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Volumn 531, Issue 7593, 2016, Pages 196-201

Structure of the voltage-gated two-pore channel TPC1 from Arabidopsis thaliana

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; MEMBRANE PROTEIN; TPC1 PROTEIN; UNCLASSIFIED DRUG; ARABIDOPSIS PROTEIN; BARIUM; CALCIUM CHANNEL; PROTEIN SUBUNIT; TPC1 PROTEIN, ARABIDOPSIS;

EID: 84960906119     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature16446     Document Type: Article
Times cited : (196)

References (57)
  • 1
    • 15244350821 scopus 로고    scopus 로고
    • The vacuolar Ca2+-activated channel TPC1 regulates germination and stomatal movement
    • Peiter, E. et al. The vacuolar Ca2+-activated channel TPC1 regulates germination and stomatal movement. Nature 434, 404-408 (2005).
    • (2005) Nature , vol.434 , pp. 404-408
    • Peiter, E.1
  • 2
    • 67349287016 scopus 로고    scopus 로고
    • NAADP mobilizes calcium from acidic organelles through two-pore channels
    • Calcraft, P. J. et al. NAADP mobilizes calcium from acidic organelles through two-pore channels. Nature 459, 596-600 (2009).
    • (2009) Nature , vol.459 , pp. 596-600
    • Calcraft, P.J.1
  • 3
    • 79957445309 scopus 로고    scopus 로고
    • TPC1-SV channels gain shape
    • Hedrich, R., Marten, I. TPC1-SV channels gain shape. Mol. Plant 4, 428-441 (2011).
    • (2011) Mol. Plant , vol.4 , pp. 428-441
    • Hedrich, R.1    Marten, I.2
  • 4
    • 84922794140 scopus 로고    scopus 로고
    • Lysosomal physiology
    • Xu, H., Ren, D. Lysosomal physiology. Annu. Rev. Physiol. 77, 57-80 (2015).
    • (2015) Annu. Rev. Physiol. , vol.77 , pp. 57-80
    • Xu, H.1    Ren, D.2
  • 5
    • 84911957032 scopus 로고    scopus 로고
    • Two-pore channels provide insight into the evolution of voltage-gated Ca2+ and Na+ channels
    • Rahman, T. et al. Two-pore channels provide insight into the evolution of voltage-gated Ca2+ and Na+ channels. Sci. Signal. 7, ra109 (2014).
    • (2014) Sci. Signal. , vol.7 , pp. 109
    • Rahman, T.1
  • 6
    • 0023225798 scopus 로고
    • Cloning of genomic and complementary DNA from Shaker, a putative potassium channel gene from Drosophila
    • Papazian, D. M., Schwarz, T. L., Tempel, B. L., Jan, Y. N., Jan, L. Y. Cloning of genomic and complementary DNA from Shaker, a putative potassium channel gene from Drosophila. Science 237, 749-753 (1987).
    • (1987) Science , vol.237 , pp. 749-753
    • Papazian, D.M.1    Schwarz, T.L.2    Tempel, B.L.3    Jan, Y.N.4    Jan, L.Y.5
  • 7
    • 0034643304 scopus 로고    scopus 로고
    • Molecular cloning of a novel form (two-repeat) protein related to voltage-gated sodium and calcium channels
    • Ishibashi, K., Suzuki, M., Imai, M. Molecular cloning of a novel form (two-repeat) protein related to voltage-gated sodium and calcium channels. Biochem. Biophys. Res. Commun. 270, 370-376 (2000).
    • (2000) Biochem. Biophys. Res. Commun. , vol.270 , pp. 370-376
    • Ishibashi, K.1    Suzuki, M.2    Imai, M.3
  • 8
    • 67749143745 scopus 로고    scopus 로고
    • Essential requirement for two-pore channel 1 in NAADPmediated calcium signaling
    • Brailoiu, E. et al. Essential requirement for two-pore channel 1 in NAADPmediated calcium signaling. J. Cell Biol. 186, 201-209 (2009).
    • (2009) J. Cell Biol. , vol.186 , pp. 201-209
    • Brailoiu, E.1
  • 9
    • 68149098891 scopus 로고    scopus 로고
    • The two-pore channel TPCN2 mediates NAADP-dependent Ca2+-release from lysosomal stores
    • Zong, X. et al. The two-pore channel TPCN2 mediates NAADP-dependent Ca2+-release from lysosomal stores. Eur. J. Phys. 458, 891-899 (2009).
