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Volumn 74, Issue , 2012, Pages 69-86

Lysosomal acidification mechanisms

Author keywords

Channel; ClC 7; Counterion; Transporter; V ATPase

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CATION; CHLORIDE CHANNEL; COUNTERION; HYDROGEN POTASSIUM ADENOSINE TRIPHOSPHATASE; TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 84857260144     PISSN: 00664278     EISSN: 15451585     Source Type: Book Series    
DOI: 10.1146/annurev-physiol-012110-142317     Document Type: Article
Times cited : (895)

References (92)
  • 2
    • 0014429803 scopus 로고
    • Digestive activity of lysosomes. I. The digestion of proteins by extracts of rat liver lysosomes
    • Coffey JW, De Duve C. 1968. Digestive activity of lysosomes. I. The digestion of proteins by extracts of rat liver lysosomes. J. Biol. Chem. 243:3255-63
    • (1968) J. Biol. Chem. , vol.243 , pp. 3255-63
    • Coffey, J.W.1    De Duve, C.2
  • 4
    • 35448946098 scopus 로고    scopus 로고
    • Vacuolar ATPases: Rotary proton pumps in physiology and pathophysiology
    • DOI 10.1038/nrm2272, PII NRM2272
    • Forgac M. 2007. Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology. Nat. Rev. Mol. Cell Biol. 8:917-29 (Pubitemid 47622561)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.11 , pp. 917-929
    • Forgac, M.1
  • 5
    • 0038606551 scopus 로고    scopus 로고
    • Subunit rotation of vacuolar-type proton pumping ATPase. Relative rotation of the G and c subunits
    • DOI 10.1074/jbc.M302756200
    • Hirata T, Iwamoto-Kihara A, Sun-Wada GH, Okajima T, Wada Y, Futai M. 2003. Subunit rotation of vacuolar-type proton pumping ATPase: relative rotation of the G and C subunits. J. Biol. Chem. 278:23714-19 (Pubitemid 36830195)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.26 , pp. 23714-23719
    • Hirata, T.1    Iwamoto-Kihara, A.2    Sun-Wada, G.-H.3    Okajima, T.4    Wada, Y.5    Futai, M.6
  • 7
    • 0023930674 scopus 로고
    • Topography and subunit stoichiometry of the coated vesicle proton pump
    • Arai H, Terres G, Pink S, Forgac M. 1988. Topography and subunit stoichiometry of the coated vesicle proton pump. J. Biol. Chem. 263:8796-802
    • (1988) J. Biol. Chem. , vol.263 , pp. 8796-802
    • Arai, H.1    Terres, G.2    Pink, S.3    Forgac, M.4
  • 8
    • 0020491150 scopus 로고
    • H+ ATPase of chromaffin granules. Kinetics, regulation, and stoichiometry
    • Johnson RG, Beers MF, Scarpa A. 1982. H+ ATPase of chromaffin granules. Kinetics, regulation, and stoichiometry. J. Biol. Chem. 257:10701-7
    • (1982) J. Biol. Chem. , vol.257 , pp. 10701-7
    • Johnson, R.G.1    Beers, M.F.2    Scarpa, A.3
  • 9
    • 0027362647 scopus 로고
    • +-ATPase by a pyrophosphate-generated proton electrochemical gradient
    • DOI 10.1006/abbi.1993.1530
    • Schmidt AL, Briskin DP. 1993. Reversal of the red beet tonoplast H+-ATPase by a pyrophosphategenerated proton electrochemical gradient. Arch. Biochem. Biophys. 306:407-14 (Pubitemid 23314465)
    • (1993) Archives of Biochemistry and Biophysics , vol.306 , Issue.2 , pp. 407-414
    • Schmidt, A.L.1    Briskin, D.P.2
  • 10
    • 0034044037 scopus 로고    scopus 로고
    • The mechanochemistry of V-ATPase proton pumps
    • Grabe M, Wang H, Oster G. 2000. The mechanochemistry of V-ATPase proton pumps. Biophys. J. 78:2798-813 (Pubitemid 30396915)
    • (2000) Biophysical Journal , vol.78 , Issue.6 , pp. 2798-2813
    • Grabe, M.1    Wang, H.2    Oster, G.3
  • 11
    • 0345683495 scopus 로고    scopus 로고
    • The vacuolar H+-ATPase of lemon fruits is regulated by variable H+/ATP coupling and slip
