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Volumn 110, Issue 22, 2013, Pages 8936-8941

STED super-resolution microscopy reveals an array of MINOS clusters along human mitochondria

Author keywords

Membrane architecture; MICOS; MitOS; Nanoscopy

Indexed keywords

CHCHD 3 PROTEIN; MEMBRANE PROTEIN; MITOCHONDRIAL INNER MEMBRANE ORGANIZING SYSTEM PROTEIN; MITOCHONDRIAL INNER MEMBRANE ORGANIZING SYSTEM PROTEIN 1; MITOFILIN PROTEIN; UNCLASSIFIED DRUG;

EID: 84878437545     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1301820110     Document Type: Article
Times cited : (148)

References (41)
  • 1
    • 27544466847 scopus 로고    scopus 로고
    • Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes
    • Okamoto K, Shaw JM (2005) Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes. Annu Rev Genet 39:503-536.
    • (2005) Annu Rev Genet , vol.39 , pp. 503-536
    • Okamoto, K.1    Shaw, J.M.2
  • 2
    • 0034235229 scopus 로고    scopus 로고
    • The internal structure of mitochondria
    • Frey TG, Mannella CA (2000) The internal structure of mitochondria. Trends Biochem Sci 25(7):319-324.
    • (2000) Trends Biochem Sci , vol.25 , Issue.7 , pp. 319-324
    • Frey, T.G.1    Mannella, C.A.2
  • 3
    • 0030794236 scopus 로고    scopus 로고
    • Electron tomography of neuronal mitochondria: Threedimensional structure and organization of cristae and membrane contacts
    • Perkins G, et al. (1997) Electron tomography of neuronal mitochondria: Threedimensional structure and organization of cristae and membrane contacts. J Struct Biol 119(3):260-272.
    • (1997) J Struct Biol , vol.119 , Issue.3 , pp. 260-272
    • Perkins, G.1
  • 4
    • 33745737928 scopus 로고    scopus 로고
    • Structure and dynamics of the mitochondrial inner membrane cristae
    • Mannella CA (2006) Structure and dynamics of the mitochondrial inner membrane cristae. Biochim Biophys Acta 1763(5-6):542-548.
    • (2006) Biochim Biophys Acta , vol.1763 , Issue.5-6 , pp. 542-548
    • Mannella, C.A.1
  • 5
    • 33749352547 scopus 로고    scopus 로고
    • Differential protein distributions define two subcompartments of the mitochondrial inner membrane in yeast
    • Wurm CA, Jakobs S (2006) Differential protein distributions define two subcompartments 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
  • 6
    • 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
  • 7
    • 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
  • 8
    • 0037494885 scopus 로고    scopus 로고
    • The cristal membrane of mitochondria is the principal site of oxidative phosphorylation
    • Gilkerson RW, Selker JML, 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.L.2    Capaldi, R.A.3
  • 9
    • 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
  • 10
    • 84862599292 scopus 로고    scopus 로고
    • SnapShot: Mitochondrial architecture
    • Neupert W (2012) SnapShot: Mitochondrial architecture. Cell 149(3):722-722e1.
    • (2012) Cell , vol.149 , Issue.3
    • Neupert, W.1
  • 11
    • 84859265052 scopus 로고    scopus 로고
    • Role of MINOS in mitochondrial membrane architecture and biogenesis
    • van der Laan M, Bohnert M, Wiedemann N, Pfanner N (2012) Role of MINOS in mitochondrial membrane architecture and biogenesis. Trends Cell Biol 22(4):185-192.
    • (2012) Trends Cell Biol , vol.22 , Issue.4 , pp. 185-192
    • Van Der Laan, M.1    Bohnert, M.2    Wiedemann, N.3    Pfanner, N.4
  • 12
    • 84869422571 scopus 로고    scopus 로고
    • Mitofilin complexes: Conserved organizers of mitochondrial membrane architecture
    • Zerbes RM, et al. (2012) Mitofilin complexes: Conserved organizers of mitochondrial membrane architecture. Biol Chem 393(11):1247-1261.
    • (2012) Biol Chem , vol.393 , Issue.11 , pp. 1247-1261
    • Zerbes, R.M.1
  • 13
    • 80054772036 scopus 로고    scopus 로고
