. Asynchronous flash initiation by a propagated triggering potential. Science 147:1142-1145.
    • (1965) Science , vol.147 , pp. 1142-1145
    • Eckert, R.1
  • 8
    • 0014316908 scopus 로고
    • The flash-triggering action potential of the luminescent dinoflagellate Noctiluca
    • Eckert R, Sibaoka T (1968) The flash-triggering action potential of the luminescent dinoflagellate Noctiluca. J Gen Physiol 52:258-282.
    • (1968) J Gen Physiol , vol.52 , pp. 258-282
    • Eckert, R.1    Sibaoka, T.2
  • 9
    • 0006402035 scopus 로고
    • Ionic composition and pH of the vacuolar sap in marine dinoflagellate Noctiluca
    • Nawata T, Sibaoka T (1976) Ionic composition and pH of the vacuolar sap in marine dinoflagellate Noctiluca. Plant Cell Physiol 17:265-272.
    • (1976) Plant Cell Physiol , vol.17 , pp. 265-272
    • Nawata, T.1    Sibaoka, T.2
  • 10
    • 0015302470 scopus 로고
    • Bioluminescence: Mechanism and mode of control of scintillon activity
    • Fogel M, Hastings JW (1972) Bioluminescence: Mechanism and mode of control of scintillon activity. Proc Natl Acad Sci USA 69:690-693.
    • (1972) Proc Natl Acad Sci USA , vol.69 , pp. 690-693
    • Fogel, M.1    Hastings, J.W.2
  • 11
    • 0014407768 scopus 로고
    • Bioluminescence: pH activity profiles of related luciferase fractions
    • Krieger N, Hastings JW (1968) Bioluminescence: pH activity profiles of related luciferase fractions. Science 161:586-589.
    • (1968) Science , vol.161 , pp. 586-589
    • Krieger, N.1    Hastings, J.W.2
  • 13
    • 0024971049 scopus 로고
    • Role of a luciferin-binding protein in the circadian bioluminescent reaction of Gonyaulax polyedra
    • Morse D, Pappenheimer AM, Jr., Hastings JW (1989) Role of a luciferin-binding protein in the circadian bioluminescent reaction of Gonyaulax polyedra. J Biol Chem 264: 11822-11826.
    • (1989) J Biol Chem , vol.264 , pp. 11822-11826
    • Morse, D.1    Pappenheimer Jr., A.M.2    Hastings, J.W.3
  • 14
    • 0014984678 scopus 로고
    • A substrate-binding protein in the Gonyaulax bioluminescence reaction
    • Fogel M, Hastings JW (1971) A substrate-binding protein in the Gonyaulax bioluminescence reaction. Arch Biochem Biophys 142:310-321.
    • (1971) Arch Biochem Biophys , vol.142 , pp. 310-321
    • Fogel, M.1    Hastings, J.W.2
  • 15
    • 39049097980 scopus 로고
    • The purification and properties of the bioluminescent system in Gonyaulax polyedra
    • Bode VC, Hastings JW (1963) The purification and properties of the bioluminescent system in Gonyaulax polyedra. Arch Biochem Biophys 103:488-499.
    • (1963) Arch Biochem Biophys , vol.103 , pp. 488-499
    • Bode, V.C.1    Hastings, J.W.2
  • 16
    • 0010920970 scopus 로고
    • Coupling between action potential and bioluminescence in Noctiluca: Effects of inorganic ions and pH in vacuolar sap
    • Nawata T, Sibaoka T (1979) Coupling between action potential and bioluminescence in Noctiluca: Effects of inorganic ions and pH in vacuolar sap. J Comp Physiol 134: 137-149.
    • (1979) J Comp Physiol , vol.134 , pp. 137-149
    • Nawata, T.1    Sibaoka, T.2
  • 17
    • 0023282124 scopus 로고
    • The ultrastructural localization of luciferase in three bioluminescent dinoflagellates, two species of Pyrocystis, and Noctiluca, using anti-luciferase and immunogold labelling
    • Nicolas MT, Sweeney BM, Hastings JW (1987) The ultrastructural localization of luciferase in three bioluminescent dinoflagellates, two species of Pyrocystis, and Noctiluca, using anti-luciferase and immunogold labelling. J Cell Sci 87:189-196.
