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Volumn 23, Issue 2, 2016, Pages 180-186

Cryo-electron microscopy structure of the TRPV2 ion channel

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN; VANILLOID RECEPTOR 1; VANILLOID RECEPTOR 2; VANILLOID RECEPTOR;

EID: 84956830463     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.3159     Document Type: Article
Times cited : (231)

References (56)
  • 2
    • 34948851846 scopus 로고    scopus 로고
    • From chills to chilis: Mechanisms for thermosensation and chemesthesis via thermoTRPs
    • Bandell, M., Macpherson, L.J., & Patapoutian, A. From chills to chilis: mechanisms for thermosensation and chemesthesis via thermoTRPs. Curr. Opin. Neurobiol. 17, 490-497 (2007
    • (2007) Curr. Opin. Neurobiol , vol.17 , pp. 490-497
    • Bandell, M.1    Macpherson, L.J.2    Patapoutian, A.3
  • 3
    • 0030777012 scopus 로고    scopus 로고
    • The capsaicin receptor: A heat-activated ion channel in the pain pathway
    • Caterina, M.J., et al. The capsaicin receptor: a heat-activated ion channel in the pain pathway. Nature 389, 816-824 (1997
    • (1997) Nature , vol.389 , pp. 816-824
    • Caterina, M.J.1
  • 4
  • 5
    • 84874229704 scopus 로고    scopus 로고
    • TRPV1 channels are intrinsically heat sensitive and negatively regulated by phosphoinositide lipids
    • Cao, E., Cordero-Morales, J.F., Liu, B., Qin, F., & Julius, D. TRPV1 channels are intrinsically heat sensitive and negatively regulated by phosphoinositide lipids. Neuron 77, 667-679 (2013
    • (2013) Neuron , vol.77 , pp. 667-679
    • Cao, E.1    Cordero-Morales, J.F.2    Liu, B.3    Qin, F.4    Julius, D.5
  • 6
    • 84947718665 scopus 로고    scopus 로고
    • Mechanism for phosphoinositide selectivity and activation of TRPV1 ion channels
    • Ufret-Vincenty, C.A., et al. Mechanism for phosphoinositide selectivity and activation of TRPV1 ion channels. J. Gen. Physiol. 145, 431-442 (2015
    • (2015) J. Gen. Physiol , vol.145 , pp. 431-442
    • Ufret-Vincenty, C.A.1
  • 7
    • 0033119629 scopus 로고    scopus 로고
    • A capsaicin-receptor homologue with a high threshold for noxious heat
    • Caterina, M.J., Rosen, T.A., Tominaga, M., Brake, A.J., & Julius, D. A capsaicin-receptor homologue with a high threshold for noxious heat. Nature 398, 436-441 (1999
    • (1999) Nature , vol.398 , pp. 436-441
    • Caterina, M.J.1    Rosen, T.A.2    Tominaga, M.3    Brake, A.J.4    Julius, D.5
  • 8
    • 84886091614 scopus 로고    scopus 로고
    • What do we know about the transient receptor potential vanilloid 2 (TRPV2) ion channel?
    • Perálvarez-Marín, A., Doñate-Macian, P., & Gaudet, R. What do we know about the transient receptor potential vanilloid 2 (TRPV2) ion channel?. FEBS J. 280, 5471-5487 (2013
    • (2013) FEBS J. , vol.280 , pp. 5471-5487
    • Perálvarez-Marín, A.1    Doñate-Macian, P.2    Gaudet, R.3
  • 9
    • 46749129338 scopus 로고    scopus 로고
    • TRPV2 is activated by cannabidiol and mediates CGRP release in cultured rat dorsal root ganglion neurons
    • Qin, N., et al. TRPV2 is activated by cannabidiol and mediates CGRP release in cultured rat dorsal root ganglion neurons. J. Neurosci. 28, 6231-6238 (2008
    • (2008) J. Neurosci , vol.28 , pp. 6231-6238
    • Qin, N.1
  • 10
    • 33646495512 scopus 로고    scopus 로고
    • PI3-kinase promotes TRPV2 activity independently of channel translocation to the plasma membrane
    • Penna, A., et al. PI3-kinase promotes TRPV2 activity independently of channel translocation to the plasma membrane. Cell Calcium 39, 495-507 (2006
    • (2006) Cell Calcium , vol.39 , pp. 495-507
    • Penna, A.1
  • 11
    • 77950669891 scopus 로고    scopus 로고
    • TRPV2 enhances axon outgrowth through its activation by membrane stretch in developing sensory and motor neurons