    • Muller ML, Jensen M, Taiz L. 1999. The vacuolar H+-ATPase of lemon fruits is regulated by variable H+/ATP coupling and slip. J. Biol. Chem. 274:10706-16
    • (1999) J. Biol. Chem. , vol.274 , pp. 10706-16
    • Muller, M.L.1    Jensen, M.2    Taiz, L.3
  • 12
    • 0020996054 scopus 로고
    • Electrogenic nature of lysosomal proton pump as revealed with a cyanine dye
    • Ohkuma S, Moriyama Y, Takano T. 1983. Electrogenic nature of lysosomal proton pump as revealed with a cyanine dye. J. Biochem. 94:1935-43
    • (1983) J. Biochem. , vol.94 , pp. 1935-43
    • Ohkuma, S.1    Moriyama, Y.2    Takano, T.3
  • 14
    • 0024342428 scopus 로고
    • + translocating ATPase and pyrophosphatase of the vacuolar-lysosomal compartment
    • Hedrich R, Kurkdjian A, Guern J, Flugge UI. 1989. Comparative studies on the electrical properties of the H+ translocating ATPase and pyrophosphatase of the vacuolar-lysosomal compartment. EMBO J. 8:2835-41 (Pubitemid 19274984)
    • (1989) EMBO Journal , vol.8 , Issue.10 , pp. 2835-2841
    • Hedrich, R.1    Kurkdjian, A.2    Guern, J.3    Flugge, U.I.4
  • 15
    • 0344982110 scopus 로고    scopus 로고
    • Electrophysiological analysis of the yeast V-Type proton pump: Variable coupling ratio and proton shunt
    • Kettner C, Bertl A, Obermeyer G, Slayman C, Bihler H. 2003. Electrophysiological analysis of the yeast V-type proton pump: variable coupling ratio and proton shunt. Biophys. J. 85:3730-38 (Pubitemid 37490284)
    • (2003) Biophysical Journal , vol.85 , Issue.6 , pp. 3730-3738
    • Kettner, C.1    Bertl, A.2    Obermeyer, G.3    Slayman, C.4    Bihler, H.5
  • 17
    • 0029063512 scopus 로고
    • Disassembly and reassembly of the yeast vacuolar H+-ATPase in vivo
    • Kane PM. 1995. Disassembly and reassembly of the yeast vacuolar H+-ATPase in vivo. J. Biol. Chem. 270:17025-32
    • (1995) J. Biol. Chem. , vol.270 , pp. 17025-32
    • Kane, P.M.1
  • 18
    • 0035067367 scopus 로고    scopus 로고
    • Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly
    • DOI 10.1038/35070067
    • Seol JH, Shevchenko A, Deshaies RJ. 2001. Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly. Nat. Cell Biol. 3:384-91 (Pubitemid 32288446)
    • (2001) Nature Cell Biology , vol.3 , Issue.4 , pp. 384-391
    • Seol, J.H.1    Shevchenko, A.2    Shevchenko, A.3    Deshaies, R.J.4
  • 19
    • 0037134525 scopus 로고    scopus 로고
    • The RAVE complex is essential for stable assembly of the yeast V-ATpase
    • DOI 10.1074/jbc.M200682200
    • Smardon AM, Tarsio M, Kane PM. 2002. The RAVE complex is essential for stable assembly of the yeast V-ATPase. J. Biol. Chem. 277:13831-39 (Pubitemid 34967988)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.16 , pp. 13831-13839
    • Smardon, A.M.1    Tarsio, M.2    Kane, P.M.3
  • 20
    • 34548826217 scopus 로고    scopus 로고
    • +-ATPase
    • DOI 10.1074/jbc.M703627200
    • Smardon AM, Kane PM. 2007. RAVE is essential for the efficient assembly of the C subunit with the vacuolar H+-ATPase. J. Biol. Chem. 282:26185-94 (Pubitemid 47443786)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.36 , pp. 26185-26194
    • Smardon, A.M.1    Kane, P.M.2
  • 21
    • 34548300007 scopus 로고    scopus 로고
    • +-ATPase is essential for the assembly and activity of the proton pump
    • DOI 10.1074/jbc.M702598200
    • Lu M, Ammar D, Ives H, Albrecht F, Gluck SL. 2007. Physical interaction between aldolase and vacuolar H+-ATPase is essential for the assembly and activity of the proton pump. J. Biol. Chem. 282:24495-503 (Pubitemid 47347536)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.34 , pp. 24495-24503
    • Lu, M.1    Ammar, D.2    Ives, H.3    Albrecht, F.4    Gluck, S.L.5
  • 22
    • 0035816719 scopus 로고    scopus 로고
