메뉴 건너뛰기




Volumn 10, Issue 5, 2009, Pages 344-352

Ion channels versus ion pumps: The principal difference, in principle

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATASE (CALCIUM); ADENOSINE TRIPHOSPHATASE (POTASSIUM); CHLORIDE CHANNEL; HYDROGEN POTASSIUM ADENOSINE TRIPHOSPHATASE; ION CHANNEL; NEUROTRANSMITTER; POTASSIUM CHANNEL;

EID: 67349185408     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm2668     Document Type: Review
Times cited : (377)

References (87)
  • 3
    • 0018799006 scopus 로고
    • A channel mechanism for electrogenic ion pumps
    • Läuger, P. A channel mechanism for electrogenic ion pumps. Biochim. Biophys. Acta 552, 143-161 (1979).
    • (1979) Biochim. Biophys. Acta , vol.552 , pp. 143-161
    • Läuger, P.1
  • 4
    • 51249194404 scopus 로고
    • Contributions to the theory of active transport. II. The gate-type non-carrier mechanism and generalization concerning tracer glow efficiency, and measurement of energy expenditure
    • Patlak, C. S. Contributions to the theory of active transport. II. The gate-type non-carrier mechanism and generalization concerning tracer glow efficiency, and measurement of energy expenditure. Bull. Math. Biophys. 19, 209-235 (1957).
    • (1957) Bull. Math. Biophys , vol.19 , pp. 209-235
    • Patlak, C.S.1
  • 5
    • 0013875762 scopus 로고
    • Inhibition of parallel flux and augmentation of counter flux shown by transport models not involving a mobile carrier
    • Vidaver, G. A. Inhibition of parallel flux and augmentation of counter flux shown by transport models not involving a mobile carrier. J. Theor. Biol. 10, 301-306 (1966).
    • (1966) J. Theor. Biol , vol.10 , pp. 301-306
    • Vidaver, G.A.1
  • 6
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetzky, O. Simple allosteric model for membrane pumps. Nature 27, 969-970 (1966).
    • (1966) Nature , vol.27 , pp. 969-970
    • Jardetzky, O.1
  • 7
    • 0242657337 scopus 로고    scopus 로고
    • Potassium channels
    • MacKinnon, R. Potassium channels. FEBS Lett. 555, 62-65 (2003).
    • (2003) FEBS Lett , vol.555 , pp. 62-65
    • MacKinnon, R.1
  • 8
    • 0035499892 scopus 로고    scopus 로고
    • Zhou, Y., Morais-Cabral, J. H., Kaufman, A. &MacKinnon, R. Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 Å resolution. Nature 414, 43-48 (2001). This high-resolution structure revealed the mechanism of the K ion channel selectivity filter. Each of its four K ion sites lies at the centre of a cage of eight carbonyl oxygens that mimic those of the eight water molecules found surrounding the hydrated K ion in the large central cavity. The selectivity filter minimizes the energetic cost of transferring K ions from the aqueous environment to the K ion channel interior.
    • Zhou, Y., Morais-Cabral, J. H., Kaufman, A. &MacKinnon, R. Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 Å resolution. Nature 414, 43-48 (2001). This high-resolution structure revealed the mechanism of the K ion channel selectivity filter. Each of its four K ion sites lies at the centre of a cage of eight carbonyl oxygens that mimic those of the eight water molecules found surrounding the hydrated K ion in the large central cavity. The selectivity filter minimizes the energetic cost of transferring K ions from the aqueous environment to the K ion channel interior.
  • 9
    • 0035499447 scopus 로고    scopus 로고
    • Energetic optimization of ion conduction rate by the K+ selectivity filter
    • Morais-Cabral, J. H., Zhou, Y. & MacKinnon, R. Energetic optimization of ion conduction rate by the K+ selectivity filter. Nature 414, 37-42 (2001).
    • (2001) Nature , vol.414 , pp. 37-42
    • Morais-Cabral, J.H.1    Zhou, Y.2    MacKinnon, R.3
  • 10
    • 0015523849 scopus 로고
    • Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase
    • Post, R. L., Hegyvary, C. & Kume, S. Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase. J. Biol. Chem. 247, 6530-6540 (1972).
    • (1972) J. Biol. Chem , vol.247 , pp. 6530-6540
    • Post, R.L.1    Hegyvary, C.2    Kume, S.3
  • 11
    • 0034621834 scopus 로고    scopus 로고
    • Toyoshima, C., Nakasako, M., Nomura, H. &Ogawa, H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature 405, 647-655 (2000). The first X-ray crystal structure of a P-type ATPase ion pump. The two transported Ca ions were found buried side by side in their binding sites, deep within the transmembrane domain and inaccessible from either side.
    • Toyoshima, C., Nakasako, M., Nomura, H. &Ogawa, H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature 405, 647-655 (2000). The first X-ray crystal structure of a P-type ATPase ion pump. The two transported Ca ions were found buried side by side in their binding sites, deep within the transmembrane domain and inaccessible from either side.
  • 12
    • 9244232176 scopus 로고    scopus 로고
    • Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues
    • Toyoshima, C., Nomura, H. & Tsuda, T. Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues. Nature 432, 361-368 (2004).