    • (2009) Eur. J. Phys. , vol.458 , pp. 891-899
    • Zong, X.1
  • 10
    • 84867565289 scopus 로고    scopus 로고
    • TPC proteins are phosphoinositide-activated sodium-selective ion channels in endosomes and lysosomes
    • Wang, X. et al. TPC proteins are phosphoinositide-activated sodium-selective ion channels in endosomes and lysosomes. Cell 151, 372-383 (2012).
    • (2012) Cell , vol.151 , pp. 372-383
    • Wang, X.1
  • 11
    • 84874105202 scopus 로고    scopus 로고
    • MTOR regulates lysosomal ATP-sensitive two-pore Na+ channels to adapt to metabolic state
    • Cang, C. et al. mTOR regulates lysosomal ATP-sensitive two-pore Na+ channels to adapt to metabolic state. Cell 152, 778-790 (2013).
    • (2013) Cell , vol.152 , pp. 778-790
    • Cang, C.1
  • 12
    • 84901235419 scopus 로고    scopus 로고
    • The voltage-gated sodium channel TPC1 confers endolysosomal excitability
    • Cang, C., Bekele, B., Ren, D. The voltage-gated sodium channel TPC1 confers endolysosomal excitability. Nature Chem. Biol. 10, 463-469 (2014).
    • (2014) Nature Chem. Biol. , vol.10 , pp. 463-469
    • Cang, C.1    Bekele, B.2    Ren, D.3
  • 13
    • 84898630877 scopus 로고    scopus 로고
    • Convergent regulation of the lysosomal two-pore channel-2 by Mg2+ NAADP, PI(3, 5)P2 and multiple protein kinases
    • Jha, A., Ahuja, M., Patel, S., Brailoiu, E., Muallem, S. Convergent regulation of the lysosomal two-pore channel-2 by Mg2+, NAADP, PI(3,5)P2 and multiple protein kinases. EMBO J. 33, 501-511 (2014).
    • (2014) EMBO J. , vol.33 , pp. 501-511
    • Jha, A.1    Ahuja, M.2    Patel, S.3    Brailoiu, E.4    Muallem, S.5
  • 14
    • 84901191676 scopus 로고    scopus 로고
    • Reconstituted human TPC1 is a proton-permeable ion channel and is activated by NAADP or Ca2
    • Pitt, S. J., Lam, A. K., Rietdorf, K., Galione, A., Sitsapesan, R. Reconstituted human TPC1 is a proton-permeable ion channel and is activated by NAADP or Ca2+. Sci. Signal. 7, ra46 (2014).
    • (2014) Sci. Signal. , vol.7 , pp. 46
    • Pitt, S.J.1    Lam, A.K.2    Rietdorf, K.3    Galione, A.4    Sitsapesan, R.5
  • 15
    • 84933674860 scopus 로고    scopus 로고
    • Expression of Ca2+-permeable two-pore channels rescues NAADP signalling in TPC-deficient cells
    • Ruas, M. et al. Expression of Ca2+-permeable two-pore channels rescues NAADP signalling in TPC-deficient cells. EMBO J. 34, 1743-1758 (2015).
    • (2015) EMBO J. , vol.34 , pp. 1743-1758
    • Ruas, M.1
  • 16
    • 84923815384 scopus 로고    scopus 로고
    • Ebola virus Two-pore channels control Ebola virus host cell entry and are drug targets for disease treatment
    • Sakurai, Y. et al. Ebola virus. Two-pore channels control Ebola virus host cell entry and are drug targets for disease treatment. Science 347, 995-998 (2015).
    • (2015) Science , vol.347 , pp. 995-998
    • Sakurai, Y.1
  • 17
    • 0034800349 scopus 로고    scopus 로고
    • A putative two pore channel AtTPC1 mediates Ca2+ flux in Arabidopsis leaf cells
    • Furuichi, T. et al. A putative two pore channel AtTPC1 mediates Ca2+ flux in Arabidopsis leaf cells. Plant Cell Physiol. 42, 900-905 (2001).
    • (2001) Plant Cell Physiol. , vol.42 , pp. 900-905
    • Furuichi, T.1
  • 18
    • 0000283706 scopus 로고
    • Cytoplasmic calcium regulates voltage-dependent ion channels
    • Hedrich, R., Neher, E. Cytoplasmic calcium regulates voltage-dependent ion channels. Nature 329, 833-836 (1987).
    • (1987) Nature , vol.329 , pp. 833-836
    • Hedrich, R.1    Neher, E.2
  • 19
    • 0028120093 scopus 로고
    • A cationic channel in the guard cell tonoplast of Allium cepa
    • Amodeo, G., Escobar, A., Zeiger, E. A cationic channel in the guard cell tonoplast of Allium cepa. Plant Physiol. 105, 999-1006 (1994).
