메뉴 건너뛰기




Volumn 436, Issue 7049, 2005, Pages 424-427

Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CRYSTAL STRUCTURE; DISEASES; GENES; PH EFFECTS; PROTEINS; PROTONS;

EID: 22944479662     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature03860     Document Type: Article
Times cited : (431)

References (26)
  • 3
    • 13344286321 scopus 로고    scopus 로고
    • A common molecular basis for three inherited kidney stone diseases
    • Lloyd, S. E. et al. A common molecular basis for three inherited kidney stone diseases. Nature 379, 445-449 (1996).
    • (1996) Nature , vol.379 , pp. 445-449
    • Lloyd, S.E.1
  • 4
    • 0035951282 scopus 로고    scopus 로고
    • Loss of the ClC-7 chloride channel leads to osteopetrosis in mice and man
    • Kornak, U. et al. Loss of the ClC-7 chloride channel leads to osteopetrosis in mice and man. Cell 104, 205-215 (2001).
    • (2001) Cell , vol.104 , pp. 205-215
    • Kornak, U.1
  • 5
    • 20144387287 scopus 로고    scopus 로고
    • Loss of the chloride channel ClC-7 leads to lysosomal storage disease and neurodegeneration
    • Kasper, D. et al. Loss of the chloride channel ClC-7 leads to lysosomal storage disease and neurodegeneration. EMBO J. 24, 1079-1091 (2005).
    • (2005) EMBO J. , vol.24 , pp. 1079-1091
    • Kasper, D.1
  • 6
    • 0029609597 scopus 로고
    • Cloning and functional expression of rat CLC-5, a chloride channel related to kidney disease
    • Steinmeyer, K., Schwappach, B., Bens, M., Vandewalle, A. & Jentsch, T. J. Cloning and functional expression of rat CLC-5, a chloride channel related to kidney disease. J. Biol. Chem. 270, 31172-31177 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 31172-31177
    • Steinmeyer, K.1    Schwappach, B.2    Bens, M.3    Vandewalle, A.4    Jentsch, T.J.5
  • 7
    • 0033534733 scopus 로고    scopus 로고
    • Mutational analysis demonstrates that ClC-4 and ClC-5 directly mediate plasma membrane currents
    • Friedrich, T., Breiderhoff, T. & Jentsch, T. J. Mutational analysis demonstrates that ClC-4 and ClC-5 directly mediate plasma membrane currents. J. Biol. Chem. 274, 896-902 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 896-902
    • Friedrich, T.1    Breiderhoff, T.2    Jentsch, T.J.3
  • 9
    • 0037122805 scopus 로고    scopus 로고
    • X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity
    • Dutzler, R., Campbell, E. B., Cadene, M., Chait, B. T. & MacKinnon, R. X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity. Nature 415, 287-294 (2002).
    • (2002) Nature , vol.415 , pp. 287-294
    • Dutzler, R.1    Campbell, E.B.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 10
    • 0029619234 scopus 로고
    • Cloning of the amiloride-sensitive FMRFamide peptide-gated sodium channel
    • Lingueglia, E., Champigny, G., Lazdunski, M. & Barbry, P. Cloning of the amiloride-sensitive FMRFamide peptide-gated sodium channel. Nature 378, 730-733 (1995).
    • (1995) Nature , vol.378 , pp. 730-733
    • Lingueglia, E.1    Champigny, G.2    Lazdunski, M.3    Barbry, P.4
  • 11
    • 0035887045 scopus 로고    scopus 로고
    • + channel
    • + channel. EMBO J. 20, 5595-5602 (2001).
    • (2001) EMBO J. , vol.20 , pp. 5595-5602
    • Poët, M.1
  • 13
    • 0019554835 scopus 로고
    • Intracellular pH
    • Roos, A. & Boron, W. F. Intracellular pH. Physiol. Rev. 61, 296-434 (1981).
    • (1981) Physiol. Rev. , vol.61 , pp. 296-434
    • Roos, A.1    Boron, W.F.2
  • 14
    • 0015499163 scopus 로고
    • Ion transfer across lipid membranes in the presence of gramicidin A. II. The ion selectivity
    • Myers, V. B. & Haydon, D. A. Ion transfer across lipid membranes in the presence of gramicidin A. II. The ion selectivity. Biochim. Biophys. Acta 274, 313-322 (1972).
    • (1972) Biochim. Biophys. Acta , vol.274 , pp. 313-322
    • Myers, V.B.1    Haydon, D.A.2
  • 15
    • 0036086313 scopus 로고    scopus 로고
    • The ClC-3 chloride channel promotes acidification of lysosomes in CHO-K1 and Huh-7 cells
    • Li, X., Wang, T., Zhao, Z. & Weinman, S. A. The ClC-3 chloride channel promotes acidification of lysosomes in CHO-K1 and Huh-7 cells. Am. J. Physiol. Cell Physiol. 282, C1483-C1491 (2002).
    • (2002) Am. J. Physiol. Cell Physiol. , vol.282