    • (2004) Nature , vol.432 , pp. 361-368
    • Toyoshima, C.1    Nomura, H.2    Tsuda, T.3
  • 13
    • 38049138584 scopus 로고    scopus 로고
    • How processing of aspartylphosphate is coupled to lumenal gating of the ion pathway in the calcium pump
    • Toyoshima, C., Norimatsu, Y., Iwasawa, S., Tsuda, T. &Ogawa, H. How processing of aspartylphosphate is coupled to lumenal gating of the ion pathway in the calcium pump. Proc. Natl Acad. Sci. USA 104, 19831-19836 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 19831-19836
    • Toyoshima, C.1    Norimatsu, Y.2    Iwasawa, S.3    Tsuda, T.4    Ogawa, H.5
  • 14
    • 0037043709 scopus 로고    scopus 로고
    • Structural changes in the calcium pump accompanying the dissociation of calcium
    • Toyoshima, C. & Nomura, H. Structural changes in the calcium pump accompanying the dissociation of calcium. Nature 418, 605-611 (2002).
    • (2002) Nature , vol.418 , pp. 605-611
    • Toyoshima, C.1    Nomura, H.2
  • 15
    • 3242888769 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump with a bound ATP analogue
    • Toyoshima, C. & Mizutani, T. Crystal structure of the calcium pump with a bound ATP analogue. Nature 430, 529-535 (2004).
    • (2004) Nature , vol.430 , pp. 529-535
    • Toyoshima, C.1    Mizutani, T.2
  • 17
    • 11144330054 scopus 로고    scopus 로고
    • Dephosphorylation of the calcium pump coupled to counterion occlusion
    • Olesen, C., Sorensen, T. L., Nielsen, R. C., Møller, J. V. &Nissen, P. Dephosphorylation of the calcium pump coupled to counterion occlusion. Science 306, 2251-2255 (2004).
    • (2004) Science , vol.306 , pp. 2251-2255
    • Olesen, C.1    Sorensen, T.L.2    Nielsen, R.C.3    Møller, J.V.4    Nissen, P.5
  • 18
    • 37249043376 scopus 로고    scopus 로고
    • The structural basis of calcium transport by the calcium pump
    • Olesen, C. et al. The structural basis of calcium transport by the calcium pump. Nature 450, 1036-1042 (2007).
    • (2007) Nature , vol.450 , pp. 1036-1042
    • Olesen, C.1
  • 19
    • 2942668632 scopus 로고    scopus 로고
    • Phosphoryl transfer and calcium ion occlusion in the calcium pump
    • Sørensen, T. L. M., Møller, J. V. & Nissen, P. Phosphoryl transfer and calcium ion occlusion in the calcium pump. Science 304, 1672-1675 (2004).
    • (2004) Science , vol.304 , pp. 1672-1675
    • Sørensen, T.L.M.1    Møller, J.V.2    Nissen, P.3
  • 20
    • 37249088547 scopus 로고    scopus 로고
    • Crystal structure of the sodiumpotassium pump
    • Morth, J. P. et al. Crystal structure of the sodiumpotassium pump. Nature 450, 1043-1049 (2007).
    • (2007) Nature , vol.450 , pp. 1043-1049
    • Morth, J.P.1
  • 21
    • 1542288949 scopus 로고    scopus 로고
    • Accardi, A. & Miller, C. Secondary active transport mediated by a prokaryotic homologue of ClC Cl- channels. Nature 427, 803-807 (2004). Using electrophysiological and biochemical functional assays on the same preparation of prokaryotic ClC proteins (ClC-ec1) that had been used for X-ray crystallography, this study came to the shocking conclusion that ClC-ec1 is a Cl/H exchange pump, rather than the Cl ion channel initially assumed.
    • Accardi, A. & Miller, C. Secondary active transport mediated by a prokaryotic homologue of ClC Cl- channels. Nature 427, 803-807 (2004). Using electrophysiological and biochemical functional assays on the same preparation of prokaryotic ClC proteins (ClC-ec1) that had been used for X-ray crystallography, this study came to the shocking conclusion that ClC-ec1 is a Cl/H exchange pump, rather than the Cl ion channel initially assumed.
  • 22
    • 0020440405 scopus 로고
    • Open-state substructure of single chloride channels from Torpedo electroplax
    • Miller, C. Open-state substructure of single chloride channels from Torpedo electroplax. Philos. Trans. R. Soc. Lond. B Biol. Sci. 299, 401-411 (1982).
    • (1982) Philos. Trans. R. Soc. Lond. B Biol. Sci , vol.299 , pp. 401-411
    • Miller, C.1
  • 23
    • 0029661878 scopus 로고    scopus 로고
    • Homodimeric architecture of a CIC-type chloride ion channel
    • Middleton, R. E., Pheasant, D. J. & Miller, C. Homodimeric architecture of a CIC-type chloride ion channel. Nature 383, 337-340 (1996).
