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Volumn 112, Issue 1, 2015, Pages 130-135

Superresolution microscopy reveals spatial separation of UCP4 and F0F1-ATP synthase in neuronal mitochondria

Author keywords

Direct stochastic optical reconstruction microscopy; Mitochondrial membrane proteins; Proton diffusion; Reactive oxygen species; Uncoupling

Indexed keywords

MITOCHONDRIAL PROTEIN; PROTON; PROTON PUMP; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG; UNCOUPLING PROTEIN; UNCOUPLING PROTEIN 4; VOLTAGE DEPENDENT ANION CHANNEL; CARRIER PROTEIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; UCP4 PROTEIN, MOUSE;

EID: 84920494257     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1415261112     Document Type: Article
Times cited : (51)

References (48)
  • 1
    • 84858376953 scopus 로고    scopus 로고
    • Mitochondria: In sickness and in health
    • Nunnari J, Suomalainen A (2012) Mitochondria: In sickness and in health. Cell 148(6):1145-1159.
    • (2012) Cell , vol.148 , Issue.6 , pp. 1145-1159
    • Nunnari, J.1    Suomalainen, A.2
  • 2
    • 84863738048 scopus 로고    scopus 로고
    • Molecular mechanisms of superoxide production by the mitochondrial respiratory chain
    • Dröse S, Brandt U (2012) Molecular mechanisms of superoxide production by the mitochondrial respiratory chain. Adv Exp Med Biol 748:145-169.
    • (2012) Adv Exp Med Biol , vol.748 , pp. 145-169
    • Dröse, S.1    Brandt, U.2
  • 3
    • 33845927357 scopus 로고    scopus 로고
    • Mitochondrial trafficking and morphology in healthy and injured neurons
    • Chang DTW, Reynolds IJ (2006) Mitochondrial trafficking and morphology in healthy and injured neurons. Prog Neurobiol 80(5):241-268.
    • (2006) Prog Neurobiol , vol.80 , Issue.5 , pp. 241-268
    • Chang, D.T.W.1    Reynolds, I.J.2
  • 4
    • 84862599292 scopus 로고    scopus 로고
    • SnapShot: Mitochondrial architecture
    • Neupert W (2012) SnapShot: Mitochondrial architecture. Cell 149(3):722-722.e1.
    • (2012) Cell , vol.149 , Issue.3 , pp. 722-722.e1
    • Neupert, W.1
  • 5
    • 84878703165 scopus 로고    scopus 로고
    • The connection between inner membrane topology and mitochondrial function
    • Mannella CA, Lederer WJ, Jafri MS (2013) The connection between inner membrane topology and mitochondrial function. J Mol Cell Cardiol 62:51-57.
    • (2013) J Mol Cell Cardiol , vol.62 , pp. 51-57
    • Mannella, C.A.1    Lederer, W.J.2    Jafri, M.S.3
  • 6
    • 0032998265 scopus 로고    scopus 로고
    • UCP4, a novel brain-specific mitochondrial protein that reduces membrane potential in mammalian cells
    • Mao W, et al. (1999) UCP4, a novel brain-specific mitochondrial protein that reduces membrane potential in mammalian cells. FEBS Lett 443(3):326-330.
    • (1999) FEBS Lett , vol.443 , Issue.3 , pp. 326-330
    • Mao, W.1
  • 7
    • 33745230018 scopus 로고    scopus 로고
    • Mitochondrial UCP4 mediates an adaptive shift in energy metabolism and increases the resistance of neurons to metabolic and oxidative stress
    • Liu D, et al. (2006) Mitochondrial UCP4 mediates an adaptive shift in energy metabolism and increases the resistance of neurons to metabolic and oxidative stress. Neuromolecular Med 8(3):389-414.
    • (2006) Neuromolecular Med , vol.8 , Issue.3 , pp. 389-414
    • Liu, D.1
  • 8
    • 70349487372 scopus 로고    scopus 로고
    • Comparative analysis of uncoupling protein 4 distribution in various tissues under physiological conditions and during development
    • Smorodchenko A, et al. (2009) Comparative analysis of uncoupling protein 4 distribution in various tissues under physiological conditions and during development. Biochim Biophys Acta 1788(10):2309-2319.