    • Shibasaki, K., Murayama, N., Ono, K., Ishizaki, Y., & Tominaga, M. TRPV2 enhances axon outgrowth through its activation by membrane stretch in developing sensory and motor neurons. J. Neurosci. 30, 4601-4612 (2010
    • (2010) J. Neurosci , vol.30 , pp. 4601-4612
    • Shibasaki, K.1    Murayama, N.2    Ono, K.3    Ishizaki, Y.4    Tominaga, M.5
  • 12
    • 84940591319 scopus 로고    scopus 로고
    • Osmosensation in TRPV2 dominant negative expressing skeletal muscle fibres
    • Zanou, N., et al. Osmosensation in TRPV2 dominant negative expressing skeletal muscle fibres. J. Physiol. 593, 3849-3863 (2015
    • (2015) J. Physiol , vol.593 , pp. 3849-3863
    • Zanou, N.1
  • 13
    • 84901779049 scopus 로고    scopus 로고
    • TRPV2 is critical for the maintenance of cardiac structure and function in mice
    • Katanosaka, Y., et al. TRPV2 is critical for the maintenance of cardiac structure and function in mice. Nat. Commun. 5, 3932 (2014
    • (2014) Nat. Commun , vol.5 , pp. 3932
    • Katanosaka, Y.1
  • 14
    • 76949094139 scopus 로고    scopus 로고
    • TRPV2 has a pivotal role in macrophage particle binding and phagocytosis
    • Link, T.M., et al. TRPV2 has a pivotal role in macrophage particle binding and phagocytosis. Nat. Immunol. 11, 232-239 (2010
    • (2010) Nat. Immunol , vol.11 , pp. 232-239
    • Link, T.M.1
  • 15
    • 76249107718 scopus 로고    scopus 로고
    • Role of cationic channel TRPV2 in promoting prostate cancer migration and progression to androgen resistance
    • Monet, M., et al. Role of cationic channel TRPV2 in promoting prostate cancer migration and progression to androgen resistance. Cancer Res. 70, 1225-1235 (2010
    • (2010) Cancer Res , vol.70 , pp. 1225-1235
    • Monet, M.1
  • 16
    • 84889594608 scopus 로고    scopus 로고
    • TRPV1 structures in distinct conformations reveal activation mechanisms
    • Cao, E., Liao, M., Cheng, Y., & Julius, D. TRPV1 structures in distinct conformations reveal activation mechanisms. Nature 504, 113-118 (2013
    • (2013) Nature , vol.504 , pp. 113-118
    • Cao, E.1    Liao, M.2    Cheng, Y.3    Julius, D.4
  • 17
    • 84889607320 scopus 로고    scopus 로고
    • Structure of the TRPV1 ion channel determined by electron cryo-microscopy
    • Liao, M., Cao, E., Julius, D., & Cheng, Y. Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504, 107-112 (2013
    • (2013) Nature , vol.504 , pp. 107-112
    • Liao, M.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 18
    • 33748748066 scopus 로고    scopus 로고
    • Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel
    • Jin, X., Touhey, J., & Gaudet, R. Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel. J. Biol. Chem. 281, 25006-25010 (2006
    • (2006) J. Biol. Chem , vol.281 , pp. 25006-25010
    • Jin, X.1    Touhey, J.2    Gaudet, R.3
  • 20
    • 84893757446 scopus 로고    scopus 로고
    • Structural insight into the assembly of TRPV channels
    • Huynh, K.W., et al. Structural insight into the assembly of TRPV channels. Structure 22, 260-268 (2014
    • (2014) Structure , vol.22 , pp. 260-268
    • Huynh, K.W.1
  • 21
    • 79960580198 scopus 로고    scopus 로고
    • Modular thermal sensors in temperature-gated transient receptor potential (TRP) channels
    • Yao, J., Liu, B., & Qin, F. Modular thermal sensors in temperature-gated transient receptor potential (TRP) channels. Proc. Natl. Acad. Sci. USA. 108, 11109-11114 (2011
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 11109-11114
    • Yao, J.1    Liu, B.2    Qin, F.3
  • 22
    • 84938524668 scopus 로고    scopus 로고
    • The integrity of the TRP domain is pivotal for correct TRPV1 channel gating
    • Gregorio-Teruel, L., et al. The integrity of the TRP domain is pivotal for correct TRPV1 channel gating. Biophys. J. 109, 529-541 (2015
    • (2015) Biophys. J. , vol.109 , pp. 529-541
    • Gregorio-Teruel, L.1
  • 23
    • 84890343204 scopus 로고    scopus 로고
