메뉴 건너뛰기




Volumn 499, Issue 7456, 2013, Pages 107-110

Structural basis for alternating access of a eukaryotic calcium/proton exchanger

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM PROTON EXCHANGER PROTEIN; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 84879882908     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature12233     Document Type: Article
Times cited : (84)

References (53)
  • 1
    • 0025353579 scopus 로고
    • Kinetics, stoichiometryand role of the Na-Ca exchange mechanism in isolated cardiac myocytes
    • Crespo, L. M. , Grantham,C. J. &Cannell, M. B. Kinetics, stoichiometryand role of the Na-Ca exchange mechanism in isolated cardiac myocytes. Nature 345, 618-621 (1990).
    • (1990) Nature , vol.345 , pp. 618-621
    • Crespo, L.M.1    Grantham, C.J.2    Cannell, M.B.3
  • 2
    • 58549116085 scopus 로고    scopus 로고
    • Simulating calciuminflux and free calciumconcentrations in yeast
    • Cui, J. et al. Simulating calciuminflux and free calciumconcentrations in yeast. Cell Calcium 45, 123-132 (2009).
    • (2009) Cell Calcium , vol.45 , pp. 123-132
    • Cui, J.1
  • 3
    • 0032588195 scopus 로고    scopus 로고
    • The vacuolarCa21/H1 exchanger Vcx1p/Hum1p tightly controls cytosolic Ca21 levels in S. cerevisiae
    • Miseta, A. , Kellermayer, R. , Aiello, D. P. , Fu, L. &Bedwell, D. M. The vacuolarCa21/H1 exchanger Vcx1p/Hum1p tightly controls cytosolic Ca21 levels in S. cerevisiae. FEBS Lett. 451, 132-136 (1999).
    • (1999) FEBS Lett , vol.451 , pp. 132-136
    • Miseta, A.1    Kellermayer, R.2    Aiello, D.P.3    Fu, L.4    Bedwell, D.M.5
  • 4
    • 0033852625 scopus 로고    scopus 로고
    • Sodium-calciumexchange: Amolecular perspective
    • Philipson, K. D. & Nicoll, D. A. Sodium-calciumexchange: amolecular perspective. Annu. Rev. Physiol. 62, 111-133 (2000).
    • (2000) Annu. Rev. Physiol , vol.62 , pp. 111-133
    • Philipson, K.D.1    Nicoll, D.A.2
  • 5
    • 0025243512 scopus 로고
    • Molecular cloning and functional expression of the cardiac sarcolemmal Na1-Ca21 exchanger
    • Nicoll, D. A. , Longoni, S. & Philipson, K. D. Molecular cloning and functional expression of the cardiac sarcolemmal Na1-Ca21 exchanger. Science 250, 562-565 (1990).
    • (1990) Science , vol.250 , pp. 562-565
    • Nicoll, D.A.1    Longoni, S.2    Philipson, K.D.3
  • 6
    • 34548714102 scopus 로고    scopus 로고
    • Na1/Ca21 exchangers: Three mammalian gene families control Ca21 transport
    • Lytton, J. Na1/Ca21 exchangers: three mammalian gene families control Ca21 transport. Biochem. J. 406, 365-382 (2007).
    • (2007) Biochem. J , vol.406 , pp. 365-382
    • Lytton, J.1
  • 8
    • 0030006878 scopus 로고    scopus 로고
    • The product of HUM1, a novel yeast gene, is required for vacuolar Ca21/H1 exchange and is related tomammalian Na1/Ca21 exchangers
    • Pozos, T. C. , Sekler, I. & Cyert, M. S. The product of HUM1, a novel yeast gene, is required for vacuolar Ca21/H1 exchange and is related tomammalian Na1/Ca21 exchangers. Mol. Cell. Biol. 16, 3730-3741 (1996).