    • MINOS is plus: A Mitofilin complex for mitochondrial membrane contacts
    • Herrmann JM (2011) MINOS is plus: A Mitofilin complex for mitochondrial membrane contacts. Dev Cell 21(4):599-600.
    • (2011) Dev Cell , vol.21 , Issue.4 , pp. 599-600
    • Herrmann, J.M.1
  • 14
    • 80054718239 scopus 로고    scopus 로고
    • Dual role of mitofilin in mitochondrial membrane organization and protein biogenesis
    • von der Malsburg K, et al. (2011) Dual role of mitofilin in mitochondrial membrane organization and protein biogenesis. Dev Cell 21(4):694-707.
    • (2011) Dev Cell , vol.21 , Issue.4 , pp. 694-707
    • Von Der Malsburg, K.1
  • 15
    • 84855874566 scopus 로고    scopus 로고
    • MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organization
    • Alkhaja AK, et al. (2012) MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organization. Mol Biol Cell 23(2): 247-257.
    • (2012) Mol Biol Cell , vol.23 , Issue.2 , pp. 247-257
    • Alkhaja, A.K.1
  • 16
    • 80155186698 scopus 로고    scopus 로고
    • A mitochondrial-focused genetic interaction map reveals a scaffold-like complex required for inner membrane organization in mitochondria
    • Hoppins S, et al. (2011) A mitochondrial-focused genetic interaction map reveals a scaffold-like complex required for inner membrane organization in mitochondria. J Cell Biol 195(2):323-340.
    • (2011) J Cell Biol , vol.195 , Issue.2 , pp. 323-340
    • Hoppins, S.1
  • 17
    • 80455143571 scopus 로고    scopus 로고
    • The mitochondrial contact site complex, a determinant of mitochondrial architecture
    • Harner M, et al. (2011) The mitochondrial contact site complex, a determinant of mitochondrial architecture. EMBO J 30(21):4356-4370.
    • (2011) EMBO J , vol.30 , Issue.21 , pp. 4356-4370
    • Harner, M.1
  • 18
    • 34447268008 scopus 로고    scopus 로고
    • The mitochondrial inner membrane protein mitofilin exists as a complex with SAM50, metaxins 1 and 2, coiledcoil-helix coiled-coil-helix domain-containing protein 3 and 6 and DnaJC11
    • Xie J, Marusich MF, Souda P, Whitelegge J, Capaldi RA (2007) The mitochondrial inner membrane protein mitofilin exists as a complex with SAM50, metaxins 1 and 2, coiledcoil-helix coiled-coil-helix domain-containing protein 3 and 6 and DnaJC11. FEBS Lett 581(18):3545-3549.
    • (2007) FEBS Lett , vol.581 , Issue.18 , pp. 3545-3549
    • Xie, J.1    Marusich, M.F.2    Souda, P.3    Whitelegge, J.4    Capaldi, R.A.5
  • 19
    • 78951493639 scopus 로고    scopus 로고
    • ChChd3, an inner mitochondrial membrane protein, is essential for maintaining crista integrity and mitochondrial function
    • Darshi M, et al. (2011) ChChd3, an inner mitochondrial membrane protein, is essential for maintaining crista integrity and mitochondrial function. J Biol Chem 286(4): 2918-2932.
    • (2011) J Biol Chem , vol.286 , Issue.4 , pp. 2918-2932
    • Darshi, M.1
  • 20
    • 84857869559 scopus 로고    scopus 로고
    • Sam50 functions in mitochondrial intermembrane space bridging and biogenesis of respiratory complexes
    • Ott C, et al. (2012) Sam50 functions in mitochondrial intermembrane space bridging and biogenesis of respiratory complexes. Mol Cell Biol 32(6):1173-1188.
    • (2012) Mol Cell Biol , vol.32 , Issue.6 , pp. 1173-1188
    • Ott, C.1
  • 21
    • 84864843177 scopus 로고    scopus 로고
    • Role of MINOS in mitochondrial membrane architecture: Cristae morphology and outer membrane interactions differentially depend on mitofilin domains
    • Zerbes RM, et al. (2012) Role of MINOS in mitochondrial membrane architecture: Cristae morphology and outer membrane interactions differentially depend on mitofilin domains. J Mol Biol 422(2):183-191.
    • (2012) J Mol Biol , vol.422 , Issue.2 , pp. 183-191
    • Zerbes, R.M.1
  • 22
    • 84861673870 scopus 로고    scopus 로고