    • Carboxyl-terminal domain of transient receptor potential vanilloid 1 contains distinct segments differentially involved in capsaicin- and heat-induced desensitization
    • Joseph, J., Wang, S., Lee, J., Ro, J.Y., & Chung, M.K. Carboxyl-terminal domain of transient receptor potential vanilloid 1 contains distinct segments differentially involved in capsaicin- and heat-induced desensitization. J. Biol. Chem. 288, 35690-35702 (2013
    • (2013) J. Biol. Chem , vol.288 , pp. 35690-35702
    • Joseph, J.1    Wang, S.2    Lee, J.3    Ro, J.Y.4    Chung, M.K.5
  • 25
    • 33646899582 scopus 로고    scopus 로고
    • A hot-sensing cold receptor: C-terminal domain determines thermosensation in transient receptor potential channels
    • Brauchi, S., Orta, G., Salazar, M., Rosenmann, E., & Latorre, R. A hot-sensing cold receptor: C-terminal domain determines thermosensation in transient receptor potential channels. J. Neurosci. 26, 4835-4840 (2006
    • (2006) J. Neurosci , vol.26 , pp. 4835-4840
    • Brauchi, S.1    Orta, G.2    Salazar, M.3    Rosenmann, E.4    Latorre, R.5
  • 26
    • 34547200183 scopus 로고    scopus 로고
    • Dissection of the components for PIP2 activation and thermosensation in TRP channels
    • Brauchi, S., et al. Dissection of the components for PIP2 activation and thermosensation in TRP channels. Proc. Natl. Acad. Sci. USA. 104, 10246-10251 (2007
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 10246-10251
    • Brauchi, S.1
  • 27
    • 0030404988 scopus 로고    scopus 로고
    • HOLE: A program for the analysis of the pore dimensions of ion channel structural models
    • Smart, O.S., Neduvelil, J.G., Wang, X., Wallace, B.A., & Sansom, M.S. HOLE: a program for the analysis of the pore dimensions of ion channel structural models. J. Mol. Graph. 14, 354-360, 376 (1996
    • (1996) J. Mol. Graph , vol.14 , pp. 354-376
    • Smart, O.S.1    Neduvelil, J.G.2    Wang, X.3    Wallace, B.A.4    Sansom, M.S.5
  • 28
    • 84892370435 scopus 로고    scopus 로고
    • Structural basis for Ca2+ selectivity of a voltage-gated calcium channel
    • Tang, L., et al. Structural basis for Ca2+ selectivity of a voltage-gated calcium channel. Nature 505, 56-61 (2014
    • (2014) Nature , vol.505 , pp. 56-61
    • Tang, L.1
  • 29
    • 28544453561 scopus 로고    scopus 로고
    • Principles of selective ion transport in channels and pumps
    • Gouaux, E., & Mackinnon, R. Principles of selective ion transport in channels and pumps. Science 310, 1461-1465 (2005
    • (2005) Science , vol.310 , pp. 1461-1465
    • Gouaux, E.1    Mackinnon, R.2
  • 30
    • 78349305451 scopus 로고    scopus 로고
    • Evolutionary origin of a secondary structure: P-helices as cryptic but widespread insertional variations of a-helices that enhance protein functionality
    • Cooley, R.B., Arp, D.J., & Karplus, P.A. Evolutionary origin of a secondary structure: p-helices as cryptic but widespread insertional variations of a-helices that enhance protein functionality. J. Mol. Biol. 404, 232-246 (2010
    • (2010) J. Mol. Biol , vol.404 , pp. 232-246
    • Cooley, R.B.1    Arp, D.J.2    Karplus, P.A.3
  • 31
    • 77952886805 scopus 로고    scopus 로고
    • Temperature-induced opening of TRPV1 ion channel is stabilized by the pore domain
    • Grandl, J., et al. Temperature-induced opening of TRPV1 ion channel is stabilized by the pore domain. Nat. Neurosci. 13, 708-714 (2010
    • (2010) Nat. Neurosci , vol.13 , pp. 708-714
    • Grandl, J.1
  • 32
    • 0034608878 scopus 로고    scopus 로고
    • Acid potentiation of the capsaicin receptor determined by a key extracellular site
    • Jordt, S.E., Tominaga, M., & Julius, D. Acid potentiation of the capsaicin receptor determined by a key extracellular site. Proc. Natl. Acad. Sci. USA. 97, 8134-8139 (2000
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8134-8139
    • Jordt, S.E.1    Tominaga, M.2    Julius, D.3