    • (1996) Mol. Cell. Biol , vol.16 , pp. 3730-3741
    • Pozos, T.C.1    Sekler, I.2    Cyert, M.S.3
  • 9
    • 0037329942 scopus 로고    scopus 로고
    • The Arabidopsis cax1 mutant exhibits impaired ion homeostasis, development, and hormonal responses and reveals interplay among vacuolar transporters
    • Cheng, N.-H. , Pittman, J. K. , Barkla, B. J. , Shigaki, T. & Hirschi, K. D. The Arabidopsis cax1 mutant exhibits impaired ion homeostasis, development, and hormonal responses and reveals interplay among vacuolar transporters. Plant Cell 15, 347-364 (2003).
    • (2003) Plant Cell , vol.15 , pp. 347-364
    • Cheng, N.-H.1    Pittman, J.K.2    Barkla, B.J.3    Shigaki, T.4    Hirschi, K.D.5
  • 10
    • 84868315303 scopus 로고    scopus 로고
    • Vacuolar CAX1 and CAX3 influence auxin transport in guard cells via regulation of apoplastic pH
    • Cho, D. et al. Vacuolar CAX1 and CAX3 influence auxin transport in guard cells via regulation of apoplastic pH. Plant Physiol. 160, 1293-1302 (2012).
    • (2012) Plant Physiol , vol.160 , pp. 1293-1302
    • Cho, D.1
  • 11
    • 79958858127 scopus 로고    scopus 로고
    • Acidic calciumstores of Saccharomyces cerevisiae
    • Cunningham, K. W. Acidic calciumstores of Saccharomyces cerevisiae. Cell Calcium 50, 129-138 (2011).
    • (2011) Cell Calcium , vol.50 , pp. 129-138
    • Cunningham, K.W.1
  • 12
    • 33845363673 scopus 로고    scopus 로고
    • Identification of three distinct phylogenetic groups of CAX cation/proton antiporters
    • Shigaki, T. , Rees, I. , Nakhleh, L. & Hirschi, K. D. Identification of three distinct phylogenetic groups of CAX cation/proton antiporters. J. Mol. Evol. 63, 815-825 (2006).
    • (2006) J. Mol. Evol , vol.63 , pp. 815-825
    • Shigaki, T.1    Rees, I.2    Nakhleh, L.3    Hirschi, K.D.4
  • 13
    • 0037033784 scopus 로고    scopus 로고
    • Internal Ca21 release in yeast is triggered by hypertonic shock andmediated by a TRP channel homologue
    • Denis, V. & Cyert, M. S. Internal Ca21 release in yeast is triggered by hypertonic shock andmediated by a TRP channel homologue. J. Cell Biol. 156, 29-34 (2002).
    • (2002) J. Cell Biol , vol.156 , pp. 29-34
    • Denis, V.1    Cyert, M.S.2
  • 14
    • 0030955318 scopus 로고    scopus 로고
    • Calx a Na-Ca exchanger gene of Drosophila melanogaster
    • Schwarz, E. M. & Benzer, S. Calx, a Na-Ca exchanger gene of Drosophila melanogaster. Proc. Natl Acad. Sci. USA 94, 10249-10254 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10249-10254
    • Schwarz, E.M.1    Benzer, S.2
  • 15
    • 4143050097 scopus 로고    scopus 로고
    • The cation/Ca21 exchanger superfamily: Phylogenetic analysis and structural implications
    • Cai, X. & Lytton, J. The cation/Ca21 exchanger superfamily: phylogenetic analysis and structural implications. Mol. Biol. Evol. 21, 1692-1703 (2004).
    • (2004) Mol. Biol. Evol , vol.21 , pp. 1692-1703
    • Cai, X.1    Lytton, J.2
  • 16
    • 0033028949 scopus 로고    scopus 로고
    • Unique topology of the internal repeats in the cardiac Na1/Ca21 exchanger
    • Iwamoto, T. et al. Unique topology of the internal repeats in the cardiac Na1/Ca21 exchanger. FEBS Lett. 446, 264-268 (1999).
    • (1999) FEBS Lett , vol.446 , pp. 264-268
    • Iwamoto, T.1
  • 17
    • 84863012221 scopus 로고    scopus 로고
    • Structural insight into the ion-exchange mechanism of the sodium/calcium exchanger
    • Liao, J. et al. Structural insight into the ion-exchange mechanism of the sodium/calcium exchanger. Science 335, 686-690 (2012).
