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Volumn 22, Issue 4, 2012, Pages 185-192

Role of MINOS in mitochondrial membrane architecture and biogenesis

Author keywords

ERMES; MINOS; Mio10; Mitochondrial contact sites; Mitochondrial cristae; Mitofilin

Indexed keywords

BIOGENESIS; CELL STRUCTURE; COMPLEX FORMATION; ENDOPLASMIC RETICULUM; HUMAN; MITOCHONDRIAL INNER MEMBRANE ORGANIZING SYSTEM; MITOCHONDRIAL MEMBRANE; NONHUMAN; OUTER MEMBRANE; PRIORITY JOURNAL; REVIEW; YEAST;

EID: 84859265052     PISSN: 09628924     EISSN: 18793088     Source Type: Journal    
DOI: 10.1016/j.tcb.2012.01.004     Document Type: Review
Times cited : (122)

References (97)
  • 1
    • 33746575844 scopus 로고    scopus 로고
    • Evolution of the molecular machines for protein import into mitochondria
    • Dolezal P., et al. Evolution of the molecular machines for protein import into mitochondria. Science 2006, 313:314-318.
    • (2006) Science , vol.313 , pp. 314-318
    • Dolezal, P.1
  • 2
    • 78651287877 scopus 로고    scopus 로고
    • Making heads or tails of phospholipids in mitochondria
    • Osman C., et al. Making heads or tails of phospholipids in mitochondria. J. Cell Biol. 2011, 192:7-16.
    • (2011) J. Cell Biol. , vol.192 , pp. 7-16
    • Osman, C.1
  • 3
    • 79952291364 scopus 로고    scopus 로고
    • Molecular mechanisms and physiologic functions of mitochondrial dynamics
    • Otera H., Mihara K. Molecular mechanisms and physiologic functions of mitochondrial dynamics. J. Biochem. 2011, 149:241-251.
    • (2011) J. Biochem. , vol.149 , pp. 241-251
    • Otera, H.1    Mihara, K.2
  • 5
    • 33746016268 scopus 로고    scopus 로고
    • Mitochondria: more than just a powerhouse
    • McBride H.M., et al. Mitochondria: more than just a powerhouse. Curr. Biol. 2006, 16:R551-R560.
    • (2006) Curr. Biol. , vol.16
    • McBride, H.M.1
  • 6
    • 73349091842 scopus 로고    scopus 로고
    • The role of mitochondria in apoptosis
    • Wang C., Youle R.J. The role of mitochondria in apoptosis. Annu. Rev. Genet. 2009, 43:95-118.
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 95-118
    • Wang, C.1    Youle, R.J.2
  • 7
    • 68949128587 scopus 로고    scopus 로고
    • Function and biogenesis of iron-sulphur proteins
    • Lill R. Function and biogenesis of iron-sulphur proteins. Nature 2009, 460:831-838.
    • (2009) Nature , vol.460 , pp. 831-838
    • Lill, R.1
  • 8
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert W., Herrmann J.M. Translocation of proteins into mitochondria. Annu. Rev. Biochem. 2007, 76:723-749.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 9
    • 68749112707 scopus 로고    scopus 로고
    • Importing mitochondrial proteins: machineries and mechanisms
    • Chacinska A., et al. Importing mitochondrial proteins: machineries and mechanisms. Cell 2009, 138:628-644.
    • (2009) Cell , vol.138 , pp. 628-644
    • Chacinska, A.1
  • 10
    • 27544466847 scopus 로고    scopus 로고
    • Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes
    • Okamoto K., Shaw J.M. Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes. Annu. Rev. Genet. 2005, 39:503-536.
    • (2005) Annu. Rev. Genet. , vol.39 , pp. 503-536
    • Okamoto, K.1    Shaw, J.M.2
  • 11
    • 78649413837 scopus 로고    scopus 로고
    • Mitochondrial fusion and fission in cell life and death
    • Westermann B. Mitochondrial fusion and fission in cell life and death. Nat. Rev. Mol. Cell Biol. 2010, 11:872-884.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 872-884
    • Westermann, B.1
  • 12
    • 79960729178 scopus 로고    scopus 로고
    • The regulation of mitochondrial morphology: intricate mechanisms and dynamic machinery
    • Palmer C.S., et al. The regulation of mitochondrial morphology: intricate mechanisms and dynamic machinery. Cell Signal. 2011, 23:1534-1545.
    • (2011) Cell Signal. , vol.23 , pp. 1534-1545
    • Palmer, C.S.1
  • 13
    • 0030794236 scopus 로고    scopus 로고
    • Electron tomography of neuronal mitochondria: three-dimensional structure and organization of cristae and membrane contacts
    • Perkins G., et al. Electron tomography of neuronal mitochondria: three-dimensional structure and organization of cristae and membrane contacts. J. Struct. Biol. 1997, 119:260-272.
    • (1997) J. Struct. Biol. , vol.119 , pp. 260-272
    • Perkins, G.1
  • 14
    • 0034235229 scopus 로고    scopus 로고
    • The internal structure of mitochondria
    • Frey T.G., Mannella C.A. The internal structure of mitochondria. Trends Biochem. Sci. 2000, 25:319-324.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 319-324
    • Frey, T.G.1    Mannella, C.A.2
  • 15
    • 0037055983 scopus 로고    scopus 로고
    • Insight into mitochondrial structure and function from electron tomography
    • Frey T.G., et al. Insight into mitochondrial structure and function from electron tomography. Biochim. Biophys. Acta 2002, 1555:196-203.
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 196-203
    • Frey, T.G.1
  • 16
    • 29344434866 scopus 로고    scopus 로고
    • The relevance of mitochondrial membrane topology to mitochondrial function
    • Mannella C.A. The relevance of mitochondrial membrane topology to mitochondrial function. Biochim. Biophys. Acta 2006, 1762:140-147.