    • (1994) Plant Physiol. , vol.105 , pp. 999-1006
    • Amodeo, G.1    Escobar, A.2    Zeiger, E.3
  • 20
    • 0027977519 scopus 로고
    • Calcium-activated K+ channels and calciuminduced calcium release by slow vacuolar ion channels in guard cell vacuoles implicated in the control of stomatal closure
    • Ward, J. M., Schroeder, J. I. Calcium-activated K+ channels and calciuminduced calcium release by slow vacuolar ion channels in guard cell vacuoles implicated in the control of stomatal closure. Plant Cell 6, 669-683 (1994).
    • (1994) Plant Cell , vol.6 , pp. 669-683
    • Ward, J.M.1    Schroeder, J.I.2
  • 21
    • 80051933262 scopus 로고    scopus 로고
    • Differential contribution of EF-hands to the Ca2+-dependent activation in the plant two-pore channel TPC1
    • Schulze, C., Sticht, H., Meyerhoff, P., Dietrich, P. Differential contribution of EF-hands to the Ca2+-dependent activation in the plant two-pore channel TPC1. Plant J. 68, 424-432 (2011).
    • (2011) Plant J. , vol.68 , pp. 424-432
    • Schulze, C.1    Sticht, H.2    Meyerhoff, P.3    Dietrich, P.4
  • 22
    • 80051948142 scopus 로고    scopus 로고
    • A novel calcium binding site in the slow vacuolar cation channel TPC1 senses luminal calcium levels
    • Dadacz-Narloch, B. et al. A novel calcium binding site in the slow vacuolar cation channel TPC1 senses luminal calcium levels. Plant Cell 23, 2696-2707 (2011).
    • (2011) Plant Cell , vol.23 , pp. 2696-2707
    • Dadacz-Narloch, B.1
  • 23
    • 33847122121 scopus 로고    scopus 로고
    • A gain-of-function allele of TPC1 activates oxylipin biogenesis after leaf wounding in Arabidopsis
    • Bonaventure, G. et al. A gain-of-function allele of TPC1 activates oxylipin biogenesis after leaf wounding in Arabidopsis. Plant J. 49, 889-898 (2007).
    • (2007) Plant J. , vol.49 , pp. 889-898
    • Bonaventure, G.1
  • 24
    • 37149016373 scopus 로고    scopus 로고
    • The fou2 gain-of-function allele and the wild-type allele of Two Pore Channel 1 contribute to different extents or by different mechanisms to defense gene expression in Arabidopsis
    • Bonaventure, G., Gfeller, A., Rodriguez, V. M., Armand, F., Farmer, E. E. The fou2 gain-of-function allele and the wild-type allele of Two Pore Channel 1 contribute to different extents or by different mechanisms to defense gene expression in Arabidopsis. Plant Cell Physiol. 48, 1775-1789 (2007).
    • (2007) Plant Cell Physiol , vol.48 , pp. 1775-1789
    • Bonaventure, G.1    Gfeller, A.2    Rodriguez, V.M.3    Armand, F.4    Farmer, E.E.5
  • 25
    • 84899648974 scopus 로고    scopus 로고
    • Salt stress-induced Ca2+ waves are associated with rapid, long-distance root-to-shoot signaling in plants
    • Choi, W. G., Toyota, M., Kim, S. H., Hilleary, R., Gilroy, S. Salt stress-induced Ca2+ waves are associated with rapid, long-distance root-to-shoot signaling in plants. Proc. Natl Acad. Sci. USA 111, 6497-6502 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 6497-6502
    • Choi, W.G.1    Toyota, M.2    Kim, S.H.3    Hilleary, R.4    Gilroy, S.5
  • 26
    • 79960621367 scopus 로고    scopus 로고
    • The crystal structure of a voltage-gated sodium channel
    • Payandeh, J., Scheuer, T., Zheng, N., Catterall, W. A. The crystal structure of a voltage-gated sodium channel. Nature 475, 353-358 (2011).
    • (2011) Nature , vol.475 , pp. 353-358
    • Payandeh, J.1    Scheuer, T.2    Zheng, N.3    Catterall, W.A.4
  • 27
    • 84861952634 scopus 로고    scopus 로고
    • Crystal structure of an orthologue of the NaChBac voltagegated sodium channel
    • Zhang, X. et al. Crystal structure of an orthologue of the NaChBac voltagegated sodium channel. Nature 486, 130-134 (2012).
