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Volumn 533, Issue , 2016, Pages 269-273

Architecture of the mitochondrial calcium uniporter

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM CHANNEL; LIGAND GATED ION CHANNEL; MEMBRANE PROTEIN; MITOCHONDRIAL CALCIUM UNIPORTER; MITOCHONDRIAL CALCIUM UNIPORTER 1; MITOCHONDRIAL CALCIUM UNIPORTER 2; NICOTINIC RECEPTOR; UNCLASSIFIED DRUG;

EID: 84969194530     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature17656     Document Type: Article
Times cited : (264)

References (42)
  • 1
    • 0025292743 scopus 로고
    • Mechanisms by which mitochondria transport calcium
    • Gunter, T. E. & Pfeiffer, D. R. Mechanisms by which mitochondria transport calcium. Am. J. Physiol. 258, C755-C786 (1990).
    • (1990) Am. J. Physiol. , vol.258 , pp. 755-786
    • Gunter, T.E.1    Pfeiffer, D.R.2
  • 2
    • 1642540210 scopus 로고    scopus 로고
    • The mitochondrial calcium uniporter is a highly selective ion channel
    • Kirichok, Y., Krapivinsky, G. & Clapham, D. E. The mitochondrial calcium uniporter is a highly selective ion channel. Nature 427, 360-364 (2004).
    • (2004) Nature , vol.427 , pp. 360-364
    • Kirichok, Y.1    Krapivinsky, G.2    Clapham, D.E.3
  • 3
    • 0019025638 scopus 로고
    • The role of calcium in the regulation of mitochondrial metabolism
    • Denton, R. M. & McCormack, J. G. The role of calcium in the regulation of mitochondrial metabolism. Biochem. Soc. Trans. 8, 266-268 (1980).
    • (1980) Biochem. Soc. Trans. , vol.8 , pp. 266-268
    • Denton, R.M.1    McCormack, J.G.2
  • 4
    • 80051946060 scopus 로고    scopus 로고
    • Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter
    • Baughman, J. M. et al. Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter. Nature 476, 341-345 (2011).
    • (2011) Nature , vol.476 , pp. 341-345
    • Baughman, J.M.1
  • 5
    • 77956928316 scopus 로고    scopus 로고
    • MICU1 encodes a mitochondrial EF hand protein required for Ca2+ uptake
    • Perocchi, F. et al. MICU1 encodes a mitochondrial EF hand protein required for Ca2+ uptake. Nature 467, 291-296 (2010).
    • (2010) Nature , vol.467 , pp. 291-296
    • Perocchi, F.1
  • 6
    • 80051936634 scopus 로고    scopus 로고
    • A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter
    • De Stefani, D., Raffaello, A., Teardo, E., Szabo, I. & Rizzuto, R. A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter. Nature 476, 336-340 (2011).
    • (2011) Nature , vol.476 , pp. 336-340
    • De Stefani, D.1    Raffaello, A.2    Teardo, E.3    Szabo, I.4    Rizzuto, R.5
  • 7
    • 84890116192 scopus 로고    scopus 로고
    • EMRE is an essential component of the mitochondrial calcium uniporter complex
    • Sancak, Y. et al. EMRE is an essential component of the mitochondrial calcium uniporter complex. Science 342, 1379-1382 (2013).
    • (2013) Science , vol.342 , pp. 1379-1382
    • Sancak, Y.1
  • 8
    • 84883286784 scopus 로고    scopus 로고
    • The mitochondrial calcium uniporter is a multimer that can include a dominant-negative pore-forming subunit
    • Raffaello, A. et al. The mitochondrial calcium uniporter is a multimer that can include a dominant-negative pore-forming subunit. EMBO J. 32, 2362-2376 (2013).
    • (2013) EMBO J. , vol.32 , pp. 2362-2376
    • Raffaello, A.1
  • 9
    • 84940438466 scopus 로고    scopus 로고
    • The molecular era of the mitochondrial calcium uniporter
    • Kamer, K. J. & Mootha, V. K. The molecular era of the mitochondrial calcium uniporter. Nature Rev. Mol. Cell Biol. 16, 545-553 (2015).
    • (2015) Nature Rev. Mol. Cell Biol. , vol.16 , pp. 545-553
    • Kamer, K.J.1    Mootha, V.K.2
  • 10
    • 84879052051 scopus 로고    scopus 로고
    • MCU encodes the pore conducting mitochondrial calcium currents
    • Chaudhuri, D., Sancak, Y., Mootha, V. K. & Clapham, D. E. MCU encodes the pore conducting mitochondrial calcium currents. eLife 2, e00704 (2013).
    • (2013) ELife , vol.2 , pp. e00704
    • Chaudhuri, D.1    Sancak, Y.2    Mootha, V.K.3    Clapham, D.E.4
  • 11
    • 84902579068 scopus 로고    scopus 로고
    • Reconstitution of the mitochondrial calcium uniporter in yeast
    • Kovács-Bogdán, E. et al. Reconstitution of the mitochondrial calcium uniporter in yeast. Proc. Natl Acad. Sci. USA 111, 8985-8990 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 8985-8990
    • Kovács-Bogdán, E.1
  • 12
    • 84942776229 scopus 로고    scopus 로고
    • Structure and function of the N-terminal domain of the human mitochondrial calcium uniporter