    • (2012) Science , vol.335 , pp. 686-690
    • Liao, J.1
  • 18
    • 0029929230 scopus 로고    scopus 로고
    • Mutation of amino acid residues in the putative transmembrane segments of the cardiac sarcolemmal Na1-Ca21 exchanger
    • Nicoll, D. A. , Hryshko, L. V. , Matsuoka, S. , Frank, J. S. & Philipson, K. D. Mutation of amino acid residues in the putative transmembrane segments of the cardiac sarcolemmal Na1-Ca21 exchanger. J. Biol. Chem. 271, 13385-13391 (1996).
    • (1996) J. Biol. Chem , vol.271 , pp. 13385-13391
    • Nicoll, D.A.1    Hryshko, L.V.2    Matsuoka, S.3    Frank, J.S.4    Philipson, K.D.5
  • 19
    • 0037457918 scopus 로고    scopus 로고
    • Scanning mutagenesis of the alpha repeats and of the transmembrane acidic residues of the human retinal cone Na/Ca-K exchanger
    • Winkfein, R. J. et al. Scanning mutagenesis of the alpha repeats and of the transmembrane acidic residues of the human retinal cone Na/Ca-K exchanger. Biochemistry 42, 543-552 (2003).
    • (2003) Biochemistry , vol.42 , pp. 543-552
    • Winkfein, R.J.1
  • 20
    • 14844321878 scopus 로고    scopus 로고
    • Residues contributing to the Ca21 and K1 binding pocket of the NCKX2 Na1/Ca21-K1 exchanger
    • Kang, K.-J. Residues contributing to the Ca21 and K1 binding pocket of the NCKX2 Na1/Ca21-K1 exchanger. J. Biol. Chem. 280, 6823-6833 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 6823-6833
    • Kang, K.-J.1
  • 22
    • 0035201584 scopus 로고    scopus 로고
    • Regulation of CAX1, an Arabidopsis Ca21/H1 antiporter. Identification of an N-terminal autoinhibitory domain
    • Pittman, J. K. & Hirschi, K. D. Regulation of CAX1, an Arabidopsis Ca21/H1 antiporter. Identification of an N-terminal autoinhibitory domain. Plant Physiol. 127, 1020-1029 (2001).
    • (2001) Plant Physiol , vol.127 , pp. 1020-1029
    • Pittman, J.K.1    Hirschi, K.D.2
  • 23
    • 0027302377 scopus 로고
    • Cloning andcharacterizationof aputativeCa21/H1antiporter gene from Escherichia coli upon functional complementation of Na1/H1 anti porterdeficient strains by the overexpressed gene
    • Ivey, D. M. et al. Cloning andcharacterizationof aputativeCa21/ H1antiporter gene from Escherichia coli upon functional complementation of Na1/H1 antiporterdeficient strains by the overexpressed gene. J. Biol. Chem. 268, 11296-11303 (1993).
    • (1993) J. Biol. Chem , vol.268 , pp. 11296-11303
    • Ivey, D.M.1
  • 24
    • 0020630774 scopus 로고
    • Calcium transport driven by a proton motive force in vacuolar membrane vesicles of Saccharomyces cerevisiae
    • Ohsumi, Y. & Anraku, Y. Calcium transport driven by a proton motive force in vacuolar membrane vesicles of Saccharomyces cerevisiae. J. Biol. Chem. 258, 5614-5617 (1983).