    • (1996) Nature , vol.383 , pp. 337-340
    • Middleton, R.E.1    Pheasant, D.J.2    Miller, C.3
  • 24
    • 0029743660 scopus 로고    scopus 로고
    • Two physcially distinct pores in the demeric CIC-0 chloride channel
    • Ludewig, U., Pusch, M. & Jentsch, T. J. Two physcially distinct pores in the demeric CIC-0 chloride channel. Nature 383, 340-343 (1996).
    • (1996) Nature , vol.383 , pp. 340-343
    • Ludewig, U.1    Pusch, M.2    Jentsch, T.J.3
  • 25
    • 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
  • 26
    • 15544362767 scopus 로고    scopus 로고
    • Physiological functions of CLC Cl- channels gleaned from human genetic disease and mouse models
    • Jentsch, T. J., Poët, M., Fuhrmann, J. C. & Zdebik, A. A. Physiological functions of CLC Cl- channels gleaned from human genetic disease and mouse models. Annu. Rev. Physiol. 67, 779-807 (2005).
    • (2005) Annu. Rev. Physiol , vol.67 , pp. 779-807
    • Jentsch, T.J.1    Poët, M.2    Fuhrmann, J.C.3    Zdebik, A.A.4
  • 27
    • 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
  • 28
    • 0034940574 scopus 로고    scopus 로고
    • Different fast-gate regulation by external Cl- and H+ of the muscle-type ClC chloride channels
    • Chen, M. F. & Chen, T. Y. Different fast-gate regulation by external Cl- and H+ of the muscle-type ClC chloride channels. J. Gen. Physiol. 118, 23-32 (2001).
    • (2001) J. Gen. Physiol , vol.118 , pp. 23-32
    • Chen, M.F.1    Chen, T.Y.2
  • 29
    • 0345146920 scopus 로고    scopus 로고
    • Conservation of chloride channel structure revealed by an inhibitor binding site in ClC-1
    • Estévez, R., Schroeder, B. C., Accardi, A., Jentsch, T. J. &Pusch, M. Conservation of chloride channel structure revealed by an inhibitor binding site in ClC-1. Neuron 38, 47-59 (2003).
    • (2003) Neuron , vol.38 , pp. 47-59
    • Estévez, R.1    Schroeder, B.C.2    Accardi, A.3    Jentsch, T.J.4    Pusch, M.5
  • 30
    • 22244489419 scopus 로고    scopus 로고
    • Cysteine accessibility in ClC-0 supports conservation of the ClC intracellular vestibule
    • Engh, A. M. & Maduke, M. Cysteine accessibility in ClC-0 supports conservation of the ClC intracellular vestibule. J. Gen. Physiol. 125, 601-617 (2005).
    • (2005) J. Gen. Physiol , vol.125 , pp. 601-617
    • Engh, A.M.1    Maduke, M.2
  • 31
    • 34548852606 scopus 로고    scopus 로고
    • ClC chloride channels and transporters: A biophysical and physiological perspective
    • Zifarelli, G. & Pusch, M. ClC chloride channels and transporters: a biophysical and physiological perspective. Rev. Physiol. Biochem. Pharmacol. 158, 23-76 (2007).
    • (2007) Rev. Physiol. Biochem. Pharmacol , vol.158 , pp. 23-76
    • Zifarelli, G.1    Pusch, M.2
  • 32
    • 33645296826 scopus 로고    scopus 로고
    • ClC chloride channels viewed through a transporter lens
    • Miller, C. ClC chloride channels viewed through a transporter lens. Nature 440, 484-489 (2006).
    • (2006) Nature , vol.440 , pp. 484-489
    • Miller, C.1
  • 33
    • 49649112453 scopus 로고    scopus 로고
    • Ion permeation through a Cl--selective channel designed from a ClC Cl-/H+ exchanger
    • Jayaram, H., Accardi, A., Wu, F., Williams, C. &Miller, C. Ion permeation through a Cl--selective channel designed from a ClC Cl-/H+ exchanger. Proc. Natl Acad. Sci. USA 105, 11194-11199 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 11194-11199
    • Jayaram, H.1    Accardi, A.2    Wu, F.3    Williams, C.4    Miller, C.5
  • 34
    • 33947720910 scopus 로고    scopus 로고
    • Uncoupling and turnover in a Cl-/H+ exchange transporter
    • Walden, M. et al. Uncoupling and turnover in a Cl-/H+ exchange transporter. J. Gen. Physiol. 129, 317-329 (2007).
    • (2007) J. Gen. Physiol , vol.129 , pp. 317-329
    • Walden, M.1
  • 35
    • 0032921415 scopus 로고    scopus 로고
    • The muscle chloride channel ClC-1 has a double-barreled appearance that is differentially affected in dominant and recessive myotonia
    • Saviane, C., Conti, F. & Pusch, M. The muscle chloride channel ClC-1 has a double-barreled appearance that is differentially affected in dominant and recessive myotonia. J. Gen. Physiol. 113, 457-468 (1999).