    • Microtubules are involved in glucose-dependent dissociation of the yeast vacuolar [H+]-ATPase in vivo
    • Xu T, Forgac M. 2001. Microtubules are involved in glucose-dependent dissociation of the yeast vacuolar [H+]-ATPase in vivo. J. Biol. Chem. 276:24855-61
    • (2001) J. Biol. Chem. , vol.276 , pp. 24855-61
    • Xu, T.1    Forgac, M.2
  • 23
    • 0026734768 scopus 로고
    • The VPH1 gene encodes a 95-kDa integral membrane polypeptide required for in vivo assembly and activity of the yeast vacuolar H+-ATPase
    • Manolson MF, Proteau D, Preston RA, Stenbit A, Roberts BT, et al. 1992. The VPH1 gene encodes a 95-kDa integral membrane polypeptide required for in vivo assembly and activity of the yeast vacuolar H+-ATPase. J. Biol. Chem. 267:14294-303
    • (1992) J. Biol. Chem. , vol.267 , pp. 14294-303
    • Manolson, M.F.1    Proteau, D.2    Preston, R.A.3    Stenbit, A.4    Roberts, B.T.5
  • 24
    • 0028224791 scopus 로고
    • STV1 gene encodes functional homologue of 95-kDa yeast vacuolar H+-ATPase subunit Vph1p
    • Manolson MF, Wu B, Proteau D, Taillon BE, Roberts BT, et al. 1994. STV1 gene encodes functional homologue of 95-kDa yeast vacuolar H+-ATPase subunit Vph1p. J. Biol. Chem. 269:14064-74
    • (1994) J. Biol. Chem. , vol.269 , pp. 14064-74
    • Manolson, M.F.1    Wu, B.2    Proteau, D.3    Taillon, B.E.4    Roberts, B.T.5
  • 25
    • 0035947711 scopus 로고    scopus 로고
    • Yeast V-ATPase complexes containing different isoforms of the 100-kDa a-subunit differ in coupling efficiency and in vivo dissociation
    • Kawasaki-Nishi S, Nishi T, ForgacM. 2001. Yeast V-ATPase complexes containing different isoforms of the 100-kDa a-subunit differ in coupling efficiency and in vivo dissociation. J. Biol. Chem. 276:17941-48
    • (2001) J. Biol. Chem. , vol.276 , pp. 17941-48
    • Kawasaki-Nishi, S.1    Nishi, T.2    Forgac, M.3
  • 26
    • 77953255215 scopus 로고    scopus 로고
    • Regulation and isoform function of the V-ATPases
    • Toei M, Saum R, Forgac M. 2010. Regulation and isoform function of the V-ATPases. Biochemistry 49:4715-23
    • (2010) Biochemistry , vol.49 , pp. 4715-23
    • Toei, M.1    Saum, R.2    Forgac, M.3
  • 30
    • 0018790497 scopus 로고
    • Evidence for an ATP-driven "proton pump" in rat liver lysosomes by basic dyes uptake
    • DellAntone P. 1979. Evidence for an ATP-driven "proton pump" in rat liver lysosomes by basic dyes uptake. Biochem. Biophys. Res. Commun. 86:180-89
    • (1979) Biochem. Biophys. Res. Commun. , vol.86 , pp. 180-89
    • Dellantone, P.1
  • 32
    • 0027381284 scopus 로고
    • Acidification of rat liver lysosomes: Quantitation and comparison with endosomes
    • Van Dyke RW. 1993. Acidification of rat liver lysosomes: quantitation and comparison with endosomes. Am. J. Physiol. Cell Physiol. 265:901-17
    • (1993) Am. J. Physiol. Cell Physiol. , vol.265 , pp. 901-17
    • Van Dyke, R.W.1
  • 33
    • 44849107047 scopus 로고    scopus 로고
    • + antiporter ClC-7 is the primary chloride permeation pathway in lysosomes
    • DOI 10.1038/nature06907, PII NATURE06907
    • Graves AR, Curran PK, Smith CL, Mindell JA. 2008. The Cl /H+ antiporter ClC-7 is the primary chloride permeation pathway in lysosomes. Nature 453:788-92 (Pubitemid 351793780)
    • (2008) Nature , vol.453 , Issue.7196 , pp. 788-792
    • Graves, A.R.1    Curran, P.K.2    Smith, C.L.3    Mindell, J.A.4
  • 35
    • 47249144272 scopus 로고    scopus 로고
    • P2X7 receptor differentially couples to distinct release pathways for IL-1βin mouse macrophage
    • Pelegrin P, Barroso-Gutierrez C, Surprenant A. 2008. P2X7 receptor differentially couples to distinct release pathways for IL-1βin mouse macrophage. J. Immunol. 180:7147-57