  • 33
    • 84861217903 scopus 로고    scopus 로고
    • Selective disruption of high sensitivity heat activation but not capsaicin activation of TRPV1 channels by pore turret mutations
    • Cui, Y., et al. Selective disruption of high sensitivity heat activation but not capsaicin activation of TRPV1 channels by pore turret mutations. J. Gen. Physiol. 139, 273-283 (2012
    • (2012) J. Gen. Physiol , vol.139 , pp. 273-283
    • Cui, Y.1
  • 34
    • 36348944117 scopus 로고    scopus 로고
    • Uncoupling proton activation of vanilloid receptor TRPV1
    • Ryu, S., Liu, B., Yao, J., Fu, Q., & Qin, F. Uncoupling proton activation of vanilloid receptor TRPV1. J. Neurosci. 27, 12797-12807 (2007
    • (2007) J. Neurosci , vol.27 , pp. 12797-12807
    • Ryu, S.1    Liu, B.2    Yao, J.3    Fu, Q.4    Qin, F.5
  • 35
    • 84931562454 scopus 로고    scopus 로고
    • Structural mechanism underlying capsaicin binding and activation of the TRPV1 ion channel
    • Yang, F., et al. Structural mechanism underlying capsaicin binding and activation of the TRPV1 ion channel. Nat. Chem. Biol. 11, 518-524 (2015
    • (2015) Nat. Chem. Biol , vol.11 , pp. 518-524
    • Yang, F.1
  • 36
    • 0036183319 scopus 로고    scopus 로고
    • Molecular basis for species-specific sensitivity to "hot chili peppers
    • Jordt, S.E., & Julius, D. Molecular basis for species-specific sensitivity to "hot chili peppers. Cell 108, 421-430 (2002
    • (2002) Cell , vol.108 , pp. 421-430
    • Jordt, S.E.1    Julius, D.2
  • 37
    • 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
  • 38
    • 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
  • 39
    • 34250190946 scopus 로고    scopus 로고
    • The ankyrin repeats of TRPV1 bind multiple ligands and modulate channel sensitivity
    • Lishko, P.V., Procko, E., Jin, X., Phelps, C.B., & Gaudet, R. The ankyrin repeats of TRPV1 bind multiple ligands and modulate channel sensitivity. Neuron 54, 905-918 (2007
    • (2007) Neuron , vol.54 , pp. 905-918
    • Lishko, P.V.1    Procko, E.2    Jin, X.3    Phelps, C.B.4    Gaudet, R.5
  • 40
    • 77957726026 scopus 로고    scopus 로고
    • Ca2+-dependent desensitization of TRPV2 channels is mediated by hydrolysis of phosphatidylinositol 4,5-bisphosphate
    • Mercado, J., Gordon-Shaag, A., Zagotta, W.N., & Gordon, S.E. Ca2+-dependent desensitization of TRPV2 channels is mediated by hydrolysis of phosphatidylinositol 4,5-bisphosphate. J. Neurosci. 30, 13338-13347 (2010
    • (2010) J. Neurosci , vol.30 , pp. 13338-13347
    • Mercado, J.1    Gordon-Shaag, A.2    Zagotta, W.N.3    Gordon, S.E.4
  • 41
    • 20544468931 scopus 로고    scopus 로고
    • Automated molecular microscopy: The new Leginon system
    • Suloway, C., et al. Automated molecular microscopy: the new Leginon system. J. Struct. Biol. 151, 41-60 (2005
    • (2005) J. Struct. Biol , vol.151 , pp. 41-60
    • Suloway, C.1
  • 42
    • 60649103238 scopus 로고    scopus 로고
    • Appion: An integrated, database-driven pipeline to facilitate em image processing
    • Lander, G.C., et al. Appion: an integrated, database-driven pipeline to facilitate EM image processing. J. Struct. Biol. 166, 95-102 (2009
    • (2009) J. Struct. Biol , vol.166 , pp. 95-102
    • Lander, G.C.1
  • 43
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell, J.A., & Grigorieff, N. Accurate determination of local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142, 334-347 (2003
    • (2003) J. Struct. Biol , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 44
    • 63649113687 scopus 로고    scopus 로고
    • DoG Picker and TiltPicker: Software tools to facilitate particle selection in single particle electron microscopy
    • Voss, N.R., Yoshioka, C.K., Radermacher, M., Potter, C.S., & Carragher, B. DoG Picker and TiltPicker: software tools to facilitate particle selection in single particle electron microscopy. J. Struct. Biol. 166, 205-213 (2009