    • Li, X.1    Wang, T.2    Zhao, Z.3    Weinman, S.A.4
  • 16
    • 0037418859 scopus 로고    scopus 로고
    • Gating the selectivity filter in ClC chloride channels
    • Dutzler, R., Campbell, E. B. & MacKinnon, R. Gating the selectivity filter in ClC chloride channels. Science 300, 108-112 (2003).
    • (2003) Science , vol.300 , pp. 108-112
    • Dutzler, R.1    Campbell, E.B.2    MacKinnon, R.3
  • 17
    • 0141513678 scopus 로고    scopus 로고
    • Gating competence of constitutively open CLC-0 mutants revealed by the interaction with a small organic inhibitor
    • Traverso, S., Elia, L. & Pusch, M. Gating competence of constitutively open CLC-0 mutants revealed by the interaction with a small organic inhibitor. J. Gen. Physiol. 122, 295-306 (2003).
    • (2003) J. Gen. Physiol. , vol.122 , pp. 295-306
    • Traverso, S.1    Elia, L.2    Pusch, M.3
  • 18
    • 0034637572 scopus 로고    scopus 로고
    • Functional and structural analysis of ClC-K chloride channels involved in renal disease
    • Waldegger, S. & Jentsch, T. J. Functional and structural analysis of ClC-K chloride channels involved in renal disease. J. Biol. Chem. 275, 24527-24533 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 24527-24533
    • Waldegger, S.1    Jentsch, T.J.2
  • 19
    • 0031468569 scopus 로고    scopus 로고
    • Pore-forming segments in voltage-gated chloride channels
    • Fahlke, C., Yu, H. T., Beck, C. L., Rhodes, T. H. & George, A. L. Jr Pore-forming segments in voltage-gated chloride channels. Nature 390, 529-532 (1997).
    • (1997) Nature , vol.390 , pp. 529-532
    • Fahlke, C.1    Yu, H.T.2    Beck, C.L.3    Rhodes, T.H.4    George Jr., A.L.5
  • 20
    • 0037274891 scopus 로고    scopus 로고
    • The ClC-5 chloride channel knock-out mouse - An animal model for Dent's disease
    • Günther, W., Piwon, N. & Jentsch, T. J. The ClC-5 chloride channel knock-out mouse - an animal model for Dent's disease. Pflügers Arch. 445, 456-462 (2003).
    • (2003) Pflügers Arch. , vol.445 , pp. 456-462
    • Günther, W.1    Piwon, N.2    Jentsch, T.J.3
  • 21
    • 17744375755 scopus 로고    scopus 로고
    • Disruption of ClC-3, a chloride channel expressed on synaptic vesicles, leads to a loss of the hippocampus
    • Stobrawa, S. M. et al. Disruption of ClC-3, a chloride channel expressed on synaptic vesicles, leads to a loss of the hippocampus. Neuron 29, 185-196 (2001).
    • (2001) Neuron , vol.29 , pp. 185-196
    • Stobrawa, S.M.1
  • 22
    • 12544249991 scopus 로고    scopus 로고
    • ClC-3 chloride channels facilitate endosomal acidification and chloride accumulation
    • Hara-Chikuma, M. et al. ClC-3 chloride channels facilitate endosomal acidification and chloride accumulation. J. Biol. Chem. 280, 1241-1247 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 1241-1247
    • Hara-Chikuma, M.1
  • 23
    • 0035998271 scopus 로고    scopus 로고
    • CLC-3 deficiency leads to phenotypes similar to human neuronal ceroid lipofuscinosis
    • Yoshikawa, M. et al. CLC-3 deficiency leads to phenotypes similar to human neuronal ceroid lipofuscinosis. Genes Cells 7, 597-605 (2002).
    • (2002) Genes Cells , vol.7 , pp. 597-605
    • Yoshikawa, M.1
  • 25
    • 0032506116 scopus 로고    scopus 로고
    • Chloride is an allosteric effector of copper assembly for the yeast multicopper oxidase Fet3p: An unexpected role for intracellular chloride channels
    • Davis-Kaplan, S. R., Askwith, C. C., Bengtzen, A. C., Radisky, D. & Kaplan, J. Chloride is an allosteric effector of copper assembly for the yeast multicopper oxidase Fet3p: an unexpected role for intracellular chloride channels. Proc. Natl Acad. Sci. USA 95, 13641-13645 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 13641-13645
    • Davis-Kaplan, S.R.1    Askwith, C.C.2    Bengtzen, A.C.3    Radisky, D.4    Kaplan, J.5
  • 26
    • 0036083537 scopus 로고    scopus 로고
    • Molecular structure and physiological function of chloride channels
    • Jentsch, T. J., Stein, V., Weinreich, F. & Zdebik, A. A. Molecular structure and physiological function of chloride channels. Physiol. Rev. 82, 503-568 (2002).
    • (2002) Physiol. Rev. , vol.82 , pp. 503-568
    • Jentsch, T.J.1    Stein, V.2    Weinreich, F.3    Zdebik, A.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.