    • The C-terminal domain of Fcj1 is required for formation of crista junctions and interacts with the TOB/SAM complex in mitochondria
    • Körner C, et al. (2012) The C-terminal domain of Fcj1 is required for formation of crista junctions and interacts with the TOB/SAM complex in mitochondria. Mol Biol Cell 23(11):2143-2155.
    • (2012) Mol Biol Cell , vol.23 , Issue.11 , pp. 2143-2155
    • Körner, C.1
  • 23
    • 63449085311 scopus 로고    scopus 로고
    • Computationally driven, quantitative experiments discover genes required for mitochondrial biogenesis
    • Hess DC, et al. (2009) Computationally driven, quantitative experiments discover genes required for mitochondrial biogenesis. PLoS Genet 5(3):e1000407.
    • (2009) PLoS Genet , vol.5 , Issue.3
    • Hess, D.C.1
  • 24
    • 67449168381 scopus 로고    scopus 로고
    • Formation of cristae and crista junctions in mitochondria depends on antagonism between Fcj1 and Su e/g
    • Rabl R, et al. (2009) Formation of cristae and crista junctions in mitochondria depends on antagonism between Fcj1 and Su e/g. J Cell Biol 185(6):1047-1063.
    • (2009) J Cell Biol , vol.185 , Issue.6 , pp. 1047-1063
    • Rabl, R.1
  • 25
    • 80051958959 scopus 로고    scopus 로고
    • Light microscopic analysis of mitochondrial heterogeneity in cell populations and within single cells
    • Jakobs S, Stoldt S, Neumann D (2011) Light microscopic analysis of mitochondrial heterogeneity in cell populations and within single cells. Adv Biochem Eng Biotechnol 124:1-19.
    • (2011) Adv Biochem Eng Biotechnol , vol.124 , pp. 1-19
    • Jakobs, S.1    Stoldt, S.2    Neumann, D.3
  • 26
    • 34249945258 scopus 로고    scopus 로고
    • Far-field optical nanoscopy
    • Hell SW (2007) Far-field optical nanoscopy. Science 316(5828):1153-1158.
    • (2007) Science , vol.316 , Issue.5828 , pp. 1153-1158
    • Hell, S.W.1
  • 27
    • 0000259466 scopus 로고
    • Cytoplasmic microtubular images in glutaraldehyde-fixed tissue culture cells by electron microscopy and by immunofluorescence microscopy
    • Weber K, Rathke PC, Osborn M (1978) Cytoplasmic microtubular images in glutaraldehyde-fixed tissue culture cells by electron microscopy and by immunofluorescence microscopy. Proc Natl Acad Sci USA 75(4):1820-1824.
    • (1978) Proc Natl Acad Sci USA , vol.75 , Issue.4 , pp. 1820-1824
    • Weber, K.1    Rathke, P.C.2    Osborn, M.3
  • 28
    • 0242290929 scopus 로고    scopus 로고
    • Immunofluorescence stimulated emission depletion microscopy
    • Dyba M, Jakobs S, Hell SW (2003) Immunofluorescence stimulated emission depletion microscopy. Nat Biotechnol 21(11):1303-1304.
    • (2003) Nat Biotechnol , vol.21 , Issue.11 , pp. 1303-1304
    • Dyba, M.1    Jakobs, S.2    Hell, S.W.3
  • 29
    • 80052010249 scopus 로고    scopus 로고
    • Nanoscale distribution of mitochondrial import receptor Tom20 is adjusted to cellular conditions and exhibits an inner-cellular gradient
    • Wurm CA, et al. (2011) Nanoscale distribution of mitochondrial import receptor Tom20 is adjusted to cellular conditions and exhibits an inner-cellular gradient. Proc Natl Acad Sci USA 108(33):13546-13551.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.33 , pp. 13546-13551
    • Wurm, C.A.1
  • 30
    • 84863229687 scopus 로고    scopus 로고
    • CHCM1/CHCHD6, novel mitochondrial protein linked to regulation of mitofilin and mitochondrial cristae morphology
    • An J, et al. (2012) CHCM1/CHCHD6, novel mitochondrial protein linked to regulation of mitofilin and mitochondrial cristae morphology. J Biol Chem 287(10):7411-7426.
    • (2012) J Biol Chem , vol.287 , Issue.10 , pp. 7411-7426
    • An, J.1
  • 31
    • 84867449307 scopus 로고    scopus 로고
    • Role of mitochondrial inner membrane organizing system in protein biogenesis of the mitochondrial outer membrane
    • Bohnert M, et al. (2012) Role of mitochondrial inner membrane organizing system in protein biogenesis of the mitochondrial outer membrane. Mol Biol Cell 23(20): 3948-3956.