    • (1987) J Cell Sci , vol.87 , pp. 189-196
    • Nicolas, M.T.1    Sweeney, B.M.2    Hastings, J.W.3
  • 18
    • 33645234919 scopus 로고    scopus 로고
    • On the identity of Karlodinium veneficum and description of Karlodinium armiger sp. nov. (Dinophyceae), based on light and electron microscopy, nuclear-encoded LSU rDNA, and pigment composition
    • Bergholtz T, Daubjerg N, Moestrup Ø, Fernández-Tejedor M (2005) On the identity of Karlodinium veneficum and description of Karlodinium armiger sp. nov. (Dinophyceae), based on light and electron microscopy, nuclear-encoded LSU rDNA, and pigment composition. J Phycol 42:170-193.
    • (2005) J Phycol , vol.42 , pp. 170-193
    • Bergholtz, T.1    Daubjerg, N.2    Moestrup, Ø.3    Fernández-Tejedor, M.4
  • 19
    • 0345391142 scopus 로고
    • Toxic marine flagellates; their occurrence and physiological effects on animals
    • Ballantine D, Abbott BC (1957) Toxic marine flagellates; their occurrence and physiological effects on animals. J Gen Microbiol 16:274-281.
    • (1957) J Gen Microbiol , vol.16 , pp. 274-281
    • Ballantine, D.1    Abbott, B.C.2
  • 20
    • 77956224854 scopus 로고    scopus 로고
    • Structure and relative potency of several karlotoxins from Karlodinium veneficum
    • Van Wagoner RM, et al. (2010) Structure and relative potency of several karlotoxins from Karlodinium veneficum. J Nat Prod 73:1360-1365.
    • (2010) J Nat Prod , vol.73 , pp. 1360-1365
    • Van Wagoner, R.M.1
  • 22
    • 0012835689 scopus 로고    scopus 로고
    • Toxic activity from cultures of Karlodinium micrum (=Gyrodinium galatheanum) (Dinophyceae) - A dinoflagellate associated with fish mortalities in an estuarine aquaculture facility
    • DOI 10.1016/S1568-9883(02)00027-6, PII S1568988302000276
    • Deeds JR, Terlizzi DE, Adolf JE, Stoecker DK, Place AR (2002) Toxic activity from cultures of Karlodinium micrum (=Gyrodinium galatheanum) (Dinophyceae) - a dinoflagellate associated with fish mortalities in an estuarine aquaculture facility. Harmful Algae 1:169-189. (Pubitemid 37379143)
    • (2002) Harmful Algae , vol.1 , Issue.2 , pp. 169-189
    • Deeds, J.R.1    Terlizzi, D.E.2    Adolf, J.E.3    Stoecker, D.K.4    Place, A.R.5
  • 23
    • 69249203617 scopus 로고    scopus 로고
    • Use of the dinoflagellate Karlodinium veneficum as a sustainable source of biodiesel production
    • Fuentes-Grünewald C, Garcés E, Rossi S, Camp J (2009) Use of the dinoflagellate Karlodinium veneficum as a sustainable source of biodiesel production. J Ind Microbiol Biotechnol 36:1215-1224.
    • (2009) J Ind Microbiol Biotechnol , vol.36 , pp. 1215-1224
    • Fuentes-Grünewald, C.1    Garcés, E.2    Rossi, S.3    Camp, J.4
  • 24
    • 83055176497 scopus 로고    scopus 로고
    • Aspartate112 is the selectivity filter of the human voltage gated proton channel
    • in press
    • Musset B, et al. (2011) Aspartate112 is the selectivity filter of the human voltage gated proton channel. Nature, in press.