    • (2008) J. Immunol. , vol.180 , pp. 7147-57
    • Pelegrin, P.1    Barroso-Gutierrez, C.2    Surprenant, A.3
  • 36
    • 33750473352 scopus 로고    scopus 로고
    • 7 receptor
    • DOI 10.1038/sj.emboj.7601378, PII 7601378
    • Pelegrin P, Surprenant A. 2006. Pannexin-1 mediates large pore formation and interleukin-1βrelease by the ATP-gated P2X7 receptor. EMBO J. 25:5071-82 (Pubitemid 44658525)
    • (2006) EMBO Journal , vol.25 , Issue.21 , pp. 5071-5082
    • Pelegrin, P.1    Surprenant, A.2
  • 37
    • 0028279373 scopus 로고
    • Use of glycyl-L-phenylalanine 2-naphthylamide, a lysosome-disrupting cathepsin G substrate, to distinguish between lysosomes and prelysosomal endocytic vacuoles
    • Berg TO, Stromhaug E, Lovdal T, Seglen O, Berg T. 1994. Use of glycyl-L-phenylalanine 2- naphthylamide, a lysosome-disrupting cathepsin C substrate, to distinguish between lysosomes and prelysosomal endocytic vacuoles. Biochem. J. 300(Pt. 1):229-36 (Pubitemid 24151040)
    • (1994) Biochemical Journal , vol.300 , Issue.1 , pp. 229-236
    • Berg, T.O.1    Stromhaug, P.E.2    Lovdal, T.3    Seglen, P.O.4    Berg, T.5
  • 38
    • 33845864416 scopus 로고    scopus 로고
    • 2+ store in the boutons of hippocampal pyramidal cells
    • DOI 10.1016/j.neuropharm.2006.07.029, PII S0028390806002395
    • 2+ store in the boutons of hippocampal pyramidal cells. Neuropharmacology 52:126-35 (Pubitemid 46026834)
    • (2007) Neuropharmacology , vol.52 , Issue.1 , pp. 126-135
    • McGuinness, L.1    Bardo, S.J.2    Emptage, N.J.3
  • 39
    • 70349335633 scopus 로고    scopus 로고
    • ABC transporters: A riddle wrapped in a mystery inside an enigma
    • Jones PM, OMara ML, George AM. 2009. ABC transporters: a riddle wrapped in a mystery inside an enigma. Trends Biochem. Sci. 34:520-31
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 520-31
    • Jones, P.M.1    Omara, M.L.2    George, A.M.3
  • 40
    • 33645307384 scopus 로고    scopus 로고
    • The ABC protein turned chloride channel whose failure causes cystic fibrosis
    • Gadsby DC, Vergani P, Csanady L. 2006. The ABC protein turned chloride channel whose failure causes cystic fibrosis. Nature 440:477-83
    • (2006) Nature , vol.440 , pp. 477-83
    • Gadsby, D.C.1    Vergani, P.2    Csanady, L.3
  • 41
    • 67049172475 scopus 로고    scopus 로고
    • Defective organellar acidification as a cause of cystic fibrosis lung disease: Reexamination of a recurring hypothesis
    • Haggie PM, Verkman AS. 2009. Defective organellar acidification as a cause of cystic fibrosis lung disease: reexamination of a recurring hypothesis. Am. J. Physiol. Lung Cell Mol. Physiol. 296:859-67
    • (2009) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.296 , pp. 859-67
    • Haggie, P.M.1    Verkman, A.S.2
  • 42
    • 0025784535 scopus 로고
    • Defective acidification of intracellular organelles in cystic fibrosis
    • Barasch J, Kiss B, Prince A, Saiman L, Gruenert D, al-Awqati Q. 1991. Defective acidification of intracellular organelles in cystic fibrosis. Nature 352:70-73 (Pubitemid 21896700)
    • (1991) Nature , vol.352 , Issue.6330 , pp. 70-73
    • Barasch, J.1    Kiss, B.2    Prince, A.3    Saiman, L.4    Gruenert, D.5    Al-Awqati, Q.6
  • 44
    • 72149093771 scopus 로고    scopus 로고
    • Disease-causing mutations in the cystic fibrosis transmembrane conductance regulator determine the functional responses of alveolar macrophages
    • Deriy LV, Gomez EA, Zhang G, Beacham DW, Hopson JA, et al. 2009. Disease-causing mutations in the cystic fibrosis transmembrane conductance regulator determine the functional responses of alveolar macrophages. J. Biol. Chem. 284:35926-38
    • (2009) J. Biol. Chem. , vol.284 , pp. 35926-38