    • (1999) J. Gen. Physiol , vol.113 , pp. 457-468
    • Saviane, C.1    Conti, F.2    Pusch, M.3
  • 36
    • 49449090405 scopus 로고    scopus 로고
    • The ClC-0 chloride channel is a 'broken' Cl -/H+ antiporter
    • Using single-channel recordings to show that the gating pattern of ClC-0 channels depends on transmembrane movement of protons, this study firmly established the evolutionary link between ClC pumps and ClC channels and suggested that the channels evolved from a dysfunctional pump
    • Lísal, J. & Maduke, M. The ClC-0 chloride channel is a 'broken' Cl -/H+ antiporter. Nature Struct. Mol. Biol. 15, 805-810 (2008). Using single-channel recordings to show that the gating pattern of ClC-0 channels depends on transmembrane movement of protons, this study firmly established the evolutionary link between ClC pumps and ClC channels and suggested that the channels evolved from a dysfunctional pump.
    • (2008) Nature Struct. Mol. Biol , vol.15 , pp. 805-810
    • Lísal, J.1    Maduke, M.2
  • 37
    • 33645307384 scopus 로고    scopus 로고
    • The ABC protein turned chloride channel whose failure causes cystic fibrosis
    • Gadsby, D. C., Vergani, P. & Csanády, L. The ABC protein turned chloride channel whose failure causes cystic fibrosis. Nature 440, 477-483 (2006).
    • (2006) Nature , vol.440 , pp. 477-483
    • Gadsby, D.C.1    Vergani, P.2    Csanády, L.3
  • 38
    • 61449361477 scopus 로고    scopus 로고
    • ATP hydrolysis-driven gating in cystic fibrosis transmembrane conductance regulator
    • Muallem, D. & Vergani, P. ATP hydrolysis-driven gating in cystic fibrosis transmembrane conductance regulator. Philos. Trans. R. Soc. Lond. B Biol. Sci. 364, 247-255 (2009).
    • (2009) Philos. Trans. R. Soc. Lond. B Biol. Sci , vol.364 , pp. 247-255
    • Muallem, D.1    Vergani, P.2
  • 39
    • 57749106719 scopus 로고    scopus 로고
    • Evolutionary and functional divergence between the cystic fibrosis transmembrane conductance regulator and related ATP-binding cassette transporter
    • Jordan, K., Kota, K. C., Cui, G., Thompson, C. H. &McCarty, N. A. Evolutionary and functional divergence between the cystic fibrosis transmembrane conductance regulator and related ATP-binding cassette transporter. Proc. Natl Acad. Sci. USA. 105, 18865-18870 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 18865-18870
    • Jordan, K.1    Kota, K.C.2    Cui, G.3    Thompson, C.H.4    McCarty, N.A.5
  • 40
    • 14544300522 scopus 로고    scopus 로고
    • Vergani, P., Lockless, S. W., Nairn, A. C. & Gadsby, D. C. CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains. Nature 24, 876-880 (2005). This study used CFTR-channel gating kinetics to demonstrate ATP-dependent energetic interaction between residues at positions shown to structurally interact across the interface of prokaryotic nucleotide-binding domain dimers. Evolutionary conservation at these interacting positions in most ABC proteins suggests that nearly all undergo the same ATP-driven cycle of conformational changes established for CFTR.
    • Vergani, P., Lockless, S. W., Nairn, A. C. & Gadsby, D. C. CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains. Nature 24, 876-880 (2005). This study used CFTR-channel gating kinetics to demonstrate ATP-dependent energetic interaction between residues at positions shown to structurally interact across the interface of prokaryotic nucleotide-binding domain dimers. Evolutionary conservation at these interacting positions in most ABC proteins suggests that nearly all undergo the same ATP-driven cycle of conformational changes established for CFTR.
  • 41
    • 0345133280 scopus 로고    scopus 로고
    • Channelrhodopsin-2, a directly lightgated cation-selective membrane channel
    • Nagel, G. et al. Channelrhodopsin-2, a directly lightgated cation-selective membrane channel. Proc. Natl Acad. Sci. USA 100, 13940-13945 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 13940-13945
    • Nagel, G.1
  • 42
    • 0025270712 scopus 로고
    • Steady-state coupling of ion-channel conformations to a transmembrane ion gradient
    • Richard, E. A. & Miller, C. Steady-state coupling of ion-channel conformations to a transmembrane ion gradient. Science 247, 1208-1210 (1990).
    • (1990) Science , vol.247 , pp. 1208-1210
    • Richard, E.A.1    Miller, C.2
  • 43
    • 22944475536 scopus 로고    scopus 로고
    • Chloride/proton antiporter activity of mammalian ClC proteins ClC-4 and ClC-5
    • Picollo, A. & Pusch, M. Chloride/proton antiporter activity of mammalian ClC proteins ClC-4 and ClC-5. Nature 436, 420-423 (2005).
    • (2005) Nature , vol.436 , pp. 420-423
    • Picollo, A.1    Pusch, M.2
  • 44
    • 0024424270 scopus 로고
    • Identification of the cystic fibrosis gene: Cloning and characterization of complementary DNA
    • Riordan, J. R. et al. Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA. Science 245, 1066-1073 (1989).
