메뉴 건너뛰기




Volumn 24, Issue 10, 2010, Pages 3696-3705

Voltage-dependent charge movement associated with activation of the CLC-5 2Cl-/1H+ exchanger

Author keywords

Chloride channel; Chloride transport; Gating charge; Voltage sensor

Indexed keywords

4 (2 HYDROXYETHYL) 1 PIPERAZINEETHANESULFONIC ACID; ASPARTIC ACID; BROMIDE ION; CHLORIDE CHANNEL; MESYLIC ACID; PROTEIN CLC5; SULFATE; UNCLASSIFIED DRUG; VOLTAGE GATED CHANNEL FORMING PROTEIN; ANION; ANTIPORTER; CHLORIDE-BASE EXCHANGER; CLC-5 CHLORIDE CHANNEL;

EID: 77957852847     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.09-150649     Document Type: Article
Times cited : (40)

References (34)
  • 2
    • 0033534733 scopus 로고    scopus 로고
    • Mutational analysis demonstrates that clc-4 and clc-5 directly mediate plasma membrane currents
    • Friedrich, T., Breiderhoff, T., and Jentsch, T. J. (1999) Mutational analysis demonstrates that ClC-4 and ClC-5 directly mediate plasma membrane currents. J. Biol. Chem. 274, 896-902 (Pubitemid 129535249)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.2 , pp. 896-902
    • Friedrich, T.1    Breiderhoff, T.2    Jentsch, T.J.3
  • 3
    • 22944475536 scopus 로고    scopus 로고
    • Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5
    • DOI 10.1038/nature03720
    • Picollo, A., and Pusch, M. (2005) Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5. Nature 436, 420-423 (Pubitemid 41059054)
    • (2005) Nature , vol.436 , Issue.7049 , pp. 420-423
    • Picollo, A.1    Pusch, M.2
  • 4
    • 22944479662 scopus 로고    scopus 로고
    • Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins
    • DOI 10.1038/nature03860
    • Scheel, O., Zdebik, A. A., Lourdel, S., and Jentsch, T. J. (2005) Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins. Nature 436, 424-427 (Pubitemid 41059055)
    • (2005) Nature , vol.436 , Issue.7049 , pp. 424-427
    • Scheel, O.1    Zdebik, A.A.2    Lourdel, S.3    Jentsch, T.J.4
  • 5
    • 59649097040 scopus 로고    scopus 로고
    • + antiporter by a single point mutation
    • + antiporter by a single point mutation. EMBO J. 28, 175-182
    • (2009) EMBO J. , vol.28 , pp. 175-182
    • Zifarelli, G.1    Pusch, M.2
  • 7
    • 0037122805 scopus 로고    scopus 로고
    • X-ray structure of a CIC chloride channel at 3.0 a reveals the molecular basis of anion selectivity
    • DOI 10.1038/415287a
    • Dutzler, R., Campbell, E. B., Cadene, M., Chait, B. T., and MacKinnon, R. (2002) X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity. Nature 415, 287-294 (Pubitemid 34087544)
    • (2002) Nature , vol.415 , Issue.6869 , pp. 287-294
    • Dutzler, R.1    Campbell, E.B.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 9
    • 0037418859 scopus 로고    scopus 로고
    • Gating the selectivity filter in ClC chloride channels
    • DOI 10.1126/science.1082708
    • Dutzler, R., Campbell, E. B., and MacKinnon, R. (2003) Gating the selectivity filter in ClC chloride channels. Science 300, 108-112 (Pubitemid 36423038)
    • (2003) Science , vol.300 , Issue.5616 , pp. 108-112
    • Dutzler, R.1    Campbell, E.B.2    MacKinnon, R.3
  • 11
    • 0028924935 scopus 로고
    • Gating of the voltage-dependent chloride channel CIC-0 by the permeant anion
    • Pusch, M., Ludewig, U., Rehfeldt, A., and Jentsch, T. J. (1995) Gating of the voltage-dependent chloride channel CIC-0 by the permeant anion. Nature 373, 527-531
    • (1995) Nature , vol.373 , pp. 527-531
    • Pusch, M.1    Ludewig, U.2    Rehfeldt, A.3    Jentsch, T.J.4
  • 14
    • 0029162517 scopus 로고
    • An aspartic acid residue important for voltage-dependent gating of human muscle chloride channels
    • Fahlke, C., Rudel, R., Mitrovic, N., Zhou, M., and George, A. L., Jr. (1995) An aspartic acid residue important for voltage-dependent gating of human muscle chloride channels. Neuron 15, 463-472
    • (1995) Neuron , vol.15 , pp. 463-472
    • Fahlke, C.1    Rudel, R.2    Mitrovic, N.3    Zhou, M.4    George Jr., A.L.5
  • 15
    • 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 (Pubitemid 30164943)
    • (2000) Physiological Reviews , vol.80 , Issue.2 , pp. 555-592
    • Bezanilla, F.1
  • 16
    • 0025200567 scopus 로고
    • Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes
    • Jentsch, T. J., Steinmeyer, K., and Schwarz, G. (1990) Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes. Nature 348, 510-514 (Pubitemid 120015094)
    • (1990) Nature , vol.348 , Issue.6301 , pp. 510-514
    • Jentsch, T.J.1    Steinmeyer, K.2    Schwarz, G.3
  • 21
    • 26944433471 scopus 로고    scopus 로고
    • Functional evaluation of Dent's disease-causing mutations: Implications for ClC-5 channel trafficking and internalization
    • DOI 10.1007/s00439-005-1303-2