    • (2011) Nature
    • Musset, B.1
  • 25
    • 0025008168 scopus 로고
    • Sequence logos: A new way to display consensus sequences
    • Schneider TD, Stephens RM (1990) Sequence logos: A new way to display consensus sequences. Nucleic Acids Res 18:6097-6100.
    • (1990) Nucleic Acids Res , vol.18 , pp. 6097-6100
    • Schneider, T.D.1    Stephens, R.M.2
  • 26
    • 78650755819 scopus 로고    scopus 로고
    • Analysis of codon usage patterns in toxic dinoflagellate Alexandrium tamarense through expressed sequence tag data
    • Hsiao YY, Lin CH, Liu JK, Wong TY, Kuo J (2010) Analysis of codon usage patterns in toxic dinoflagellate Alexandrium tamarense through expressed sequence tag data. Comp Funct Genomics 2010:138538.
    • (2010) Comp Funct Genomics , vol.2010 , pp. 138538
    • Hsiao, Y.Y.1    Lin, C.H.2    Liu, J.K.3    Wong, T.Y.4    Kuo, J.5
  • 27
    • 0037379781 scopus 로고    scopus 로고
    • Voltage-gated proton channels and other proton transfer pathways
    • DeCoursey TE (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
  • 28
    • 0029034117 scopus 로고
    • The voltage-activated hydrogen ion conductance in rat alveolar epithelial cells is determined by the pH gradient
    • Cherny VV, Markin VS, DeCoursey TE (1995) The voltage-activated hydrogen ion conductance in rat alveolar epithelial cells is determined by the pH gradient. J Gen Physiol 105:861-896.
    • (1995) J Gen Physiol , vol.105 , pp. 861-896
    • Cherny, V.V.1    Markin, V.S.2    DeCoursey, T.E.3
  • 29
    • 0029597849 scopus 로고
    • Voltage-activated proton currents in membrane patches of rat alveolar epithelial cells
    • DeCoursey TE, Cherny VV (1995) Voltage-activated proton currents in membrane patches of rat alveolar epithelial cells. J Physiol 489:299-307. (Pubitemid 26009413)
    • (1995) Journal of Physiology , vol.489 , Issue.2 , pp. 299-307
    • DeCoursey, T.E.1    Cherny, V.V.2
  • 30
  • 32
  • 34
    • 0026032209 scopus 로고
    • Alteration of voltage-dependence of Shaker potassium channel by mutations in the S4 sequence
    • Papazian DM, Timpe LC, Jan YN, Jan LY (1991) Alteration of voltage-dependence of Shaker potassium channel by mutations in the S4 sequence. Nature 349:305-310. (Pubitemid 21912066)
    • (1991) Nature , vol.349 , Issue.6307 , pp. 305-310
    • Papazian, D.M.1    Timpe, L.C.2    Jan, Y.N.3    Jan, L.Y.4
  • 35
    • 0030175348 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1016/S0896-6273(00)80143-9
    • Aggarwal SK, MacKinnon R (1996) Contribution of the S4 segment to gating charge in the Shaker K+ channel. Neuron 16:1169-1177. (Pubitemid 26227238)
    • (1996) Neuron , vol.16 , Issue.6 , pp. 1169-1177
    • Aggarwal, S.K.1    MacKinnon, R.2
  • 39
    • 21744438625 scopus 로고    scopus 로고
    • Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor
    • DOI 10.1038/nature03650
    • Murata Y, Iwasaki H, Sasaki M, Inaba K, Okamura Y (2005) Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor. Nature 435:1239-1243. (Pubitemid 40943089)
    • (2005) Nature , vol.435 , Issue.7046 , pp. 1239-1243
    • Murata, Y.1    Iwasaki, H.2    Sasaki, M.3    Inaba, K.4    Okamura, Y.5
  • 40
    • 77954383905 scopus 로고    scopus 로고
    • + permeation pathway in the voltage-gated proton channel Hv1
    • + permeation pathway in the voltage-gated proton channel Hv1. Nat Struct Mol Biol 17:869-875.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 869-875
    • Ramsey, I.S.1
  • 41
    • 33646229810 scopus 로고    scopus 로고
    • A voltage sensor-domain protein is a voltagegated proton channel
    • Sasaki M, Takagi M, Okamura Y (2006) A voltage sensor-domain protein is a voltagegated proton channel. Science 312:589-592.