    • Deriy, L.V.1    Gomez, E.A.2    Zhang, G.3    Beacham, D.W.4    Hopson, J.A.5
  • 45
    • 0029984180 scopus 로고    scopus 로고
    • Evidence against defective trans-Golgi acidification in cystic fibrosis
    • DOI 10.1074/jbc.271.26.15542
    • Seksek O, Biwersi J, Verkman AS. 1996. Evidence against defective trans-Golgi acidification in cystic fibrosis. J. Biol. Chem. 271:15542-48 (Pubitemid 26225328)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.26 , pp. 15542-15548
    • Seksek, O.1    Biwersi, J.2    Verkman, A.S.3
  • 46
    • 0028045712 scopus 로고
    • Functional CFTR in endosomal compartment of CFTR-expressing fibroblasts and T84 cells
    • Biwersi J, Verkman AS. 1994. Functional CFTR in endosomal compartment of CFTR-expressing fibroblasts and T84 cells. Am. J. Physiol. Cell Physiol. 266:149-56
    • (1994) Am. J. Physiol. Cell Physiol. , vol.266 , pp. 149-56
    • Biwersi, J.1    Verkman, A.S.2
  • 47
    • 0026777811 scopus 로고
    • The cystic fibrosis transmembrane regulator is present and functional in endosomes. Role as a determinant of endosomal pH
    • Lukacs GL, Chang XB, Kartner N, Rotstein OD, Riordan JR, Grinstein S. 1992. The cystic fibrosis transmembrane regulator is present and functional in endosomes. Role as a determinant of endosomal pH. J. Biol. Chem. 267:14568-72
    • (1992) J. Biol. Chem. , vol.267 , pp. 14568-72
    • Lukacs, G.L.1    Chang, X.B.2    Kartner, N.3    Rotstein, O.D.4    Riordan, J.R.5    Grinstein, S.6
  • 48
    • 35748973573 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane conductance regulator-independent phagosomal acidification in macrophages
    • DOI 10.1074/jbc.M705296200
    • Haggie PM, Verkman AS. 2007. Cystic fibrosis transmembrane conductance regulator-independent phagosomal acidification in macrophages. J. Biol. Chem. 282:31422-28 (Pubitemid 350044877)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.43 , pp. 31422-31428
    • Haggie, P.M.1    Verkman, A.S.2
  • 49
    • 65549134742 scopus 로고    scopus 로고
    • Unimpaired lysosomal acidification in respiratory epithelial cells in cystic fibrosis
    • Haggie PM, Verkman AS. 2009. Unimpaired lysosomal acidification in respiratory epithelial cells in cystic fibrosis. J. Biol. Chem. 284:7681-86
    • (2009) J. Biol. Chem. , vol.284 , pp. 7681-86
    • Haggie, P.M.1    Verkman, A.S.2
  • 50
    • 0018801493 scopus 로고
    • A voltage-gated anion channel from the electric organ of Torpedo californica
    • White MM, Miller C. 1979. A voltage-gated anion channel from the electric organ of Torpedo californica. J. Biol. Chem. 254:10161-66
    • (1979) J. Biol. Chem. , vol.254 , pp. 10161-66
    • White, M.M.1    Miller, C.2
  • 51
    • 0025200567 scopus 로고
    • Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes
    • Jentsch TJ, Steinmeyer K, Schwarz G. 1990. Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes. Nature 348:510-14 (Pubitemid 120015094)
    • (1990) Nature , vol.348 , Issue.6301 , pp. 510-514
    • Jentsch, T.J.1    Steinmeyer, K.2    Schwarz, G.3
  • 52
    • 39849092445 scopus 로고    scopus 로고
    • CLC chloride channels and transporters: From genes to protein structure, pathology and physiology
    • DOI 10.1080/10409230701829110, PII 791049831
    • Jentsch TJ. 2008. CLC chloride channels and transporters: from genes to protein structure, pathology and physiology. Crit. Rev. Biochem. Mol. Biol. 43:3-36 (Pubitemid 351315859)
    • (2008) Critical Reviews in Biochemistry and Molecular Biology , vol.43 , Issue.1 , pp. 3-36
    • Jentsch, T.J.1
  • 54