    • Lee, Y. et al. Structure and function of the N-terminal domain of the human mitochondrial calcium uniporter. EMBO Rep. (2015).
    • (2015) EMBO Rep.
    • Lee, Y.1
  • 13
    • 67649908268 scopus 로고    scopus 로고
    • Solution nuclear magnetic resonance structure of membrane-integral diacylglycerol kinase
    • Van Horn, W. D. et al. Solution nuclear magnetic resonance structure of membrane-integral diacylglycerol kinase. Science 324, 1726-1729 (2009).
    • (2009) Science , vol.324 , pp. 1726-1729
    • Van Horn, W.D.1
  • 14
    • 38749106195 scopus 로고    scopus 로고
    • Structure and mechanism of the M2 proton channel of influenza A virus
    • Schnell, J. R. & Chou, J. J. Structure and mechanism of the M2 proton channel of influenza A virus. Nature 451, 591-595 (2008).
    • (2008) Nature , vol.451 , pp. 591-595
    • Schnell, J.R.1    Chou, J.J.2
  • 15
    • 84879695534 scopus 로고    scopus 로고
    • Unusual architecture of the p7 channel from hepatitis C virus
    • OuYang, B. et al. Unusual architecture of the p7 channel from hepatitis C virus. Nature 498, 521-525 (2013).
    • (2013) Nature , vol.498 , pp. 521-525
    • OuYang, B.1
  • 16
    • 29444439322 scopus 로고    scopus 로고
    • Single particle reconstructions of the transferrin-transferrin receptor complex obtained with different specimen preparation techniques
    • Cheng, Y. et al. Single particle reconstructions of the transferrin-transferrin receptor complex obtained with different specimen preparation techniques. J. Mol. Biol. 355, 1048-1065 (2006).
    • (2006) J. Mol. Biol. , vol.355 , pp. 1048-1065
    • Cheng, Y.1
  • 17
    • 84868515149 scopus 로고    scopus 로고
    • Structural insights into the mechanisms of Mg2+ uptake, transport, and gating by CorA
    • Guskov, A. et al. Structural insights into the mechanisms of Mg2+ uptake, transport, and gating by CorA. Proc. Natl Acad. Sci. USA 109, 18459-18464 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 18459-18464
    • Guskov, A.1
  • 18
    • 84869223151 scopus 로고    scopus 로고
    • Structural asymmetry in the magnesium channel CorA points to sequential allosteric regulation
    • Pfoh, R. et al. Structural asymmetry in the magnesium channel CorA points to sequential allosteric regulation. Proc. Natl Acad. Sci. USA 109, 18809-18814 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 18809-18814
    • Pfoh, R.1
  • 19
    • 33746549925 scopus 로고    scopus 로고
    • Crystal structure of a divalent metal ion transporter CorA at 2.9 angstrom resolution
    • Eshaghi, S. et al. Crystal structure of a divalent metal ion transporter CorA at 2.9 angstrom resolution. Science 313, 354-357 (2006).
    • (2006) Science , vol.313 , pp. 354-357
    • Eshaghi, S.1
  • 20
    • 33645748904 scopus 로고    scopus 로고
    • Crystal structure of the CorA Mg2+ transporter
    • Lunin, V. V. et al. Crystal structure of the CorA Mg2+ transporter. Nature 440, 833-837 (2006).
    • (2006) Nature , vol.440 , pp. 833-837
    • Lunin, V.V.1
  • 21
    • 84870655957 scopus 로고    scopus 로고
    • Crystal structure of the calcium release-activated calcium channel Orai
    • Hou, X., Pedi, L., Diver, M. M. & Long, S. B. Crystal structure of the calcium release-activated calcium channel Orai. Science 338, 1308-1313 (2012).
    • (2012) Science , vol.338 , pp. 1308-1313
    • Hou, X.1    Pedi, L.2    Diver, M.M.3    Long, S.B.4
  • 22
    • 84861219896 scopus 로고    scopus 로고
    • Evolutionary diversity of the mitochondrial calcium uniporter
    • Bick, A. G., Calvo, S. E. & Mootha, V. K. Evolutionary diversity of the mitochondrial calcium uniporter. Science 336, 886 (2012).
    • (2012) Science , vol.336 , pp. 886
    • Bick, A.G.1    Calvo, S.E.2    Mootha, V.K.3
  • 23
    • 84906545550 scopus 로고    scopus 로고
    • X-ray structure of the mouse serotonin 5-HT3 receptor
    • Hassaine, G. et al. X-ray structure of the mouse serotonin 5-HT3 receptor. Nature 512, 276-281 (2014).
    • (2014) Nature , vol.512 , pp. 276-281
    • Hassaine, G.1
  • 24
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4 Å resolution
    • Unwin, N. Refined structure of the nicotinic acetylcholine receptor at 4 Å resolution. J. Mol. Biol. 346, 967-989 (2005).
    • (2005) J. Mol. Biol. , vol.346 , pp. 967-989
    • Unwin, N.1
  • 25
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas, A., Van Dyke, M. & Stock, J. Predicting coiled coils from protein sequences. Science 252, 1162-1164 (1991).
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 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 (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