    • (2006) Science , vol.312 , pp. 589-592
    • Sasaki, M.1    Takagi, M.2    Okamura, Y.3
  • 42
    • 33646358260 scopus 로고    scopus 로고
    • A voltage-gated proton-selective channel lacking the pore domain
    • Ramsey IS, Moran MM, Chong JA, Clapham DE (2006) A voltage-gated proton-selective channel lacking the pore domain. Nature 440:1213-1216.
    • (2006) Nature , vol.440 , pp. 1213-1216
    • Ramsey, I.S.1    Moran, M.M.2    Chong, J.A.3    Clapham, D.E.4
  • 43
    • 76649113437 scopus 로고    scopus 로고
    • Functionality of the voltage-gated proton channel truncated in S4
    • Sakata S, et al. (2010) Functionality of the voltage-gated proton channel truncated in S4. Proc Natl Acad Sci USA 107:2313-2318.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 2313-2318
    • Sakata, S.1
  • 44
    • 43449139690 scopus 로고    scopus 로고
    • The Voltage-Gated Proton Channel Hv1 Has Two Pores, Each Controlled by One Voltage Sensor
    • DOI 10.1016/j.neuron.2008.03.026, PII S0896627308003000
    • Tombola F, Ulbrich MH, Isacoff EY (2008) The voltage-gated proton channel Hv1 has two pores, each controlled by one voltage sensor. Neuron 58:546-556. (Pubitemid 351672357)
    • (2008) Neuron , vol.58 , Issue.4 , pp. 546-556
    • Tombola, F.1    Ulbrich, M.H.2    Isacoff, E.Y.3
  • 47
    • 78649501042 scopus 로고    scopus 로고
    • Molecular and functional characterization of Hv1 proton channel in human granulocytes
    • Petheo{combining double acute accent} GL, et al. (2010) Molecular and functional characterization of Hv1 proton channel in human granulocytes. PLoS One 5:e14081.
    • (2010) PLoS One , vol.5
    • Petheo, G.L.1
  • 48
    • 48249143183 scopus 로고    scopus 로고
    • Multimeric nature of voltage-gated proton channels
    • Koch HP, et al. (2008) Multimeric nature of voltage-gated proton channels. Proc Natl Acad Sci USA 105:9111-9116.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 9111-9116
    • Koch, H.P.1
  • 49
    • 77952939105 scopus 로고    scopus 로고
    • Zinc inhibition of monomeric and dimeric proton channels suggests cooperative gating
    • Musset B, et al. (2010) Zinc inhibition of monomeric and dimeric proton channels suggests cooperative gating. J Physiol 588:1435-1449.
    • (2010) J Physiol , vol.588 , pp. 1435-1449
    • Musset, B.1
  • 50
    • 77951236493 scopus 로고    scopus 로고
    • The role and structure of the carboxyl-terminal domain of the human voltage-gated proton channel Hv1
    • Li SJ, et al. (2010) The role and structure of the carboxyl-terminal domain of the human voltage-gated proton channel Hv1. J Biol Chem 285:12047-12054.