    • (2009) Biochim Biophys Acta , vol.1788 , Issue.10 , pp. 2309-2319
    • Smorodchenko, A.1
  • 10
    • 14644439938 scopus 로고    scopus 로고
    • The mitochondrial uncoupling-protein homologues
    • Krauss S, Zhang CY, Lowell BB (2005) The mitochondrial uncoupling-protein homologues. Nat Rev Mol Cell Biol 6(3):248-261.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , Issue.3 , pp. 248-261
    • Krauss, S.1    Zhang, C.Y.2    Lowell, B.B.3
  • 11
    • 84879358003 scopus 로고    scopus 로고
    • Human neuronal uncoupling proteins 4 and 5 (UCP4 and UCP5): Structural properties, regulation, and physiological role in protection against oxidative stress and mitochondrial dysfunction
    • Ramsden DB, et al. (2012) Human neuronal uncoupling proteins 4 and 5 (UCP4 and UCP5): Structural properties, regulation, and physiological role in protection against oxidative stress and mitochondrial dysfunction. Brain Behav 2(4):468-478.
    • (2012) Brain Behav , vol.2 , Issue.4 , pp. 468-478
    • Ramsden, D.B.1
  • 12
    • 84861134135 scopus 로고    scopus 로고
    • Toward understanding the mechanism of ion transport activity of neuronal uncoupling proteins UCP2, UCP4, and UCP5
    • Hoang T, Smith MD, Jelokhani-Niaraki M (2012) Toward understanding the mechanism of ion transport activity of neuronal uncoupling proteins UCP2, UCP4, and UCP5. Biochemistry 51(19):4004-4014.
    • (2012) Biochemistry , vol.51 , Issue.19 , pp. 4004-4014
    • Hoang, T.1    Smith, M.D.2    Jelokhani-Niaraki, M.3
  • 13
    • 0033971898 scopus 로고    scopus 로고
    • Mitochondria and neuronal survival
    • Nicholls DG, Budd SL (2000) Mitochondria and neuronal survival. Physiol Rev 80(1):315-360.
    • (2000) Physiol Rev , vol.80 , Issue.1 , pp. 315-360
    • Nicholls, D.G.1    Budd, S.L.2
  • 14
    • 33750305666 scopus 로고    scopus 로고
    • Dynamic subcompartmentalization of the mitochondrial inner membrane
    • Vogel F, Bornhövd C, Neupert W, Reichert AS (2006) Dynamic subcompartmentalization of the mitochondrial inner membrane. J Cell Biol 175(2):237-247.
    • (2006) J Cell Biol , vol.175 , Issue.2 , pp. 237-247
    • Vogel, F.1    Bornhövd, C.2    Neupert, W.3    Reichert, A.S.4
  • 15
    • 33749352547 scopus 로고    scopus 로고
    • Differential protein distributions define two sub-compartments of the mitochondrial inner membrane in yeast
    • Wurm CA, Jakobs S (2006) Differential protein distributions define two sub-compartments of the mitochondrial inner membrane in yeast. FEBS Lett 580(24):5628-5634.
    • (2006) FEBS Lett , vol.580 , Issue.24 , pp. 5628-5634
    • Wurm, C.A.1    Jakobs, S.2
  • 16
    • 61949403154 scopus 로고    scopus 로고
    • The m-AAA protease processes cytochrome c peroxidase preferentially at the inner boundary membrane of mitochondria
    • Suppanz IE, Wurm CA, Wenzel D, Jakobs S (2009) The m-AAA protease processes cytochrome c peroxidase preferentially at the inner boundary membrane of mitochondria. Mol Biol Cell 20(2):572-580.
    • (2009) Mol Biol Cell , vol.20 , Issue.2 , pp. 572-580
    • Suppanz, I.E.1    Wurm, C.A.2    Wenzel, D.3    Jakobs, S.4
  • 17
    • 84862527999 scopus 로고    scopus 로고
    • The inner-mitochondrial distribution of Oxa1 depends on the growth conditions and on the availability of substrates
    • Stoldt S, et al. (2012) The inner-mitochondrial distribution of Oxa1 depends on the growth conditions and on the availability of substrates. Mol Biol Cell 23(12):2292-2301.
    • (2012) Mol Biol Cell , vol.23 , Issue.12 , pp. 2292-2301
    • Stoldt, S.1
  • 18
    • 84899637111 scopus 로고    scopus 로고
    • Super-resolution microscopy of mitochondria
    • Jakobs S, Wurm CA (2014) Super-resolution microscopy of mitochondria. Curr Opin Chem Biol 20:9-15.
    • (2014) Curr Opin Chem Biol , vol.20 , pp. 9-15
    • Jakobs, S.1    Wurm, C.A.2
  • 19
    • 0037494885 scopus 로고    scopus 로고
    • The cristal membrane of mitochondria is the principal site of oxidative phosphorylation
    • Gilkerson RW, Selker JM, Capaldi RA (2003) The cristal membrane of mitochondria is the principal site of oxidative phosphorylation. FEBS Lett 546(2-3):355-358.