    • (1989) Science , vol.245 , pp. 1066-1073
    • Riordan, J.R.1
  • 45
    • 0028972501 scopus 로고
    • Reconstitution of IKATP: An inward rectifier subunit plus the sulfonylurea receptor
    • Inagaki, N. et al. Reconstitution of IKATP: an inward rectifier subunit plus the sulfonylurea receptor. Science 270, 1166-1170 (1995).
    • (1995) Science , vol.270 , pp. 1166-1170
    • Inagaki, N.1
  • 46
    • 0034705293 scopus 로고    scopus 로고
    • Hopfner, K. P. et al. Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily. Cell 101, 789-800 (2000). This was the first demonstration that the nucleotide-binding domains of ABC proteins form head-to-tail dimers in the presence of ATP, with one ATP molecule enclosed in each of the two composite catalytic sites formed in the dimer interface. As ADP did not support dimerization, it was proposed that cycles of ATP-induced dimerization and hydrolysistriggered dissociation provide the basis for function of all ABC proteins.
    • Hopfner, K. P. et al. Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily. Cell 101, 789-800 (2000). This was the first demonstration that the nucleotide-binding domains of ABC proteins form head-to-tail dimers in the presence of ATP, with one ATP molecule enclosed in each of the two composite catalytic sites formed in the dimer interface. As ADP did not support dimerization, it was proposed that cycles of ATP-induced dimerization and hydrolysistriggered dissociation provide the basis for function of all ABC proteins.
  • 47
    • 0035252682 scopus 로고    scopus 로고
    • DNA mismatch repair: MutS structures bound to mismatches
    • Sixma, T. K. DNA mismatch repair: MutS structures bound to mismatches. Curr. Opin. Struct. Biol. 11, 47-52 (2001).
    • (2001) Curr. Opin. Struct. Biol , vol.11 , pp. 47-52
    • Sixma, T.K.1
  • 48
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • Smith, P. C. et al. ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol. Cell 10, 139-149 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 139-149
    • Smith, P.C.1
  • 49
    • 29144502288 scopus 로고    scopus 로고
    • ATP hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation
    • Lu, G., Westbrooks, J. M., Davidson, A. L. & Chen, J. ATP hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation. Proc. Natl Acad. Sci. USA 102, 17969-17974 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 17969-17974
    • Lu, G.1    Westbrooks, J.M.2    Davidson, A.L.3    Chen, J.4
  • 50
    • 33748644877 scopus 로고    scopus 로고
    • Dawson, R. J. & Locher, K. P. Structure of a bacterial multidrug ABC transporter. Nature 443, 180-185 (2006). This paper reported the first high-resolution structure of an entire ABC transporter that is homologous to clinically relevant human ABC proteins. The structure revealed that the transmembrane helices extend long linker helices into the cytoplasm where they connect to the nucleotide-binding domains via short conserved coupling helices. It also revealed a domain-swapped architecture in which each nucleotide-binding domain receives connections from both N- and C-terminal transmembrane domains.
    • Dawson, R. J. & Locher, K. P. Structure of a bacterial multidrug ABC transporter. Nature 443, 180-185 (2006). This paper reported the first high-resolution structure of an entire ABC transporter that is homologous to clinically relevant human ABC proteins. The structure revealed that the transmembrane helices extend long linker helices into the cytoplasm where they connect to the nucleotide-binding domains via short conserved coupling helices. It also revealed a domain-swapped architecture in which each nucleotide-binding domain receives connections from both N- and C-terminal transmembrane domains.
  • 51
    • 33847134349 scopus 로고    scopus 로고
    • Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP
    • Dawson, R. J. & Locher, K. P. Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP. FEBS Lett. 581, 935-938 (2007).
    • (2007) FEBS Lett , vol.581 , pp. 935-938
    • Dawson, R.J.1    Locher, K.P.2
  • 52
    • 36549018568 scopus 로고    scopus 로고
    • Crystal structure of a catalytic intermediate of the maltose transporter
    • Oldham, M. L., Khare, D., Quiocho, F. A., Davidson, A. L. & Chen, J. Crystal structure of a catalytic intermediate of the maltose transporter. Nature 450, 515-521 (2007).
    • (2007) Nature , vol.450 , pp. 515-521
    • Oldham, M.L.1    Khare, D.2    Quiocho, F.A.3    Davidson, A.L.4    Chen, J.5
  • 53
    • 37649004412 scopus 로고    scopus 로고
    • Flexibility in the ABC transporter MsbA: Alternating access with a twist
    • Ward, A., Reyes, C. L., Yu, J., Roth, C. B. & Chang, G. Flexibility in the ABC transporter MsbA: alternating access with a twist. Proc. Natl Acad. Sci. USA 104, 19005-19010 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 19005-19010
    • Ward, A.1    Reyes, C.L.2    Yu, J.3    Roth, C.B.4    Chang, G.5
  • 54
    • 0031954021 scopus 로고    scopus 로고
    • Adenosine triphosphatedependent asymmetry of anion permeation in the cystic fibrosis transmembrane conductance regulator chloride channel
    • Linsdell, P. & Hanrahan, J. W. Adenosine triphosphatedependent asymmetry of anion permeation in the cystic fibrosis transmembrane conductance regulator chloride channel. J. Gen. Physiol. 111, 601-614 (1998).