    • (2010) J Biol Chem , vol.285 , pp. 12047-12054
    • Li, S.J.1
  • 51
    • 0030881872 scopus 로고    scopus 로고
    • A functionally defined model for the M2 proton channel of influenza A virus suggests a mechanism for its ion selectivity
    • Pinto LH, et al. (1997) A functionally defined model for the M2 proton channel of influenza A virus suggests a mechanism for its ion selectivity. Proc Natl Acad Sci USA 94:11301-11306.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11301-11306
    • Pinto, L.H.1
  • 52
    • 20444385829 scopus 로고    scopus 로고
    • Chemical rescue of histidine selectivity filter mutants of the M2 ion channel of influenza A virus
    • DOI 10.1074/jbc.M412406200
    • Venkataraman P, Lamb RA, Pinto LH (2005) Chemical rescue of histidine selectivity filter mutants of the M2 ion channel of influenza A virus. J Biol Chem 280: 21463-21472. (Pubitemid 40805711)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.22 , pp. 21463-21472
    • Venkataraman, P.1    Lamb, R.A.2    Pinto, L.H.3
  • 53
    • 0035039731 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1085/jgp.117.5.469
    • Starace DM, Bezanilla F (2001) Histidine scanning mutagenesis of basic residues of the S4 segment of the Shaker K+ channel. J Gen Physiol 117:469-490. (Pubitemid 32441397)
    • (2001) Journal of General Physiology , vol.117 , Issue.5 , pp. 469-490
    • Starace, D.M.1    Bezanilla, F.2
  • 54
    • 1142274549 scopus 로고    scopus 로고
    • A proton pore in a potassium channel voltage sensor reveals a focused electric field
    • DOI 10.1038/nature02270
    • Starace DM, Bezanilla F (2004) A proton pore in a potassium channel voltage sensor reveals a focused electric field. Nature 427:548-553. (Pubitemid 38209113)
    • (2004) Nature , vol.427 , Issue.6974 , pp. 548-553
    • Starace, D.M.1    Bezanilla, F.2
  • 55
    • 34347211819 scopus 로고    scopus 로고
    • + channel mutation linked to hypokalemic periodic paralysis exposes a proton-selective gating pore
    • + channel mutation linked to hypokalemic periodic paralysis exposes a proton-selective gating pore. J Gen Physiol 130:11-20.
    • (2007) J Gen Physiol , vol.130 , pp. 11-20
    • Struyk, A.F.1    Cannon, S.C.2
  • 56
    • 0031474978 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1016/S0896-6273(00)80422-5
    • Starace DM, Stefani E, Bezanilla F (1997) Voltage-dependent proton transport by the voltage sensor of the Shaker K+ channel. Neuron 19:1319-1327. (Pubitemid 28030550)
    • (1997) Neuron , vol.19 , Issue.6 , pp. 1319-1327
    • Starace, D.M.1    Stefani, E.2    Bezanilla, F.3
  • 57
    • 75549085495 scopus 로고    scopus 로고
    • EggNOG v2.0: Extending the evolutionary genealogy of genes with enhanced non-supervised orthologous groups, species and functional annotations
    • Muller J, et al. (2010) eggNOG v2.0: Extending the evolutionary genealogy of genes with enhanced non-supervised orthologous groups, species and functional annotations. Nucleic Acids Res 38:D190-D195.
    • (2010) Nucleic Acids Res , vol.38
    • Muller, J.1
  • 58
    • 42449090264 scopus 로고    scopus 로고
    • PROMALS3D: A tool for multiple protein sequence and structure alignments
    • DOI 10.1093/nar/gkn072
    • Pei J, Kim BH, Grishin NV (2008) PROMALS3D: A tool for multiple protein sequence and structure alignments. Nucleic Acids Res 36:2295-2300. (Pubitemid 351567002)
    • (2008) Nucleic Acids Research , vol.36 , Issue.7 , pp. 2295-2300
    • Pei, J.1    Kim, B.-H.2    Grishin, N.V.3
  • 60
    • 0035682886 scopus 로고    scopus 로고
    • Evolution of an artificial seawater medium: Improvements in enriched seawater, artificial water over the last two decades
    • DOI 10.1046/j.1529-8817.2001.01052.x
    • Berges JA, Franklin DJ, Harrison PJ (2001) Evolution of an artificial seawater medium: Improvements in enriched seawater, artificial water over the last two decades. J Phycol 37:1138-1145. (Pubitemid 34067672)
    • (2001) Journal of Phycology , vol.37 , Issue.6 , pp. 1138-1145
    • Berges, J.A.1    Franklin, D.J.2    Harrison, P.J.3


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