    • (2009) J. Struct. Biol , vol.166 , pp. 205-213
    • Voss, N.R.1    Yoshioka, C.K.2    Radermacher, M.3    Potter, C.S.4    Carragher, B.5
  • 45
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke, S.J., Baldwin, P.R., & Chiu, W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128, 82-97 (1999
    • (1999) J. Struct. Biol , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 46
    • 0142059303 scopus 로고    scopus 로고
    • Topology representing network enables highly accurate classification of protein images taken by cryo electron-microscope without masking
    • Ogura, T., Iwasaki, K., & Sato, C. Topology representing network enables highly accurate classification of protein images taken by cryo electron-microscope without masking. J. Struct. Biol. 143, 185-200 (2003
    • (2003) J. Struct. Biol , vol.143 , pp. 185-200
    • Ogura, T.1    Iwasaki, K.2    Sato, C.3
  • 47
    • 84868444740 scopus 로고    scopus 로고
    • Relion: Implementation of a Bayesian approach to cryo-em structure determination
    • Scheres, S.H. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519-530 (2012
    • (2012) J. Struct. Biol , vol.180 , pp. 519-530
    • Scheres, S.H.1
  • 48
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM.
    • Li, X., et al. Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nat. Methods 10, 584-590 (2013
    • (2013) Nat. Methods , vol.10 , pp. 584-590
    • Li, X.1
  • 49
    • 0346816491 scopus 로고    scopus 로고
    • Find EM: A fast, efficient program for automatic selection of particles from electron micrographs
    • Roseman, A.M. FindEM: a fast, efficient program for automatic selection of particles from electron micrographs. J. Struct. Biol. 145, 91-99 (2004
    • (2004) J. Struct. Biol , vol.145 , pp. 91-99
    • Roseman, A.M.1
  • 50
    • 84920942671 scopus 로고    scopus 로고
    • Beam-induced motion correction for sub-megadalton cryo-EM particles
    • Scheres, S.H. Beam-induced motion correction for sub-megadalton cryo-EM particles. eLife 3, e03665 (2014
    • (2014) ELife , vol.3 , pp. e03665
    • Scheres, S.H.1
  • 51
    • 33845336533 scopus 로고    scopus 로고
    • Bsoft: Image processing and molecular modeling for electron microscopy
    • Heymann, J.B., & Belnap, D.M. Bsoft: image processing and molecular modeling for electron microscopy. J. Struct. Biol. 157, 3-18 (2007
    • (2007) J. Struct. Biol , vol.157 , pp. 3-18
    • Heymann, J.B.1    Belnap, D.M.2
  • 52
  • 53
    • 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 Biol. Crystallogr. 66, 213-221 (2010
    • (2010) Acta Crystallogr. D Biol. Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 54
    • 84921777915 scopus 로고    scopus 로고
    • Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions
    • Brown, A., et al. Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions. Acta Crystallogr. D Biol. Crystallogr. 71, 136-153 (2015
    • (2015) Acta Crystallogr. D Biol. Crystallogr , vol.71 , pp. 136-153
    • Brown, A.1
  • 55
    • 84900435661 scopus 로고    scopus 로고
    • Initiation of translation by cricket paralysis virus IRES requires its translocation in the ribosome
    • Fernández, I.S., Bai, X.C., Murshudov, G., Scheres, S.H., & Ramakrishnan, V. Initiation of translation by cricket paralysis virus IRES requires its translocation in the ribosome. Cell 157, 823-831 (2014
    • (2014) Cell , vol.157 , pp. 823-831
    • Fernández, I.S.1    Bai, X.C.2    Murshudov, G.3    Scheres, S.H.4    Ramakrishnan, V.5
  • 56
    • 18344386202 scopus 로고    scopus 로고
    • A TRP channel that senses cold stimuli and menthol
    • Peier, A.M., et al. A TRP channel that senses cold stimuli and menthol. Cell 108, 705-715 (2002
    • (2002) Cell , vol.108 , pp. 705-715
    • Peier, A.M.1


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