    • 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 EB, Cadene M, Chait BT, MacKinnon R. 2002. X-ray structure of a ClC chloride channel at 3. 0 A reveals the molecular basis of anion selectivity. Nature 415:287-94 (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
  • 55
    • 78049362741 scopus 로고    scopus 로고
    • Structure of a eukaryotic CLC transporter defines an intermediate state in the transport cycle
    • Feng L, Campbell EB, Hsiung Y, Mackinnon R. 2010. Structure of a eukaryotic CLC transporter defines an intermediate state in the transport cycle. Science 330:635-41
    • (2010) Science , vol.330 , pp. 635-41
    • Feng, L.1    Campbell, E.B.2    Hsiung, Y.3    MacKinnon, R.4
  • 56
    • 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. Ser. B 299:401-11
    • (1982) Philos. Trans. R. Soc. Lond. Ser. B , vol.299 , pp. 401-11
    • Miller, C.1
  • 57
    • 0029661878 scopus 로고    scopus 로고
    • Homodimeric architecture of a CIC-type chloride ion channel
    • DOI 10.1038/383337a0
    • Middleton RE, Pheasant DJ, Miller C. 1996. Homodimeric architecture of a ClC-type chloride ion channel. Nature 383:337-40 (Pubitemid 26321763)
    • (1996) Nature , vol.383 , Issue.6598 , pp. 337-340
    • Middleton, R.E.1    Pheasant, D.J.2    Miller, C.3
  • 58
    • 1542288949 scopus 로고    scopus 로고
    • - channels
    • DOI 10.1038/nature02314
    • Accardi A, Miller C. 2004. Secondary active transport mediated by a prokaryotic homologue of ClC Cl channels. Nature 427:803-7 (Pubitemid 38297735)
    • (2004) Nature , vol.427 , Issue.6977 , pp. 803-807
    • Accardi, A.1    Miller, C.2
  • 60
    • 22944479662 scopus 로고    scopus 로고
    • Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins
    • DOI 10.1038/nature03860
    • Scheel O, Zdebik AA, Lourdel S, Jentsch TJ. 2005. Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins. Nature 436:424-27 (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
  • 61
    • 22944475536 scopus 로고    scopus 로고
    • Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5
    • DOI 10.1038/nature03720
    • Picollo A, Pusch M. 2005. Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5. Nature 436:420-23 (Pubitemid 41059054)
    • (2005) Nature , vol.436 , Issue.7049 , pp. 420-423
    • Picollo, A.1    Pusch, M.2
  • 62
    • 0032493276 scopus 로고    scopus 로고
    • ClC-5, the chloride channelmutated in Dents disease, colocalizes with the proton pump in endocytotically active kidney cells
    • Gunther W, Luchow A, Cluzeaud F, Vandewalle A, Jentsch TJ. 1998. ClC-5, the chloride channelmutated in Dents disease, colocalizes with the proton pump in endocytotically active kidney cells. Proc. Natl. Acad. Sci. USA 95:8075-80
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8075-80
    • Gunther, W.1    Luchow, A.2    Cluzeaud, F.3    Vandewalle, A.4    Jentsch, T.J.5
  • 64
    • 0034676433 scopus 로고    scopus 로고
    • ClC-5 Cl-channel disruption impairs endocytosis in a mouse model for Dents disease
    • Piwon N, Gunther W, Schwake M, Bosl MR, Jentsch TJ. 2000. ClC-5 Cl-channel disruption impairs endocytosis in a mouse model for Dents disease. Nature 408:369-73
    • (2000) Nature , vol.408 , pp. 369-73
    • Piwon, N.1    Gunther, W.2    Schwake, M.3    Bosl, M.R.4    Jentsch, T.J.5
  • 66
    • 0029589606 scopus 로고
    • ClC-6 and ClC-7 are two novel broadly expressed members of the CLC chloride channel family
    • DOI 10.1016/0014-5793(95)01298-2
    • Brandt S, Jentsch TJ. 1995. ClC-6 and ClC-7 are two novel broadly expressed members of the CLC chloride channel family. FEBS Lett. 377:15-20 (Pubitemid 26008977)
    • (1995) FEBS Letters , vol.377 , Issue.1 , pp. 15-20
    • Brandt, S.1    Jentsch, T.J.2
  • 68
    • 0037315475 scopus 로고    scopus 로고