    • (2012) Mol Biol Cell , vol.23 , Issue.20 , pp. 3948-3956
    • Bohnert, M.1
  • 32
    • 80051972817 scopus 로고    scopus 로고
    • Super-resolution microscopy reveals that mammalian mitochondrial nucleoids have a uniform size and frequently contain a single copy of mtDNA
    • Kukat C, et al. (2011) Super-resolution microscopy reveals that mammalian mitochondrial nucleoids have a uniform size and frequently contain a single copy of mtDNA. Proc Natl Acad Sci USA 108(33):13534-13539.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.33 , pp. 13534-13539
    • Kukat, C.1
  • 33
    • 75749098116 scopus 로고    scopus 로고
    • The micro-architecture of mitochondria at active zones: Electron tomography reveals novel anchoring scaffolds and cristae structured for high-rate metabolism
    • Perkins GA, et al. (2010) The micro-architecture of mitochondria at active zones: Electron tomography reveals novel anchoring scaffolds and cristae structured for high-rate metabolism. J Neurosci 30(3):1015-1026.
    • (2010) J Neurosci , vol.30 , Issue.3 , pp. 1015-1026
    • Perkins, G.A.1
  • 34
    • 84862870271 scopus 로고    scopus 로고
    • The axonal transport of mitochondria
    • Saxton WM, Hollenbeck PJ (2012) The axonal transport of mitochondria. J Cell Sci 125(Pt 9):2095-2104.
    • (2012) J Cell Sci , vol.125 , Issue.PART 9 , pp. 2095-2104
    • Saxton, W.M.1    Hollenbeck, P.J.2
  • 35
    • 35948978460 scopus 로고    scopus 로고
    • Moving mitochondria: Establishing distribution of an essential organelle
    • Frederick RL, Shaw JM (2007) Moving mitochondria: Establishing distribution of an essential organelle. Traffic 8(12):1668-1675.
    • (2007) Traffic , vol.8 , Issue.12 , pp. 1668-1675
    • Frederick, R.L.1    Shaw, J.M.2
  • 36
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • de Brito OM, Scorrano L (2008) Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature 456(7222):605-610.
    • (2008) Nature , vol.456 , Issue.7222 , pp. 605-610
    • De Brito, O.M.1    Scorrano, L.2
  • 37
    • 84866728707 scopus 로고    scopus 로고
    • Endoplasmic reticulum-mitochondria contacts: Function of the junction
    • Rowland AA, Voeltz GK (2012) Endoplasmic reticulum-mitochondria contacts: Function of the junction. Nat Rev Mol Cell Biol 13(10):607-625.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , Issue.10 , pp. 607-625
    • Rowland, A.A.1    Voeltz, G.K.2
  • 38
    • 80052172908 scopus 로고    scopus 로고
    • The conserved GTPase Gem1 regulates endoplasmic reticulum-mitochondria connections
    • Kornmann B, Osman C, Walter P (2011) The conserved GTPase Gem1 regulates endoplasmic reticulum-mitochondria connections. Proc Natl Acad Sci USA 108(34): 14151-14156.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.34 , pp. 14151-14156
    • Kornmann, B.1    Osman, C.2    Walter, P.3
  • 39
    • 80054847097 scopus 로고    scopus 로고
    • Composition and topology of the endoplasmic reticulummitochondria encounter structure
    • Stroud DA, et al. (2011) Composition and topology of the endoplasmic reticulummitochondria encounter structure. J Mol Biol 413(4):743-750.
    • (2011) J Mol Biol , vol.413 , Issue.4 , pp. 743-750
    • Stroud, D.A.1
  • 41
    • 79957976176 scopus 로고    scopus 로고
    • Two-color STED microscopy reveals different degrees of colocalization between hexokinase-I and the three human VDAC isoforms
    • Neumann D, Bückers J, Kastrup L, Hell SW, Jakobs S (2010) Two-color STED microscopy reveals different degrees of colocalization between hexokinase-I and the three human VDAC isoforms. PMC Biophys 3(1):4.
    • (2010) PMC Biophys , vol.3 , Issue.1 , pp. 4
    • Neumann, D.1    Bückers, J.2    Kastrup, L.3    Hell, S.W.4    Jakobs, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.