    • (2012) Nature , vol.486 , pp. 130-134
    • Zhang, X.1
  • 28
    • 85027943451 scopus 로고    scopus 로고
    • An N-terminal dileucine motif directs two-pore channels to the tonoplast of plant cells
    • Larisch, N., Schulze, C., Galione, A., Dietrich, P. An N-terminal dileucine motif directs two-pore channels to the tonoplast of plant cells. Traffic 13, 1012-1022 (2012).
    • (2012) Traffic , vol.13 , pp. 1012-1022
    • Larisch, N.1    Schulze, C.2    Galione, A.3    Dietrich, P.4
  • 29
    • 84897977217 scopus 로고    scopus 로고
    • X-ray crystal structure of voltage-gated proton channel
    • Takeshita, K. et al. X-ray crystal structure of voltage-gated proton channel. Nature Struct. Mol. Biol. 21, 352-357 (2014).
    • (2014) Nature Struct. Mol. Biol. , vol.21 , pp. 352-357
    • Takeshita, K.1
  • 31
    • 36248982122 scopus 로고    scopus 로고
    • Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment
    • Long, S. B., Tao, X., Campbell, E. B., MacKinnon, R. Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment. Nature 450, 376-382 (2007).
    • (2007) Nature , vol.450 , pp. 376-382
    • Long, S.B.1    Tao, X.2    Campbell, E.B.3    MacKinnon, R.4
  • 32
    • 78650055985 scopus 로고    scopus 로고
    • 310 helices in channels and other membrane proteins
    • Vieira-Pires, R. S., Morais-Cabral, J. H. 310 helices in channels and other membrane proteins. J. Gen. Physiol. 136, 585-592 (2010).
    • (2010) J. Gen. Physiol. , vol.136 , pp. 585-592
    • Vieira-Pires, R.S.1    Morais-Cabral, J.H.2
  • 33
    • 0016354136 scopus 로고
    • Charge movement associated with the opening and closing of the activation gates of the Na channels
    • Armstrong, C. M., Bezanilla, F. Charge movement associated with the opening and closing of the activation gates of the Na channels. J. Gen. Physiol. 63, 533-552 (1974).
    • (1974) J. Gen. Physiol. , vol.63 , pp. 533-552
    • Armstrong, C.M.1    Bezanilla, F.2
  • 34
    • 0030175867 scopus 로고    scopus 로고
    • Voltage-sensing residues in the S2 and S4 segments of the Shaker K+ channel
    • Seoh, S. A., Sigg, D., Papazian, D. M., Bezanilla, F. Voltage-sensing residues in the S2 and S4 segments of the Shaker K+ channel. Neuron 16, 1159-1167 (1996).
    • (1996) Neuron , vol.16 , pp. 1159-1167
    • Seoh, S.A.1    Sigg, D.2    Papazian, D.M.3    Bezanilla, F.4
  • 35
    • 0030175348 scopus 로고    scopus 로고
    • Contribution of the S4 segment to gating charge in the Shaker K+ channel
    • Aggarwal, S. K., MacKinnon, R. Contribution of the S4 segment to gating charge in the Shaker K+ channel. Neuron 16, 1169-1177 (1996).
    • (1996) Neuron , vol.16 , pp. 1169-1177
    • Aggarwal, S.K.1    MacKinnon, R.2
  • 36
    • 0026594721 scopus 로고
    • The size of gating charge in wild-type and mutant Shaker potassium channels
    • Schoppa, N. E., McCormack, K., Tanouye, M. A., Sigworth, F. J. The size of gating charge in wild-type and mutant Shaker potassium channels. Science 255, 1712-1715 (1992).
    • (1992) Science , vol.255 , pp. 1712-1715
    • Schoppa, N.E.1    McCormack, K.2    Tanouye, M.A.3    Sigworth, F.J.4
  • 38
    • 0030070436 scopus 로고    scopus 로고
    • Transmembrane movement of the Shaker K+ channel S4
    • Larsson, H. P., Baker, O. S., Dhillon, D. S., Isacoff, E. Y. Transmembrane movement of the Shaker K+ channel S4. Neuron 16, 387-397 (1996).
    • (1996) Neuron , vol.16 , pp. 387-397
    • Larsson, H.P.1    Baker, O.S.2    Dhillon, D.S.3    Isacoff, E.Y.4
  • 39
    • 0038752614 scopus 로고    scopus 로고
    • The principle of gating charge movement in a voltage-dependent K+ channel
    • Jiang, Y., Ruta, V., Chen, J., Lee, A., MacKinnon, R. The principle of gating charge movement in a voltage-dependent K+ channel. Nature 423, 42-48 (2003).