    • (2003) FEBS Lett , vol.546 , Issue.2-3 , pp. 355-358
    • Gilkerson, R.W.1    Selker, J.M.2    Capaldi, R.A.3
  • 20
    • 80052177663 scopus 로고    scopus 로고
    • Macromolecular organization of ATP synthase and complex I in whole mitochondria
    • Davies KM, et al. (2011) Macromolecular organization of ATP synthase and complex I in whole mitochondria. Proc Natl Acad Sci USA 108(34):14121-14126.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.34 , pp. 14121-14126
    • Davies, K.M.1
  • 22
    • 67149094710 scopus 로고    scopus 로고
    • Heterogeneity of mitochondria and mitochondrial function within cells as another level of mitochondrial complexity
    • Kuznetsov AV, Margreiter R (2009) Heterogeneity of mitochondria and mitochondrial function within cells as another level of mitochondrial complexity. Int J Mol Sci 10(4):1911-1929.
    • (2009) Int J Mol Sci , vol.10 , Issue.4 , pp. 1911-1929
    • Kuznetsov, A.V.1    Margreiter, R.2
  • 23
    • 0037007227 scopus 로고    scopus 로고
    • Mitochondria are morphologically and functionally heterogeneous within cells
    • Collins TJ, Berridge MJ, Lipp P, Bootman MD (2002) Mitochondria are morphologically and functionally heterogeneous within cells. EMBO J 21(7):1616-1627.
    • (2002) EMBO J , vol.21 , Issue.7 , pp. 1616-1627
    • Collins, T.J.1    Berridge, M.J.2    Lipp, P.3    Bootman, M.D.4
  • 24
    • 84902982320 scopus 로고    scopus 로고
    • Multiparametric optical analysis of mitochondrial redox signals during neuronal physiology and pathology in vivo
    • Breckwoldt MO, et al. (2014) Multiparametric optical analysis of mitochondrial redox signals during neuronal physiology and pathology in vivo. Nat Med 20(5):555-560.
    • (2014) Nat Med , vol.20 , Issue.5 , pp. 555-560
    • Breckwoldt, M.O.1
  • 25
    • 33644792251 scopus 로고    scopus 로고
    • Cellular mitochondrial heterogeneity in cultured astrocytes as demonstrated by immunogold labeling of alpha-ketoglutarate dehydrogenase
    • Waagepetersen HS, et al. (2006) Cellular mitochondrial heterogeneity in cultured astrocytes as demonstrated by immunogold labeling of alpha-ketoglutarate dehydrogenase. Glia 53(2):225-231.
    • (2006) Glia , vol.53 , Issue.2 , pp. 225-231
    • Waagepetersen, H.S.1
  • 26
    • 68949114217 scopus 로고    scopus 로고
    • Complexity of mitochondrial dynamics in neurons and its control by ADP produced during synaptic activity
    • Mironov SL (2009) Complexity of mitochondrial dynamics in neurons and its control by ADP produced during synaptic activity. Int J Biochem Cell Biol 41(10):2005-2014.
    • (2009) Int J Biochem Cell Biol , vol.41 , Issue.10 , pp. 2005-2014
    • Mironov, S.L.1
  • 27
    • 84895752271 scopus 로고    scopus 로고
    • Uncoupling protein 2 and 4 expression pattern during stem cell differentiation provides new insight into their putative function
    • Rupprecht A, et al. (2014) Uncoupling protein 2 and 4 expression pattern during stem cell differentiation provides new insight into their putative function. PLoS ONE 9(2):e88474.
    • (2014) PLoS ONE , vol.9 , Issue.2 , pp. e88474
    • Rupprecht, A.1
  • 28
    • 36949083936 scopus 로고
    • Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism
    • Mitchell P (1961) Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism. Nature 191:144-148.