    • (1983) J. Biol. Chem , vol.258 , pp. 5614-5617
    • Ohsumi, Y.1    Anraku, Y.2
  • 25
    • 0028174938 scopus 로고
    • Regulation of cellular Ca21 by yeast vacuoles
    • Dunn, T. , Gable, K. & Beeler, T. Regulation of cellular Ca21 by yeast vacuoles. J. Biol. Chem. 269, 7273-7278 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 7273-7278
    • Dunn, T.1    Gable, K.2    Beeler, T.3
  • 26
    • 0345791501 scopus 로고    scopus 로고
    • Residues in internal repeats of the rice cation/H1 exchanger are involved in the transport and selection of cations
    • Kamiya, T. & Maeshima, M. Residues in internal repeats of the rice cation/H1 exchanger are involved in the transport and selection of cations. J. Biol. Chem. 279, 812-819 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 812-819
    • Kamiya, T.1    Maeshima, M.2
  • 27
    • 24044521004 scopus 로고    scopus 로고
    • Identification of a crucial histidine involved in metal transport activity in the Arabidopsis cation/H1 exchanger CAX1
    • Shigaki, T. et al. Identification of a crucial histidine involved in metal transport activity in the Arabidopsis cation/H1 exchanger CAX1. J. Biol. Chem. 280, 30136-30142 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 30136-30142
    • Shigaki, T.1
  • 29
    • 33746809433 scopus 로고    scopus 로고
    • The crystal structure of the primary Ca21 sensor of the Na1/Ca21 exchanger reveals a novel Ca21 binding motif
    • Nicoll, D. A. et al. The crystal structure of the primary Ca21 sensor of the Na1/Ca21 exchanger reveals a novel Ca21 binding motif. J. Biol. Chem. 281, 21577-21581 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 21577-21581
    • Nicoll, D.A.1
  • 30
    • 50649120655 scopus 로고    scopus 로고
    • Vacuolar and plasma membrane proton pumps collaborate to achieve cytosolic pH homeostasis in yeast
    • Mart?́nez-Muñoz, G. A. & Kane, P. Vacuolar and plasma membrane proton pumps collaborate to achieve cytosolic pH homeostasis in yeast. J. Biol. Chem. 283, 20309-20319 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 20309-20319
    • Mart́nez-Muñoz, G.A.1    Kane, P.2
  • 31
    • 58149110771 scopus 로고    scopus 로고
    • Selecting optimumeukaryotic integralmembraneproteins for structure determination by rapid expression and solubilization screening
    • Li, M. et al. Selecting optimumeukaryotic integralmembraneproteins for structure determination by rapid expression and solubilization screening. J. Mol. Biol. 385, 820-830 (2009).
    • (2009) J. Mol. Biol , vol.385 , pp. 820-830
    • Li, M.1
  • 32
    • 84870482175 scopus 로고    scopus 로고
    • Identification of the dimer interface of a bacterial Ca21/H1 antiporter
    • Ridilla, M. , Narayanan, A. , Bolin, J. T. & Yernool, D. A. Identification of the dimer interface of a bacterial Ca21/H1 antiporter. Biochemistry 51, 9603-9611 (2012).
    • (2012) Biochemistry , vol.51 , pp. 9603-9611
    • Ridilla, M.1    Narayanan, A.2    Bolin, J.T.3    Yernool, D.A.4
  • 33
    • 0021895138 scopus 로고
    • A new generation of Ca21 indicators with greatly improved fluorescence properties
    • Grynkiewicz, G. , Poenie, M. & Tsien, R. Y. A new generation of Ca21 indicators with greatly improved fluorescence properties. J. Biol. Chem. 260, 3440-3450 (1985).
    • (1985) J. Biol. Chem , vol.260 , pp. 3440-3450
    • Grynkiewicz, G.1    Poenie, M.2    Tsien, R.Y.3
  • 34
    • 67649392795 scopus 로고    scopus 로고
    • Crystallizing membrane proteins using lipidic mesophases
    • Caffrey, M. & Cherezov, V. Crystallizing membrane proteins using lipidic mesophases. Nature Protocols 4, 706-731 (2009).
    • (2009) Nature Protocols , vol.4 , pp. 706-731
    • Caffrey, M.1    Cherezov, V.2
  • 36
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX : A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX : a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 37
    • 79953737180 scopus 로고    scopus 로고
    • Overview of the CCP4 suite and current developments
    • Winn, M. D. et al. Overview of the CCP4 suite and current developments. Acta Crystallogr. 67, 235-242 (2011).
    • (2011) Acta Crystallogr , vol.67 , pp. 235-242
    • Winn, M.D.1
  • 39
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger, T. C. Maximum-likelihood density modification. Acta Crystallogr. D 56, 965-972 (2000).
    • (2000) Acta Crystallogr. D , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
  • 40
    • 13244281317 scopus 로고    scopus 로고
    • Model-building tools for molecular graphics
    • Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Coot, C.K.2
  • 41
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A. & Blundell, T. L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815 (1993).