    • (2003) Nature , vol.423 , pp. 42-48
    • Jiang, Y.1    Ruta, V.2    Chen, J.3    Lee, A.4    MacKinnon, R.5
  • 40
    • 27544516349 scopus 로고    scopus 로고
    • Calibrated measurement of gating-charge arginine displacement in the KvAP voltage-dependent K+ channel
    • Ruta, V., Chen, J., MacKinnon, R. Calibrated measurement of gating-charge arginine displacement in the KvAP voltage-dependent K+ channel. Cell 123, 463-475 (2005).
    • (2005) Cell , vol.123 , pp. 463-475
    • Ruta, V.1    Chen, J.2    MacKinnon, R.3
  • 41
    • 84895872710 scopus 로고    scopus 로고
    • Structural mechanism of voltage-dependent gating in an isolated voltage-sensing domain
    • Li, Q. et al. Structural mechanism of voltage-dependent gating in an isolated voltage-sensing domain. Nature Struct. Mol. Biol. 21, 244-252 (2014).
    • (2014) Nature Struct. Mol. Biol. , vol.21 , pp. 244-252
    • Li, Q.1
  • 42
    • 0038076054 scopus 로고    scopus 로고
    • X-ray structure of a voltage-dependent K+ channel
    • Jiang, Y. et al. X-ray structure of a voltage-dependent K+ channel. Nature 423, 33-41 (2003).
    • (2003) Nature , vol.423 , pp. 33-41
    • Jiang, Y.1
  • 43
    • 77955626630 scopus 로고    scopus 로고
    • Shaker K+ channel with a miniature engineered voltage sensor
    • Xu, Y., Ramu, Y., Lu, Z. Shaker K+ channel with a miniature engineered voltage sensor. Cell 142, 580-589 (2010).
    • (2010) Cell , vol.142 , pp. 580-589
    • Xu, Y.1    Ramu, Y.2    Lu, Z.3
  • 44
    • 0036795297 scopus 로고    scopus 로고
    • Voltage sensor movements
    • Bezanilla, F. Voltage sensor movements. J. Gen. Physiol. 120, 465-473 (2002).
    • (2002) J. Gen. Physiol. , vol.120 , pp. 465-473
    • Bezanilla, F.1
  • 45
    • 0036792837 scopus 로고    scopus 로고
    • Molecular models of voltage sensing
    • Gandhi, C. S., Isacoff, E. Y. Molecular models of voltage sensing. J. Gen. Physiol. 120, 455-463 (2002).
    • (2002) J. Gen. Physiol. , vol.120 , pp. 455-463
    • Gandhi, C.S.1    Isacoff, E.Y.2
  • 46
    • 0036794098 scopus 로고    scopus 로고
    • Coupled movements in voltage-gated ion channels
    • Horn, R. Coupled movements in voltage-gated ion channels. J. Gen. Physiol. 120, 449-453 (2002).
    • (2002) J. Gen. Physiol. , vol.120 , pp. 449-453
    • Horn, R.1
  • 47
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 48
    • 33744459472 scopus 로고    scopus 로고
    • Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis
    • Strong, M. et al. Toward the structural genomics of complexes: crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis. Proc. Natl Acad. Sci. USA 103, 8060-8065 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 8060-8065
    • Strong, M.1
  • 51
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • Fortelle, E. l., Bricogne, G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494 (1997).
    • (1997) Methods Enzymol , vol.276 , pp. 472-494
    • Fortelle, E.L.1    Bricogne, G.2
  • 52
    • 0242460576 scopus 로고    scopus 로고
    • Generation representation and flow of phase information in structure determination: Recent developments in and around SHARP 2.0
    • Bricogne, G., Vonrhein, C., Flensburg, C., Schiltz, M., Paciorek, W. Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0. Acta Crystallogr. D 59, 2023-2030 (2003).
    • (2003) Acta Crystallogr. D , vol.59 , pp. 2023-2030
    • Bricogne, G.1    Vonrhein, C.2    Flensburg, C.3    Schiltz, M.4    Paciorek, W.5
  • 53
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1-ATPase
    • Abrahams, J. P., Leslie, A. G. W. Methods used in the structure determination of bovine mitochondrial F1-ATPase. Acta Crystallogr. D 52, 30-42 (1996).
    • (1996) Acta Crystallogr. D , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.W.2
  • 54
    • 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
  • 56
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., Thornton, J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291 (1993).
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4


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