    • Chloride channel 7 (CLCN7) gene mutations in intermediate autosomal recessive osteopetrosis
    • Campos-Xavier AB, Saraiva JM, Ribeiro LM, Munnich A, Cormier-Daire V. 2003. Chloride channel 7 (CLCN7) gene mutations in intermediate autosomal recessive osteopetrosis. Hum. Genet. 112:186-89 (Pubitemid 36869102)
    • (2003) Human Genetics , vol.112 , Issue.2 , pp. 186-189
    • Campos-Xavier, A.B.1    Saraiva, J.M.2    Ribeiro, L.M.3    Munnich, A.4    Cormier-Daire, V.5
  • 71
    • 33644827486 scopus 로고    scopus 로고
    • Polymorphisms in the CLCN7 gene modulate bone density in postmenopausal women and in patients with autosomal dominant osteopetrosis type II
    • DOI 10.1210/jc.2005-2017
    • Kornak U, Ostertag A, Branger S, Benichou O, de Vernejoul MC. 2006. Polymorphisms in the CLCN7 gene modulate bone density in postmenopausal women and in patients with autosomal dominant osteopetrosis type II. J. Clin. Endocrinol. Metab. 91:995-1000 (Pubitemid 43357771)
    • (2006) Journal of Clinical Endocrinology and Metabolism , vol.91 , Issue.3 , pp. 995-1000
    • Kornak, U.1    Ostertag, A.2    Branger, S.3    Benichou, O.4    De Vernejoul, M.-C.5
  • 73
    • 33644861728 scopus 로고    scopus 로고
    • ClC-7 requires Ostm1 as a β-subunit to support bone resorption and lysosomal function
    • DOI 10.1038/nature04535, PII N04535
    • Lange PF, Wartosch L, Jentsch TJ, Fuhrmann JC. 2006. ClC-7 requires Ostm1 as a β-subunit to support bone resorption and lysosomal function. Nature 440:220-23 (Pubitemid 43372100)
    • (2006) Nature , vol.440 , Issue.7081 , pp. 220-223
    • Lange, P.F.1    Wartosch, L.2    Jentsch, T.J.3    Fuhrmann, J.C.4
  • 74
    • 79955644635 scopus 로고    scopus 로고
    • Lysosomal pH and analysis of the counter ion pathways that support acidification
    • DiCiccio JE, Steinberg BE. 2011. Lysosomal pH and analysis of the counter ion pathways that support acidification. J. Gen. Physiol. 137:385-90
    • (2011) J. Gen. Physiol. , vol.137 , pp. 385-90
    • Diciccio, J.E.1    Steinberg, B.E.2
  • 75
    • 69249230769 scopus 로고    scopus 로고
    • Mammalian cell-cycle regulation: Several Cdks, numerous cyclins and diverse compensatory mechanisms
    • Satyanarayana A, Kaldis P. 2009. Mammalian cell-cycle regulation: several Cdks, numerous cyclins and diverse compensatory mechanisms. Oncogene 28:2925-39
    • (2009) Oncogene , vol.28 , pp. 2925-39
    • Satyanarayana, A.1    Kaldis, P.2
  • 76
    • 0032978418 scopus 로고    scopus 로고
    • Utilization of genetically altered animals in the pharmaceutical industry
    • Rudmann DG, Durham SK. 1999. Utilization of genetically altered animals in the pharmaceutical industry. Toxicol. Pathol. 27:111-14 (Pubitemid 29075755)
    • (1999) Toxicologic Pathology , vol.27 , Issue.1 , pp. 111-114
    • Rudmann, D.G.1    Durham, S.K.2
  • 78
    • 72749119040 scopus 로고    scopus 로고
    • Lysosomal degradation of endocytosed proteins depends on the chloride transport protein ClC-7
    • Wartosch L, Fuhrmann JC, Schweizer M, Stauber T, Jentsch TJ. 2009. Lysosomal degradation of endocytosed proteins depends on the chloride transport protein ClC-7. FASEB J. 23:4056-68
    • (2009) FASEB J. , vol.23 , pp. 4056-68
    • Wartosch, L.1    Fuhrmann, J.C.2    Schweizer, M.3    Stauber, T.4    Jentsch, T.J.5
  • 79
    • 0033568737 scopus 로고    scopus 로고
    • Location of the binding site for chloride ion activation of cathepsin C
    • DOI 10.1046/j.1432-1327.1999.00697.x
    • Cigic B, Pain RH. 1999. Location of the binding site for chloride ion activation of cathepsin C. Eur. J. Biochem. 264:944-51 (Pubitemid 29437226)
    • (1999) European Journal of Biochemistry , vol.264 , Issue.3 , pp. 944-951
    • Cigic, B.1    Pain, R.H.2
  • 80