    • (1993) J. Mol. Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 42
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-a visualization system for exploratory research and analysis
    • Pettersen, E. F. et al. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 43
    • 42449090264 scopus 로고    scopus 로고
    • PROMALS3D: A tool formultiple protein sequence and structure alignments
    • Pei, J. , Kim, B.-H. &Grishin, N. V. PROMALS3D: a tool formultiple protein sequence and structure alignments. Nucleic Acids Res. 36, 2295-2300 (2008).
    • (2008) Nucleic Acids Res , vol.36 , pp. 2295-2300
    • Pei, J.1    Kim, B.-H.2    Grishin, N.V.3
  • 45
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of nanosystems: Application to microtubules and the ribosome
    • Baker, N. A. , Sept, D. , Joseph, S. , Holst, M. J. & McCammon, J. A. Electrostatics of nanosystems: Application to microtubules and the ribosome. Proc. Natl Acad. Sci. USA 98, 10037-10041 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 10037-10041
    • Baker, N.A.1    Sept, D.2    Joseph, S.3    Holst, M.J.4    McCammon, J.A.5
  • 46
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalablemolecular simulation
    • Hess, B. , Kutzner, C. , Van der Spoel, D. & Lindahl, E. GROMACS 4: Algorithms for highly efficient, load-balanced, and scalablemolecular simulation. J. Chem. Theory Comput. 4, 435-447 (2008).
    • (2008) J. Chem. Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 47
    • 77950106854 scopus 로고    scopus 로고
    • Implementation of the CHARMM force field in GROMACS: Analysis of protein stability effects from correction maps, virtual interaction sites, and water models
    • Bjelkmar, P. , Larsson, P. , Cuendet, M. A. , Hess, B. & Lindahl, E. Implementation of the CHARMM force field in GROMACS: Analysis of protein stability effects from correction maps, virtual interaction sites, and water models. J. Chem. Theory Comput. 6, 459-466 (2010).
    • (2010) J. Chem. Theory Comput , vol.6 , pp. 459-466
    • Bjelkmar, P.1    Larsson, P.2    Cuendet, M.A.3    Hess, B.4    Lindahl, E.5
  • 49
    • 84861060898 scopus 로고    scopus 로고
    • OPMdatabase andPPMweb server: Resources for positioning of proteins inmembranes
    • Lomize, M. A. , Pogozheva, I. D. , Joo, H. ,Mosberg, H. I. & Lomize, A. L. OPMdatabase andPPMweb server: resources for positioning of proteins inmembranes. Nucleic Acids Res. 40, D370-D376 (2012).
    • (2012) Nucleic Acids Res , vol.40
    • Lomize, M.A.1    Pogozheva, I.D.2    Joo Mosberg, H.H.I.3    Lomize, A.L.4
  • 50
    • 68949149548 scopus 로고    scopus 로고
    • CHARMM-GUI Membrane Builder for mixed bilayers and its application to yeast membranes
    • Jo, S. , Lim, J. B. , Klauda, J. B. & Im, W. CHARMM-GUI Membrane Builder for mixed bilayers and its application to yeast membranes. Biophys. J. 97, 50-58 (2009).
    • (2009) Biophys. J , vol.97 , pp. 50-58
    • Jo, S.1    Lim, J.B.2    Klauda, J.B.3    Im, W.4
  • 52
    • 33846086933 scopus 로고    scopus 로고
    • Canonical sampling through velocity rescaling
    • Bussi, G. , Donadio, D. & Parrinello, M. Canonical sampling through velocity rescaling. J. Chem. Phys. 126, 014101-014101-7 (2007).
    • (2007) J. Chem. Phys , vol.126 , pp. 014101-0141017
    • Bussi, G.1    Donadio, D.2    Parrinello, M.3
  • 53
    • 0019707626 scopus 로고
    • Polymorphic transitions in single crystals: A new molecular dynamics method
    • Parrinello, M. & Rahman, A. Polymorphic transitions in single crystals: A new molecular dynamics method. J. Appl. Phys. 52, 7182-7190 (1981).
    • (1981) J. Appl. Phys , vol.52 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.