    • (1961) Nature , vol.191 , pp. 144-148
    • Mitchell, P.1
  • 29
    • 80052283926 scopus 로고    scopus 로고
    • Protons migrate along interfacial water without significant contributions from jumps between ionizable groups on the membrane surface
    • Springer A, Hagen V, Cherepanov DA, Antonenko YN, Pohl P (2011) Protons migrate along interfacial water without significant contributions from jumps between ionizable groups on the membrane surface. Proc Natl Acad Sci USA 108(35):14461-14466.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.35 , pp. 14461-14466
    • Springer, A.1    Hagen, V.2    Cherepanov, D.A.3    Antonenko, Y.N.4    Pohl, P.5
  • 30
    • 84862571258 scopus 로고    scopus 로고
    • Water at hydrophobic interfaces delays proton surface-to-bulk transfer and provides a pathway for lateral proton diffusion
    • Zhang C, et al. (2012) Water at hydrophobic interfaces delays proton surface-to-bulk transfer and provides a pathway for lateral proton diffusion. Proc Natl Acad Sci USA 109(25):9744-9749.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.25 , pp. 9744-9749
    • Zhang, C.1
  • 31
    • 77957689381 scopus 로고    scopus 로고
    • Functional interactions between membrane-bound transporters and membranes
    • Ojemyr LN, Lee HJ, Gennis RB, Brzezinski P (2010) Functional interactions between membrane-bound transporters and membranes. Proc Natl Acad Sci USA 107(36):15763-15767.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.36 , pp. 15763-15767
    • Ojemyr, L.N.1    Lee, H.J.2    Gennis, R.B.3    Brzezinski, P.4
  • 32
    • 84920407372 scopus 로고    scopus 로고
    • Lateral pH gradient between OXPHOS complex IV and F(0)F(1) ATP-synthase in folded mitochondrial membranes
    • Rieger B, Junge W, Busch KB (2014) Lateral pH gradient between OXPHOS complex IV and F(0)F(1) ATP-synthase in folded mitochondrial membranes. Nat Commun 5:3103.
    • (2014) Nat Commun , vol.5 , pp. 3103
    • Rieger, B.1    Junge, W.2    Busch, K.B.3
  • 33
    • 84907210953 scopus 로고    scopus 로고
    • Biophysical significance of the inner mitochondrial membrane structure on the electrochemical potential of mitochondria
    • Song DH, et al. (2013) Biophysical significance of the inner mitochondrial membrane structure on the electrochemical potential of mitochondria. Phys Rev E Stat Nonlin Soft Matter Phys 88(6):062723.
    • (2013) Phys Rev e Stat Nonlin Soft Matter Phys , vol.88 , Issue.6 , pp. 062723
    • Song, D.H.1
  • 34
    • 41949123425 scopus 로고    scopus 로고
    • Dimer ribbons of ATP synthase shape the inner mitochondrial membrane
    • Strauss M, Hofhaus G, Schröder RR, Kühlbrandt W (2008) Dimer ribbons of ATP synthase shape the inner mitochondrial membrane. EMBO J 27(7):1154-1160.
    • (2008) EMBO J , vol.27 , Issue.7 , pp. 1154-1160
    • Strauss, M.1    Hofhaus, G.2    Schröder, R.R.3    Kühlbrandt, W.4
  • 35
    • 84875601992 scopus 로고    scopus 로고
    • Restricted diffusion of OXPHOS complexes in dynamic mitochondria delays their exchange between cristae and engenders a transitory mosaic distribution
    • Wilkens V, Kohl W, Busch K (2013) Restricted diffusion of OXPHOS complexes in dynamic mitochondria delays their exchange between cristae and engenders a transitory mosaic distribution. J Cell Sci 126(Pt 1):103-116.
    • (2013) J Cell Sci , vol.126 , pp. 103-116
    • Wilkens, V.1    Kohl, W.2    Busch, K.3
  • 36
    • 0029765443 scopus 로고    scopus 로고
    • Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants
    • Skulachev VP (1996) Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants. Q Rev Biophys 29(2):169-202.
    • (1996) Q Rev Biophys , vol.29 , Issue.2 , pp. 169-202
    • Skulachev, V.P.1
  • 37
    • 77951649660 scopus 로고    scopus 로고
    • Role of the transmembrane potential in the membrane proton leak
    • Rupprecht A, et al. (2010) Role of the transmembrane potential in the membrane proton leak. Biophys J 98(8):1503-1511.
    • (2010) Biophys J , vol.98 , Issue.8 , pp. 1503-1511
    • Rupprecht, A.1
  • 38
    • 84883462956 scopus 로고    scopus 로고
    • Protective effects of resveratrol on glutamate-induced damages in murine brain cultures
    • Moldzio R, et al. (2013) Protective effects of resveratrol on glutamate-induced damages in murine brain cultures. J Neural Transm 120(9):1271-1280.
    • (2013) J Neural Transm , vol.120 , Issue.9 , pp. 1271-1280
    • Moldzio, R.1
  • 39
    • 55649112045 scopus 로고    scopus 로고
    • Subdiffraction-resolution fluorescence imaging of proteins in the mitochondrial inner membrane with photoswitchable fluorophores
    • van de Linde S, Sauer M, Heilemann M (2008) Subdiffraction-resolution fluorescence imaging of proteins in the mitochondrial inner membrane with photoswitchable fluorophores. J Struct Biol 164(3):250-254.