    • (1998) J. Gen. Physiol , vol.111 , pp. 601-614
    • Linsdell, P.1    Hanrahan, J.W.2
  • 55
    • 0038369932 scopus 로고    scopus 로고
    • CFTR directly mediates nucleotideregulated glutathione flux
    • Kogan, I. et al. CFTR directly mediates nucleotideregulated glutathione flux. EMBO J. 22, 1981-1989 (2003).
    • (2003) EMBO J , vol.22 , pp. 1981-1989
    • Kogan, I.1
  • 56
    • 0024470756 scopus 로고
    • Palytoxin acts through Na+ K+ ATPase
    • Habermann, E. Palytoxin acts through Na+ K+ ATPase. Toxicon 27, 1171-1187 (1989).
    • (1989) Toxicon , vol.27 , pp. 1171-1187
    • Habermann, E.1
  • 58
    • 0028339693 scopus 로고
    • Palytoxin induces K+ efflux from yeast cells expressing the mammalian sodium pump
    • Scheiner-Bobis, G., Meyer zu Heringdorf, D., Christ, M. &Habermann, E. Palytoxin induces K+ efflux from yeast cells expressing the mammalian sodium pump. Mol. Pharmacol. 45, 1132-1136 (1994).
    • (1994) Mol. Pharmacol , vol.45 , pp. 1132-1136
    • Scheiner-Bobis, G.1    Meyer zu Heringdorf, D.2    Christ, M.3    Habermann, E.4
  • 59
    • 0031081706 scopus 로고    scopus 로고
    • Palytoxin-induced singlechannel currents from the sodium pump synthesized by in vitro expression
    • Hirsh, J. K. & Wu, C. H. Palytoxin-induced singlechannel currents from the sodium pump synthesized by in vitro expression. Toxicon 35, 169-176 (1997).
    • (1997) Toxicon , vol.35 , pp. 169-176
    • Hirsh, J.K.1    Wu, C.H.2
  • 60
    • 1842736450 scopus 로고    scopus 로고
    • Large diameter of palytoxininduced Na/K pump channels and modulation of palytoxin interaction by Na/K pump ligands
    • Artigas, P. & Gadsby, D. C. Large diameter of palytoxininduced Na/K pump channels and modulation of palytoxin interaction by Na/K pump ligands. J. Gen. Physiol. 123, 357-376 (2004).
    • (2004) J. Gen. Physiol , vol.123 , pp. 357-376
    • Artigas, P.1    Gadsby, D.C.2
  • 61
    • 0037458010 scopus 로고    scopus 로고
    • Artigas, P. & Gadsby, D. C. Na+/K+-pump ligands modulate gating of palytoxin-induced ion channels. Proc. Natl Acad. Sci. USA 100, 501-505 (2003). This study provided support for the view of the Na, K pump as a channel controlled by two gates that open strictly alternately. Current recordings showed that palytoxin interferes with this strict coupling, allowing the two gates to sometimes both be open, but that each gate in a palytoxin-bound pump-channel still responds to its physiological ligand, external K ions or cytoplasmic ATP.
    • Artigas, P. & Gadsby, D. C. Na+/K+-pump ligands modulate gating of palytoxin-induced ion channels. Proc. Natl Acad. Sci. USA 100, 501-505 (2003). This study provided support for the view of the Na, K pump as a channel controlled by two gates that open strictly alternately. Current recordings showed that palytoxin interferes with this strict coupling, allowing the two gates to sometimes both be open, but that each gate in a palytoxin-bound pump-channel still responds to its physiological ligand, external K ions or cytoplasmic ATP.
  • 62
    • 38349138943 scopus 로고    scopus 로고
    • The K+-translocating KdpFABC complex from Escherichia coli: A P-type ATPase with unique features
    • Greie, J. C. & Altendorf, K. The K+-translocating KdpFABC complex from Escherichia coli: a P-type ATPase with unique features. J. Bioenerg. Biomembr. 39, 397-402 (2007).
    • (2007) J. Bioenerg. Biomembr , vol.39 , pp. 397-402
    • Greie, J.C.1    Altendorf, K.2
  • 63
    • 33749169688 scopus 로고    scopus 로고
    • Ion permeation through the Na+, K+-ATPase
    • Reyes, N. & Gadsby, D. C. Ion permeation through the Na+, K+-ATPase. Nature 443, 470-474 (2006).
    • (2006) Nature , vol.443 , pp. 470-474
    • Reyes, N.1    Gadsby, D.C.2
  • 64
    • 56749163392 scopus 로고    scopus 로고
    • The ion pathway through the opened Na+, K+-ATPase pump
    • Takeuchi, A., Reyes, N., Artigas, P., Gadsby, D. C. The ion pathway through the opened Na+, K+-ATPase pump. Nature 456, 413-416 (2008).
    • (2008) Nature , vol.456 , pp. 413-416
    • Takeuchi, A.1    Reyes, N.2    Artigas, P.3    Gadsby, D.C.4
  • 66
    • 28244457359 scopus 로고    scopus 로고
    • Separate ion pathways in a Cl-/H+ exchanger
    • Accardi, A. et al. Separate ion pathways in a Cl-/H+ exchanger. J. Gen. Physiol. 126, 563-570 (2005).