    • 0037418859 scopus 로고    scopus 로고
    • Gating the selectivity filter in ClC chloride channels
    • DOI 10.1126/science.1082708
    • Dutzler R, Campbell EB, MacKinnon R. 2003. Gating the selectivity filter in ClC chloride channels. Science 300:108-12 (Pubitemid 36423038)
    • (2003) Science , vol.300 , Issue.5616 , pp. 108-112
    • Dutzler, R.1    Campbell, E.B.2    MacKinnon, R.3
  • 81
    • 77953564940 scopus 로고    scopus 로고
    • Lysosomal pathology and osteopetrosis upon loss of H+-driven lysosomal Cl accumulation
    • Weinert S, Jabs S, Supanchart C, Schweizer M, Gimber N, et al. 2010. Lysosomal pathology and osteopetrosis upon loss of H+-driven lysosomal Cl accumulation. Science 328:1401-3
    • (2010) Science , vol.328 , pp. 1401-3
    • Weinert, S.1    Jabs, S.2    Supanchart, C.3    Schweizer, M.4    Gimber, N.5
  • 82
    • 40849105303 scopus 로고    scopus 로고
    • Degradation of fibrillar forms of Alzheimer's amyloid β-peptide by macrophages
    • DOI 10.1016/j.neurobiolaging.2006.12.001, PII S0197458006004593
    • Majumdar A, Chung H, Dolios G, Wang R, Asamoah N, et al. 2008. Degradation of fibrillar forms of Alzheimers amyloid β-peptide by macrophages. Neurobiol. Aging 29:707-15 (Pubitemid 351400828)
    • (2008) Neurobiology of Aging , vol.29 , Issue.5 , pp. 707-715
    • Majumdar, A.1    Chung, H.2    Dolios, G.3    Wang, R.4    Asamoah, N.5    Lobel, P.6    Maxfield, F.R.7
  • 84
    • 79955970157 scopus 로고    scopus 로고
    • Degradation of Alzheimers amyloid fibrils by microglia requires delivery of ClC-7 to lysosomes
    • Majumdar A, Capetillo-Zarate E, Cruz D, Gouras GK, Maxfield FR. 2011. Degradation of Alzheimers amyloid fibrils by microglia requires delivery of ClC-7 to lysosomes. Mol. Biol. Cell 22:1664-76
    • (2011) Mol. Biol. Cell , vol.22 , pp. 1664-76
    • Majumdar, A.1    Capetillo-Zarate, E.2    Cruz, D.3    Gouras, G.K.4    Maxfield, F.R.5
  • 87
    • 0032965433 scopus 로고    scopus 로고
    • Elevated lysosomal pH in mucolipidosis type IV cells
    • DOI 10.1016/S0009-8981(98)00183-1, PII S0009898198001831
    • Bach G, Chen CS, Pagano RE. 1999. Elevated lysosomal pH in Mucolipidosis type IV cells. Clin. Chim. Acta 280:173-79 (Pubitemid 29094592)
    • (1999) Clinica Chimica Acta , vol.280 , Issue.1-2 , pp. 173-179
    • Bach, G.1    Chen, C.-S.2    Pagano, R.E.3
  • 88
    • 33748572921 scopus 로고    scopus 로고
    • Mucolipin-1 is a lysosomal membrane protein required for intracellular lactosylceramide traffic
    • DOI 10.1111/j.1600-0854.2006.00475.x
    • Pryor PR, Reimann F, Gribble FM, Luzio JP. 2006. Mucolipin-1 is a lysosomal membrane protein required for intracellular lactosylceramide traffic. Traffic 7:1388-98 (Pubitemid 44364176)
    • (2006) Traffic , vol.7 , Issue.10 , pp. 1388-1398
    • Pryor, P.R.1    Reimann, F.2    Gribble, F.M.3    Luzio, J.P.4
  • 90
    • 54049156405 scopus 로고    scopus 로고
    • The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel
    • Dong XP, Cheng X, Mills E, Delling M, Wang F, et al. 2008. The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel. Nature 455:992-96
    • (2008) Nature , vol.455 , pp. 992-96
    • Dong, X.P.1    Cheng, X.2    Mills, E.3    Delling, M.4    Wang, F.5
  • 92
    • 67349287016 scopus 로고    scopus 로고
    • NAADP mobilizes calcium from acidic organelles through two-pore channels
    • Calcraft PJ, Ruas M, Pan Z, Cheng X, Arredouani A, et al. 2009. NAADP mobilizes calcium from acidic organelles through two-pore channels. Nature 459:596-600
    • (2009) Nature , vol.459 , pp. 596-600
    • Calcraft, P.J.1    Ruas, M.2    Pan, Z.3    Cheng, X.4    Arredouani, A.5


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