    • (2008) J Struct Biol , vol.164 , Issue.3 , pp. 250-254
    • Van De Linde, S.1    Sauer, M.2    Heilemann, M.3
  • 40
    • 77955964893 scopus 로고    scopus 로고
    • Make them blink: Probes for super-resolution microscopy
    • Vogelsang J, et al. (2010) Make them blink: Probes for super-resolution microscopy. ChemPhysChem 11(12):2475-2490.
    • (2010) ChemPhysChem , vol.11 , Issue.12 , pp. 2475-2490
    • Vogelsang, J.1
  • 41
    • 51649083593 scopus 로고    scopus 로고
    • Subdiffraction-resolution fluorescence imaging with conventional fluorescent probes
    • Heilemann M, et al. (2008) Subdiffraction-resolution fluorescence imaging with conventional fluorescent probes. Angew Chem Int Ed Engl 47(33):6172-6176.
    • (2008) Angew Chem Int Ed Engl , vol.47 , Issue.33 , pp. 6172-6176
    • Heilemann, M.1
  • 42
    • 38749118235 scopus 로고    scopus 로고
    • Highly inclined thin illumination enables clear single-molecule imaging in cells
    • Tokunaga M, Imamoto N, Sakata-Sogawa K (2008) Highly inclined thin illumination enables clear single-molecule imaging in cells. Nat Methods 5(2):159-161.
    • (2008) Nat Methods , vol.5 , Issue.2 , pp. 159-161
    • Tokunaga, M.1    Imamoto, N.2    Sakata-Sogawa, K.3
  • 43
    • 80052803313 scopus 로고    scopus 로고
    • Binding-activated localization microscopy of DNA structures
    • Schoen I, Ries J, Klotzsch E, Ewers H, Vogel V (2011) Binding-activated localization microscopy of DNA structures. Nano Lett 11(9):4008-4011.
    • (2011) Nano Lett , vol.11 , Issue.9 , pp. 4008-4011
    • Schoen, I.1    Ries, J.2    Klotzsch, E.3    Ewers, H.4    Vogel, V.5
  • 44
    • 77952216273 scopus 로고    scopus 로고
    • Fast, single-molecule localization that achieves theoretically minimum uncertainty
    • Smith CS, Joseph N, Rieger B, Lidke KA (2010) Fast, single-molecule localization that achieves theoretically minimum uncertainty. Nat Methods 7(5):373-375.
    • (2010) Nat Methods , vol.7 , Issue.5 , pp. 373-375
    • Smith, C.S.1    Joseph, N.2    Rieger, B.3    Lidke, K.A.4
  • 45
    • 0036231415 scopus 로고    scopus 로고
    • Precise nanometer localization analysis for individual fluorescent probes
    • Thompson RE, Larson DR, Webb WW (2002) Precise nanometer localization analysis for individual fluorescent probes. Biophys J 82(5):2775-2783.
    • (2002) Biophys J , vol.82 , Issue.5 , pp. 2775-2783
    • Thompson, R.E.1    Larson, D.R.2    Webb, W.W.3
  • 46
    • 84879826657 scopus 로고    scopus 로고
    • Multiscale spatial organization of RNA polymerase in Escherichia coli
    • Endesfelder U, et al. (2013) Multiscale spatial organization of RNA polymerase in Escherichia coli. Biophys J 105(1):172-181.
    • (2013) Biophys J , vol.105 , Issue.1 , pp. 172-181
    • Endesfelder, U.1
  • 47
    • 79960806755 scopus 로고    scopus 로고
    • Quantitative photo activated localization microscopy: Unraveling the effects of photoblinking
    • Annibale P, Vanni S, Scarselli M, Rothlisberger U, Radenovic A (2011) Quantitative photo activated localization microscopy: Unraveling the effects of photoblinking. PLoS ONE 6(7):e22678.
    • (2011) PLoS ONE , vol.6 , Issue.7 , pp. e22678
    • Annibale, P.1    Vanni, S.2    Scarselli, M.3    Rothlisberger, U.4    Radenovic, A.5
  • 48
    • 84907319813 scopus 로고    scopus 로고
    • Quantitative super-resolution imaging of Bruchpilot distinguishes active zone states
    • Ehmann N, et al. (2014) Quantitative super-resolution imaging of Bruchpilot distinguishes active zone states. Nat Commun 5:4650.
    • (2014) Nat Commun , vol.5 , pp. 4650
    • Ehmann, N.1


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