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Volumn 550, Issue 7676, 2017, Pages

Cryo-electron microscopy structure of the lysosomal calcium-permeable channel TRPML3

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM CHANNEL; CALCIUM ION; LYSOSOMAL CALCIUM PERMEABLE CHANNEL TRPML3; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL 3,5 BISPHOSPHATE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; UNCLASSIFIED DRUG; PHOSPHATIDYLINOSITOL 3,5-DIPHOSPHATE; POLYPHOSPHOINOSITIDE; TRANSIENT RECEPTOR POTENTIAL CHANNEL;

EID: 85032875994     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature24055     Document Type: Article
Times cited : (94)

References (52)
  • 3
    • 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
  • 4
    • 0033822172 scopus 로고    scopus 로고
    • Identification of the gene causing mucolipidosis type IV
    • Bargal, R., et al. Identification of the gene causing mucolipidosis type IV. Nat. Genet. 26, 118-123 (2000).
    • (2000) Nat. Genet. , vol.26 , pp. 118-123
    • Bargal, R.1
  • 5
    • 0037069373 scopus 로고    scopus 로고
    • Mutations in Mcoln3 associated with deafness and pigmentation defects in varitint-waddler (Va) mice
    • Di Palma, F., et al. Mutations in Mcoln3 associated with deafness and pigmentation defects in varitint-waddler (Va) mice. Proc. Natl Acad. Sci. USA 99, 14994-14999 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 14994-14999
    • Di Palma, F.1
  • 6
    • 36749008553 scopus 로고    scopus 로고
    • Activating mutation in a mucolipin transient receptor potential channel leads to melanocyte loss in varitint-waddler mice
    • Xu, H., Delling, M., Li, L., Dong, X. & Clapham, D. E. Activating mutation in a mucolipin transient receptor potential channel leads to melanocyte loss in varitint-waddler mice. Proc. Natl Acad. Sci. USA 104, 18321-18326 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 18321-18326
    • Xu, H.1    Delling, M.2    Li, L.3    Dong, X.4    Clapham, D.E.5
  • 7
    • 80051473235 scopus 로고    scopus 로고
    • PI(3, 5)P2 controls membrane trafficking by direct activation of mucolipin Ca2+ release channels in the endolysosome
    • Dong, X. P., et al. PI(3, 5)P2 controls membrane trafficking by direct activation of mucolipin Ca2+ release channels in the endolysosome. Nat. Commun. 1, 38 (2010).
    • (2010) Nat. Commun. , vol.1 , pp. 38
    • Dong, X.P.1
  • 8
    • 84863922724 scopus 로고    scopus 로고
    • Phosphoinositide isoforms determine compartmentspecific ion channel activity
    • Zhang, X., Li, X. & Xu, H. Phosphoinositide isoforms determine compartmentspecific ion channel activity. Proc. Natl Acad. Sci. USA 109, 11384-11389 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 11384-11389
    • Zhang, X.1    Li, X.2    Xu, H.3
  • 9
    • 42449103570 scopus 로고    scopus 로고
    • A novel mode of TRPML3 regulation by extracytosolic pH absent in the varitint-waddler phenotype
    • Kim, H. J., et al. A novel mode of TRPML3 regulation by extracytosolic pH absent in the varitint-waddler phenotype. EMBO J. 27, 1197-1205 (2008).
    • (2008) EMBO J. , vol.27 , pp. 1197-1205
    • Kim, H.J.1
  • 10
    • 37549009562 scopus 로고    scopus 로고
    • Gain-of-function mutation in TRPML3 causes the mouse Varitint-Waddler phenotype
    • Kim, H. J., et al. Gain-of-function mutation in TRPML3 causes the mouse Varitint-Waddler phenotype. J. Biol. Chem. 282, 36138-36142 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 36138-36142
    • Kim, H.J.1
  • 11
    • 77049105199 scopus 로고    scopus 로고
    • Small molecule activators of TRPML3
    • Grimm, C., et al. Small molecule activators of TRPML3. Chem. Biol. 17, 135-148 (2010).
    • (2010) Chem. Biol. , vol.17 , pp. 135-148
    • Grimm, C.1
  • 12
    • 85009831976 scopus 로고    scopus 로고
    • Molecular insights into lipid-assisted Ca2+ regulation of the TRP channel Polycystin-2
    • Wilkes, M., et al. Molecular insights into lipid-assisted Ca2+ regulation of the TRP channel Polycystin-2. Nat. Struct. Mol. Biol. 24, 123-130 (2017).
    • (2017) Nat. Struct. Mol. Biol. , vol.24 , pp. 123-130
    • Wilkes, M.1
  • 13
    • 84992597299 scopus 로고    scopus 로고
    • The structure of the polycystic kidney disease channel PKD2 in lipid nanodiscs
    • Shen, P. S., et al. The structure of the polycystic kidney disease channel PKD2 in lipid nanodiscs. Cell 167, 763-773 (2016).
    • (2016) Cell , vol.167 , pp. 763-773
    • Shen, P.S.1
  • 14
    • 84969627248 scopus 로고    scopus 로고
    • TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action
    • Gao, Y., Cao, E., Julius, D. & Cheng, Y. TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action. Nature 534, 347-351 (2016).
    • (2016) Nature , vol.534 , pp. 347-351
    • Gao, Y.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 15
    • 85010872102 scopus 로고    scopus 로고
    • Structural basis of dual Ca2+/pH regulation of the endolysosomal TRPML1 channel
    • Li, M., et al. Structural basis of dual Ca2+/pH regulation of the endolysosomal TRPML1 channel. Nat. Struct. Mol. Biol. 24, 205-213 (2017).
    • (2017) Nat. Struct. Mol. Biol. , vol.24 , pp. 205-213
    • Li, M.1
  • 16
    • 85006515501 scopus 로고    scopus 로고
    • Structure of the polycystic kidney disease TRP channel Polycystin-2 (PC2)
    • Grieben, M., et al. Structure of the polycystic kidney disease TRP channel Polycystin-2 (PC2). Nat. Struct. Mol. Biol. 24, 114-122 (2017).
    • (2017) Nat. Struct. Mol. Biol. , vol.24 , pp. 114-122
    • Grieben, M.1
  • 17
    • 84928474213 scopus 로고    scopus 로고
    • Structure of the TRPA1 ion channel suggests regulatory mechanisms
    • Paulsen, C. E., Armache, J. P., Gao, Y., Cheng, Y. & Julius, D. Structure of the TRPA1 ion channel suggests regulatory mechanisms. Nature 520, 511-517 (2015).
    • (2015) Nature , vol.520 , pp. 511-517
    • Paulsen, C.E.1    Armache, J.P.2    Gao, Y.3    Cheng, Y.4    Julius, D.5
  • 18
    • 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
  • 19
    • 84956830463 scopus 로고    scopus 로고
    • Cryo-electron microscopy structure of the TRPV2 ion channel
    • Zubcevic, L., et al. Cryo-electron microscopy structure of the TRPV2 ion channel. Nat. Struct. Mol. Biol. 23, 180-186 (2016).
    • (2016) Nat. Struct. Mol. Biol. , vol.23 , pp. 180-186
    • Zubcevic, L.1
  • 20
    • 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
  • 21
    • 84975688014 scopus 로고    scopus 로고
    • Crystal structure of the epithelial calcium channel TRPV6
    • Saotome, K., Singh, A. K., Yelshanskaya, M. V. & Sobolevsky, A. I. Crystal structure of the epithelial calcium channel TRPV6. Nature 534, 506-511 (2016).
    • (2016) Nature , vol.534 , pp. 506-511
    • Saotome, K.1    Singh, A.K.2    Yelshanskaya, M.V.3    Sobolevsky, A.I.4
  • 22
    • 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
  • 23
    • 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
  • 24
    • 84975726435 scopus 로고    scopus 로고
    • Molecular basis of ion permeability in a voltage-gated sodium channel
    • Naylor, C. E., et al. Molecular basis of ion permeability in a voltage-gated sodium channel. EMBO J. 35, 820-830 (2016).
    • (2016) EMBO J. , vol.35 , pp. 820-830
    • Naylor, C.E.1
  • 25
    • 77952765622 scopus 로고    scopus 로고
    • Properties of the TRPML3 channel pore and its stable expansion by the Varitint-Waddler-causing mutation
    • Kim, H. J., Yamaguchi, S., Li, Q., So, I. & Muallem, S. Properties of the TRPML3 channel pore and its stable expansion by the Varitint-Waddler-causing mutation. J. Biol. Chem. 285, 16513-16520 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 16513-16520
    • Kim, H.J.1    Yamaguchi, S.2    Li, Q.3    So, I.4    Muallem, S.5
  • 26
    • 84930541540 scopus 로고    scopus 로고
    • The role of TRPMLs in endolysosomal trafficking and function
    • Venkatachalam, K., Wong, C. O. & Zhu, M. X. The role of TRPMLs in endolysosomal trafficking and function. Cell Calcium 58, 48-56 (2015).
    • (2015) Cell Calcium , vol.58 , pp. 48-56
    • Venkatachalam, K.1    Wong, C.O.2    Zhu, M.X.3
  • 27
    • 84880740812 scopus 로고    scopus 로고
    • A novel mutation in a large family causes a unique phenotype of Mucolipidosis IV
    • AlBakheet, A., et al. A novel mutation in a large family causes a unique phenotype of Mucolipidosis IV. Gene 526, 464-466 (2013).
    • (2013) Gene , vol.526 , pp. 464-466
    • AlBakheet, A.1
  • 28
    • 69249202518 scopus 로고    scopus 로고
    • Mucolipidosis type IV in a Turkish boy associated with a novel MCOLN1 mutation
    • Tuÿsüz, B., Goldin, E., Metin, B., Korkmaz, B. & Yalçinkaya, C. Mucolipidosis type IV in a Turkish boy associated with a novel MCOLN1 mutation. Brain Dev. 31, 702-705 (2009).
    • (2009) Brain Dev. , vol.31 , pp. 702-705
    • Tuÿsüz, B.1    Goldin, E.2    Metin, B.3    Korkmaz, B.4    Yalçinkaya, C.5
  • 29
    • 0034894817 scopus 로고    scopus 로고
    • Mucolipidosis type IV