  • 28
    • 55649088213 scopus 로고    scopus 로고
    • Static light scattering to characterize membrane proteins in detergent solution
    • Slotboom, D. J., Duurkens, R. H., Olieman, K. & Erkens, G. B. Static light scattering to characterize membrane proteins in detergent solution. Methods 46, 73-82 (2008).
    • (2008) Methods , vol.46 , pp. 73-82
    • Slotboom, D.J.1    Duurkens, R.H.2    Olieman, K.3    Erkens, G.B.4
  • 29
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • Tang, G. et al. EMAN2: An extensible image processing suite for electron microscopy. J. Struct. Biol. 157, 38-46 (2007).
    • (2007) J. Struct. Biol. , vol.157 , pp. 38-46
    • Tang, G.1
  • 30
    • 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
  • 31
    • 84925511390 scopus 로고    scopus 로고
    • Structural insight into autoinhibition and histone H3-induced activation of DNMT3A
    • Guo, X. et al. Structural insight into autoinhibition and histone H3-induced activation of DNMT3A. Nature 517, 640-644 (2015).
    • (2015) Nature , vol.517 , pp. 640-644
    • Guo, X.1
  • 32
    • 0344552370 scopus 로고    scopus 로고
    • 2D fast rotational matching for image processing of biophysical data
    • Cong, Y., Kovacs, J. A. & Wriggers, W. 2D fast rotational matching for image processing of biophysical data. J. Struct. Biol. 144, 51-60 (2003).
    • (2003) J. Struct. Biol. , vol.144 , pp. 51-60
    • Cong, Y.1    Kovacs, J.A.2    Wriggers, W.3
  • 33
    • 27744506655 scopus 로고    scopus 로고
    • Fast rotational matching of single-particle images
    • Cong, Y. et al. Fast rotational matching of single-particle images. J. Struct. Biol. 152, 104-112 (2005).
    • (2005) J. Struct. Biol. , vol.152 , pp. 104-112
    • Cong, Y.1
  • 34
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F. et al. NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293 (1995).
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1
  • 35
    • 19444382397 scopus 로고    scopus 로고
    • The CCPN data model for NMR spectroscopy: Development of a software pipeline
    • Vranken, W. F. et al. The CCPN data model for NMR spectroscopy: Development of a software pipeline. Proteins 59, 687-696 (2005).
    • (2005) Proteins , vol.59 , pp. 687-696
    • Vranken, W.F.1
  • 36
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels, C., Xia, T. H., Billeter, M., Guntert, P. & Wuthrich, K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR 6, 1-10 (1995).
    • (1995) J. Biomol. NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.H.2    Billeter, M.3    Guntert, P.4    Wuthrich, K.5
  • 37
    • 84859396347 scopus 로고
    • Three-dimensional triple resonance NMR spectroscopy of isotopically enriched proteins
    • Kay, L. E., Ikura, M., Tschudin, R. & Bax, A. Three-dimensional triple resonance NMR spectroscopy of isotopically enriched proteins. J. Magn. Reson. 213, 423-441 (1990).
    • (1990) J. Magn. Reson. , vol.213 , pp. 423-441
    • Kay, L.E.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 38
    • 0032695328 scopus 로고    scopus 로고
    • Improved sensitivity and coherence selection for [15N1H]-TROSY elements in triple resonance experiments
    • Salzmann, M., Wider, G., Pervushin, K. & Wuthrich, K. Improved sensitivity and coherence selection for [15N,1H]-TROSY elements in triple resonance experiments. J. Biomol. NMR 15, 181-184 (1999).
    • (1999) J. Biomol. NMR , vol.15 , pp. 181-184
    • Salzmann, M.1    Wider, G.2    Pervushin, K.3    Wuthrich, K.4
  • 39
    • 0026889426 scopus 로고
    • Support of 1H NMR assignments in proteins by biosynthetically directed fractional 13C-labeling
    • Szyperski, T., Neri, D., Leiting, B., Otting, G. & Wuthrich, K. Support of 1H NMR assignments in proteins by biosynthetically directed fractional 13C-labeling. J. Biomol. NMR 2, 323-334 (1992).
    • (1992) J. Biomol. NMR , vol.2 , pp. 323-334
    • Szyperski, T.1    Neri, D.2    Leiting, B.3    Otting, G.4    Wuthrich, K.5
  • 41
    • 68349093958 scopus 로고    scopus 로고
    • TALOS+a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Shen, Y., Delaglio, F., Cornilescu, G. & Bax, A. TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J. Biomol. NMR 44, 213-223 (2009).
    • (2009) J. Biomol. NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 42
    • 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. W. 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.W.4


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