    • (2005) J. Gen. Physiol , vol.126 , pp. 563-570
    • Accardi, A.1
  • 67
    • 36348975209 scopus 로고    scopus 로고
    • Glutamate transporters: Confining runaway excitation by shaping synaptic transmission
    • Tzingounis, A. V. & Wadiche, J. I. Glutamate transporters: confining runaway excitation by shaping synaptic transmission. Nature Rev. Neurosci. 8, 935-947 (2007).
    • (2007) Nature Rev. Neurosci , vol.8 , pp. 935-947
    • Tzingounis, A.V.1    Wadiche, J.I.2
  • 68
    • 34249935610 scopus 로고    scopus 로고
    • Glutamate and monoamine transporters: New visions of form and function
    • Torres, G. E. & Amara, S. G. Glutamate and monoamine transporters: new visions of form and function. Curr. Opin. Neurobiol. 17, 304-312 (2007).
    • (2007) Curr. Opin. Neurobiol , vol.17 , pp. 304-312
    • Torres, G.E.1    Amara, S.G.2
  • 69
    • 61449361479 scopus 로고    scopus 로고
    • The molecular logic of sodium-coupled neurotransmitter transporters
    • Gouaux, E. The molecular logic of sodium-coupled neurotransmitter transporters. Philos. Trans. R. Soc. Lond. B Biol. Sci. 364, 149-154 (2009).
    • (2009) Philos. Trans. R. Soc. Lond. B Biol. Sci , vol.364 , pp. 149-154
    • Gouaux, E.1
  • 70
    • 0029076899 scopus 로고
    • An excitatory aminoacid transporter with properties of a ligand-gated chloride channel
    • Fairman, W. A., Vandenberg, R. J., Arriza, J. L., Kavanaugh, M. P. & Amara, S. G. An excitatory aminoacid transporter with properties of a ligand-gated chloride channel. Nature 375, 599-603 (1995).
    • (1995) Nature , vol.375 , pp. 599-603
    • Fairman, W.A.1    Vandenberg, R.J.2    Arriza, J.L.3    Kavanaugh, M.P.4    Amara, S.G.5
  • 71
    • 0030030516 scopus 로고    scopus 로고
    • Noise analysis of the glutamate-activated current in photoreceptors
    • Larsson, H. P., Picaud, S. A., Werblin, F. S. & Lecar, H. Noise analysis of the glutamate-activated current in photoreceptors. Biophys. J. 70, 733-742 (1996).
    • (1996) Biophys. J , vol.70 , pp. 733-742
    • Larsson, H.P.1    Picaud, S.A.2    Werblin, F.S.3    Lecar, H.4
  • 72
    • 0032189020 scopus 로고    scopus 로고
    • Macroscopic and microscopic properties of a cloned glutamate transporter/chloride channel
    • Wadiche, J. I. & Kavanaugh, M. P. Macroscopic and microscopic properties of a cloned glutamate transporter/chloride channel. J. Neurosci. 18, 7650-7661 (1998).
    • (1998) J. Neurosci , vol.18 , pp. 7650-7661
    • Wadiche, J.I.1    Kavanaugh, M.P.2
  • 73
    • 34247648737 scopus 로고    scopus 로고
    • The uncoupled chloride conductance of a bacterial glutamate transporter homolog
    • This study used reconstituted purified glutamate transporter protein to establish that the uncoupled channel-like Cl current flows through the same protein that carries out stoichiometric Na-dependent transport of glutamate
    • Ryan, R. M. & Mindell, J. A. The uncoupled chloride conductance of a bacterial glutamate transporter homolog. Nature Struct. Mol. Biol. 14, 365-371 (2007). This study used reconstituted purified glutamate transporter protein to establish that the uncoupled channel-like Cl current flows through the same protein that carries out stoichiometric Na-dependent transport of glutamate.
    • (2007) Nature Struct. Mol. Biol , vol.14 , pp. 365-371
    • Ryan, R.M.1    Mindell, J.A.2
  • 74
    • 55749090236 scopus 로고    scopus 로고
    • Slips, leaks and channels in glutamate transporters
    • Vandenberg, R. J., Huang, S. & Ryan, R. M. Slips, leaks and channels in glutamate transporters. Channels 2, 51-58 (2008).
    • (2008) Channels , vol.2 , pp. 51-58
    • Vandenberg, R.J.1    Huang, S.2    Ryan, R.M.3
  • 75
    • 2442693929 scopus 로고    scopus 로고
    • The chloride permeation pathway of a glutamate transporter and its proximity to the glutamate translocation pathway
    • Ryan, R. M., Mitrovic, A. D. & Vandenberg, R. J. The chloride permeation pathway of a glutamate transporter and its proximity to the glutamate translocation pathway. J. Biol. Chem. 279, 20742-20751 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 20742-20751
    • Ryan, R.M.1    Mitrovic, A.D.2    Vandenberg, R.J.3
  • 76
    • 0034655871 scopus 로고    scopus 로고
    • Isolation of current components and partial reaction cycles in the glial glutamate transporter EAAT2
    • Otis, T. S. & Kavanaugh, M. P. Isolation of current components and partial reaction cycles in the glial glutamate transporter EAAT2. J. Neurosci. 20, 2749-2757 (2000).