    • Bach, G. Mucolipidosis type IV. Mol. Genet. Metab. 73, 197-203 (2001).
    • (2001) Mol. Genet. Metab. , vol.73 , pp. 197-203
    • Bach, G.1
  • 30
    • 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
  • 31
    • 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
  • 32
    • 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
  • 33
    • 84946488108 scopus 로고    scopus 로고
    • CTFFIND4: Fast and accurate defocus estimation from electron micrographs
    • Rohou, A. & Grigorieff, N. CTFFIND4: Fast and accurate defocus estimation from electron micrographs. J. Struct. Biol. 192, 216-221 (2015).
    • (2015) J. Struct. Biol. , vol.192 , pp. 216-221
    • Rohou, A.1    Grigorieff, N.2
  • 34
    • 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
  • 35
    • 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
  • 36
    • 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
  • 37
    • 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
  • 38
    • 0346816491 scopus 로고    scopus 로고
    • FindEM-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
  • 39
    • 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
  • 40
    • 84866078359 scopus 로고    scopus 로고
    • Prevention of overfitting in cryo-EM structure determination
    • Scheres, S. H. & Chen, S. Prevention of overfitting in cryo-EM structure determination. Nat. Methods 9, 853-854 (2012).
    • (2012) Nat. Methods , vol.9 , pp. 853-854
    • Scheres, S.H.1    Chen, S.2
  • 41
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal, P. B. & Henderson, R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J. Mol. Biol. 333, 721-745 (2003).
    • (2003) J. Mol. Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 42
    • 85014129582 scopus 로고    scopus 로고
    • MotionCor2: Anisotropic correction of beam-induced motion for improved cryo-electron microscopy
    • Zheng, S. Q., et al. MotionCor2: Anisotropic correction of beam-induced motion for improved cryo-electron microscopy. Nat. Methods 14, 331-332 (2017).
    • (2017) Nat. Methods , vol.14 , pp. 331-332
    • Zheng, S.Q.1
  • 43
    • 85009208040 scopus 로고    scopus 로고
    • Accelerated cryo-EM structure determination with parallelisation using GPUs in RELION-2
    • Kimanius, D., Forsberg, B. O., Scheres, S. H. & Lindahl, E. Accelerated cryo-EM structure determination with parallelisation using GPUs in RELION-2. eLife 5, e18722 (2016).
    • (2016) ELife , vol.5 , pp. e18722
    • Kimanius, D.1    Forsberg, B.O.2    Scheres, S.H.3    Lindahl, E.4
  • 44
    • 84880607763 scopus 로고    scopus 로고
    • High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy
    • Chen, S., et al. High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy. Ultramicroscopy 135, 24-35 (2013).
    • (2013) Ultramicroscopy , vol.135 , pp. 24-35
    • Chen, S.1
  • 45
    • 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
  • 46
    • 33845345287 scopus 로고    scopus 로고
    • Visualizing density maps with UCSF Chimera
    • Goddard, T. D., Huang, C. C. & Ferrin, T. E. Visualizing density maps with UCSF Chimera. J. Struct. Biol. 157, 281-287 (2007).
    • (2007) J. Struct. Biol. , vol.157 , pp. 281-287
    • Goddard, T.D.1    Huang, C.C.2    Ferrin, T.E.3
  • 47
    • 13244281317 scopus 로고    scopus 로고
    • Coot: 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    Cowtan, K.2
  • 48
    • 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
  • 49
    • 0030404988 scopus 로고    scopus 로고
    • HOLE: A program for the analysis of the pore dimensions of ion channel structural models
    • 376
    • 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. 354-360
    • Smart, O.S.1    Neduvelil, J.G.2    Wang, X.3    Wallace, B.A.4    Sansom, M.S.5
  • 50
    • 84908199292 scopus 로고    scopus 로고
    • Screening and large-scale expression of membrane proteins in mammalian cells for structural studies
    • Goehring, A., et al. Screening and large-scale expression of membrane proteins in mammalian cells for structural studies. Nat. Protocols 9, 2574-2585 (2014).
    • (2014) Nat. Protocols , vol.9 , pp. 2574-2585
    • Goehring, A.1
  • 51
    • 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
  • 52
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • Trott, O. & Olson, A. J. AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J. Comput. Chem. 31, 455-461 (2010).
    • (2010) J. Comput. Chem. , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2


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