    • Ludwig, M., Doroszewicz, J., Seyberth, H. W., Bokenkamp, A., Balluch, B., Nuutinen, M., Utsch, B., and Waldegger, S. (2005) Functional evaluation of Dent's disease-causing mutations: implications for ClC-5 channel trafficking and internalization. Hum. Genet. 117, 228-237 (Pubitemid 43136799)
    • (2005) Human Genetics , vol.117 , Issue.2-3 , pp. 228-237
    • Ludwig, M.1    Doroszewicz, J.2    Seyberth, H.W.3    Bokenkamp, A.4    Balluch, B.5    Nuutinen, M.6    Utsch, B.7    Waldegger, S.8
  • 22
    • 60549099384 scopus 로고    scopus 로고
    • Characterization of Dent's disease mutations of CLC-5 reveals a correlation between functional and cell biological consequences and protein structure
    • Smith, A. J., Reed, A. A., Loh, N. Y., Thakker, R. V., and Lippiat, J. D. (2009) Characterization of Dent's disease mutations of CLC-5 reveals a correlation between functional and cell biological consequences and protein structure. Am. J. Physiol. Renal Physiol. 296, F390-F397
    • (2009) Am. J. Physiol. Renal Physiol. , vol.296
    • Smith, A.J.1    Reed, A.A.2    Loh, N.Y.3    Thakker, R.V.4    Lippiat, J.D.5
  • 24
    • 0025270712 scopus 로고
    • Steady-state coupling of ion-channel conformations to a transmembrane ion gradient
    • Richard, E. A., and Miller, C. (1990) Steady-state coupling of ion-channel conformations to a transmembrane ion gradient. Science 247, 1208-1210 (Pubitemid 20102479)
    • (1990) Science , vol.247 , Issue.4947 , pp. 1208-1210
    • Richard, E.A.1    Miller, C.2
  • 25
    • 0030877627 scopus 로고    scopus 로고
    • Inward rectification in ClC-0 chloride channels caused by mutations in several protein regions
    • DOI 10.1085/jgp.110.2.165
    • Ludewig, U., Jentsch, T. J., and Pusch, M. (1997) Inward rectification in ClC-0 chloride channels caused by mutations in several protein regions. J. Gen. Physiol. 110, 165-171 (Pubitemid 27340488)
    • (1997) Journal of General Physiology , vol.110 , Issue.2 , pp. 165-171
    • Ludewig, U.1    Jentsch, T.J.2    Pusch, M.3
  • 26
    • 33748310543 scopus 로고    scopus 로고
    • + exchange transporter by polyatomic anions
    • + exchange transporter by polyatomic anions. J. Mol. Biol. 362, 682-690
    • (2006) J. Mol. Biol. , vol.362 , pp. 682-690
    • Nguitragool, W.1    Miller, C.2
  • 28
    • 0029609597 scopus 로고
    • Cloning and functional expression of rat CLC-5, a chloride channel related to kidney disease
    • DOI 10.1074/jbc.270.52.31172
    • Steinmeyer, K., Schwappach, B., Bens, M., Vandewalle, A., and Jentsch, T. J. (1995) Cloning and functional expression of rat CLC-5, a chloride channel related to kidney disease. J. Biol. Chem. 270, 31172-31177 (Pubitemid 26012205)
    • (1995) Journal of Biological Chemistry , vol.270 , Issue.52 , pp. 31172-31177
    • Steinmeyer, K.1    Schwappach, B.2    Bens, M.3    Vandewalle, A.4    Jentsch, T.J.5
  • 30
    • 2342483717 scopus 로고    scopus 로고
    • Electrophysiological insights into the mechanism of ion-coupled cotransporters
    • Peres, A., Giovannardi, S., Bossi, E., and Fesce, R. (2004) Electrophysiological insights into the mechanism of ion-coupled cotransporters. News Physiol. Sci. 19, 80-84
    • (2004) News Physiol. Sci. , vol.19 , pp. 80-84
    • Peres, A.1    Giovannardi, S.2    Bossi, E.3    Fesce, R.4
  • 31
    • 0026594721 scopus 로고
    • The size of gating charge in wild-type and mutant Shaker potassium channels
    • Schoppa, N. E., McCormack, K., Tanouye, M. A., and Sigworth, F. J. (1992) The size of gating charge in wild-type and mutant Shaker potassium channels. Science 255, 1712-1715
    • (1992) Science , vol.255 , pp. 1712-1715
    • Schoppa, N.E.1    McCormack, K.2    Tanouye, M.A.3    Sigworth, F.J.4
  • 32
    • 0020440405 scopus 로고
    • Open-state substructure of single chloride channels from Torpedo electroplax
    • Miller, C. (1982) Open-state substructure of single chloride channels from Torpedo electroplax. Philos. Trans. R. Soc. Lond. B Biol. Sci. 299, 401-411
    • (1982) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.299 , pp. 401-411
    • Miller, C.1
  • 33
    • 28244475369 scopus 로고    scopus 로고
    • Quantitative analysis of the voltage-dependent gating of mouse parotid ClC-2 chloride channel
    • DOI 10.1085/jgp.200509310
    • De Santiago, J. A., Nehrke, K., and Arreola, J. (2005) Quantitative analysis of the voltage-dependent gating of mouse parotid ClC-2 chloride channel. J. Gen. Physiol. 126, 591-603 (Pubitemid 41713739)
    • (2005) Journal of General Physiology , vol.126 , Issue.6 , pp. 591-603
    • De Santiago, J.A.1    Nehrke, K.2    Arreola, J.3
  • 34
    • 1542349179 scopus 로고    scopus 로고
    • Ion transport: Spot the difference
    • Gadsby, D. C. (2004) Ion transport: spot the difference. Nature 427, 795-797
    • (2004) Nature , vol.427 , pp. 795-797
    • Gadsby, D.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.