    • (2000) J. Neurosci , vol.20 , pp. 2749-2757
    • Otis, T.S.1    Kavanaugh, M.P.2
  • 77
    • 0000760057 scopus 로고
    • The linkage of sodium, potassium, and ammonium active transport across the human erythrocyte membrane
    • Post, R. L. & Jolly, P. C. The linkage of sodium, potassium, and ammonium active transport across the human erythrocyte membrane. Biochim. Biophys. Acta 25, 118-128 (1957).
    • (1957) Biochim. Biophys. Acta , vol.25 , pp. 118-128
    • Post, R.L.1    Jolly, P.C.2
  • 78
    • 0016367998 scopus 로고
    • Isolation of (Na+ plus K+)-ATPase
    • Jørgensen P. L. Isolation of (Na+ plus K+)-ATPase. Methods Enzymol. 32, 277-290 (1974).
    • (1974) Methods Enzymol , vol.32 , pp. 277-290
    • Jørgensen, P.L.1
  • 79
    • 0021867974 scopus 로고
    • Voltage dependence of Na/K pump current in isolated heart cells
    • Gadsby, D. C., Kimura, J. & Noma, A. Voltage dependence of Na/K pump current in isolated heart cells. Nature 315, 63-65 (1985).
    • (1985) Nature , vol.315 , pp. 63-65
    • Gadsby, D.C.1    Kimura, J.2    Noma, A.3
  • 80
    • 0022471974 scopus 로고
    • Voltage dependence of Na translocation by the Na/K pump
    • Nakao, M. & Gadsby, D. C. Voltage dependence of Na translocation by the Na/K pump. Nature 323, 628-630 (1986).
    • (1986) Nature , vol.323 , pp. 628-630
    • Nakao, M.1    Gadsby, D.C.2
  • 81
    • 0036969001 scopus 로고    scopus 로고
    • Ion channel-like properties of the Na+/K+ pump
    • Artigas, P. & Gadsby, D. C. Ion channel-like properties of the Na+/K+ pump. Ann. NY Acad. Sci. 976, 31-40 (2002).
    • (2002) Ann. NY Acad. Sci , vol.976 , pp. 31-40
    • Artigas, P.1    Gadsby, D.C.2
  • 82
    • 0016424181 scopus 로고
    • The interaction of ATP-analogues possessing a blocked γ-phosphate group with the sodium pump in human red cells
    • Simons, T. J. B. The interaction of ATP-analogues possessing a blocked γ-phosphate group with the sodium pump in human red cells. J. Physiol. 244, 731-739 (1975).
    • (1975) J. Physiol , vol.244 , pp. 731-739
    • Simons, T.J.B.1
  • 83
    • 67349271378 scopus 로고    scopus 로고
    • Forbush, B. 3rd. Rapid release of 42K and 86Rb from an occluded state of the Na, K-pump in the presence of ATP or ADP. J. Biol. Chem. 244, 731-739 (1987).
    • Forbush, B. 3rd. Rapid release of 42K and 86Rb from an occluded state of the Na, K-pump in the presence of ATP or ADP. J. Biol. Chem. 244, 731-739 (1987).
  • 84
    • 1542349179 scopus 로고    scopus 로고
    • Ion transport: Spot the difference
    • Gadsby D. C. Ion transport: spot the difference. Nature 427, 795-797 (2004).
    • (2004) Nature , vol.427 , pp. 795-797
    • Gadsby, D.C.1
  • 85
    • 30444442312 scopus 로고    scopus 로고
    • Ion-binding properties of the CIC chloride selectivity filter
    • Lobet, S. & Dutzler, R. Ion-binding properties of the CIC chloride selectivity filter. EMBO J. 25, 24-33 (2006).
    • (2006) EMBO J , vol.25 , pp. 24-33
    • Lobet, S.1    Dutzler, R.2
  • 86
    • 34249881600 scopus 로고    scopus 로고
    • A structural perspective on CIC channel and transporter function
    • Dutzler, R. A structural perspective on CIC channel and transporter function. FEBS Letters 581, 2839-2844 (2007).
    • (2007) FEBS Letters , vol.581 , pp. 2839-2844
    • Dutzler, R.1
  • 87
    • 50249090046 scopus 로고    scopus 로고
    • Atomic model of human cystic fibrosis transmembrane conductance regulator: Membrane-spanning domains and coupling interfaces
    • Mornon, J. P., Lehn, P. & Callebaut, I. Atomic model of human cystic fibrosis transmembrane conductance regulator: membrane-spanning domains and coupling interfaces. Cell. Mol. Life Sci. 65, 2594-2612 (2008).
    • (2008) Cell. Mol. Life Sci , vol.65 , pp. 2594-2612
    • Mornon, J.P.1    Lehn, P.2    Callebaut, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.