    • (2006) Biochim. Biophys. Acta , vol.1762 , pp. 140-147
    • Mannella, C.A.1
  • 17
    • 56349166020 scopus 로고    scopus 로고
    • Cristae formation - linking ultrastructure and function of mitochondria
    • Zick M., et al. Cristae formation - linking ultrastructure and function of mitochondria. Biochim. Biophys. Acta 2009, 1793:5-19.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 5-19
    • Zick, M.1
  • 18
    • 0015507556 scopus 로고
    • Functional and biogenetical heterogeneity of the inner membrane of rat-liver mitochondria
    • Werner S., Neupert W. Functional and biogenetical heterogeneity of the inner membrane of rat-liver mitochondria. Eur. J. Biochem. 1972, 25:379-396.
    • (1972) Eur. J. Biochem. , vol.25 , pp. 379-396
    • Werner, S.1    Neupert, W.2
  • 19
    • 0037494885 scopus 로고    scopus 로고
    • The cristal membrane of mitochondria is the principal site of oxidative phosphorylation
    • Gilkerson R.W., et al. The cristal membrane of mitochondria is the principal site of oxidative phosphorylation. FEBS Lett. 2003, 546:355-358.
    • (2003) FEBS Lett. , vol.546 , pp. 355-358
    • Gilkerson, R.W.1
  • 20
    • 33750305666 scopus 로고    scopus 로고
    • Dynamic subcompartmentalization of the mitochondrial inner membrane
    • Vogel F., et al. Dynamic subcompartmentalization of the mitochondrial inner membrane. J. Cell Biol. 2006, 175:237-247.
    • (2006) J. Cell Biol. , vol.175 , pp. 237-247
    • Vogel, F.1
  • 21
    • 33749352547 scopus 로고    scopus 로고
    • Differential protein distributions define two sub-compartments of the mitochondrial inner membrane in yeast
    • Wurm C.A., Jakobs S. Differential protein distributions define two sub-compartments of the mitochondrial inner membrane in yeast. FEBS Lett. 2006, 580:5628-5634.
    • (2006) FEBS Lett. , vol.580 , pp. 5628-5634
    • Wurm, C.A.1    Jakobs, S.2
  • 22
    • 61949403154 scopus 로고    scopus 로고
    • The m-AAA protease processes cytochrome c peroxidase preferentially at the inner boundary membrane of mitochondria
    • Suppanz I.E., et al. The m-AAA protease processes cytochrome c peroxidase preferentially at the inner boundary membrane of mitochondria. Mol. Biol. Cell 2009, 20:572-580.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 572-580
    • Suppanz, I.E.1
  • 23
    • 33744939757 scopus 로고    scopus 로고
    • o-ATP synthase supracomplexes
    • o-ATP synthase supracomplexes. J. Biol. Chem. 2006, 281:13990-13998.
    • (2006) J. Biol. Chem. , vol.281 , pp. 13990-13998
    • Bornhövd, C.1
  • 24
    • 41949123425 scopus 로고    scopus 로고
    • Dimer ribbons of ATP synthase shape the inner mitochondrial membrane
    • Strauss M., et al. Dimer ribbons of ATP synthase shape the inner mitochondrial membrane. EMBO J. 2008, 27:1154-1160.
    • (2008) EMBO J. , vol.27 , pp. 1154-1160
    • Strauss, M.1
  • 25
    • 80052177663 scopus 로고    scopus 로고
    • Macromolecular organization of ATP synthase and complex I in whole mitochondria
    • Davies K.M., et al. Macromolecular organization of ATP synthase and complex I in whole mitochondria. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:14121-14126.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 14121-14126
    • Davies, K.M.1
  • 26
    • 80054718239 scopus 로고    scopus 로고
    • Dual role of mitofilin in mitochondrial membrane organization and protein biogenesis
    • von der Malsburg K., et al. Dual role of mitofilin in mitochondrial membrane organization and protein biogenesis. Dev. Cell 2011, 21:694-707.
    • (2011) Dev. Cell , vol.21 , pp. 694-707
    • von der Malsburg, K.1
  • 27
    • 80455143571 scopus 로고    scopus 로고
    • The mitochondrial contact site complex, a determinant of mitochondrial architecture
    • Harner M., et al. The mitochondrial contact site complex, a determinant of mitochondrial architecture. EMBO J. 2011, 30:4356-4370.
    • (2011) EMBO J. , vol.30 , pp. 4356-4370
    • Harner, M.1
  • 28
    • 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. A mitochondrial-focused genetic interaction map reveals a scaffold-like complex required for inner membrane organization in mitochondria. J. Cell Biol. 2011, 195:323-340.
    • (2011) J. Cell Biol. , vol.195 , pp. 323-340
    • Hoppins, S.1
  • 29
    • 84855874566 scopus 로고    scopus 로고
    • MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organization
    • Alkhaja A.K., et al. MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organization. Mol. Biol. Cell 2012, 23:247-257.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 247-257
    • Alkhaja, A.K.1
  • 30
    • 0037055982 scopus 로고    scopus 로고
    • Is there a relationship between the supramolecular organization of the mitochondrial ATP synthase and the formation of cristae?
    • Giraud M.F., et al. Is there a relationship between the supramolecular organization of the mitochondrial ATP synthase and the formation of cristae?. Biochim. Biophys. Acta 2002, 1555:174-180.
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 174-180
    • Giraud, M.F.1
  • 31
    • 0036470775 scopus 로고    scopus 로고
    • The ATP synthase is involved in generating mitochondrial cristae morphology
    • Paumard P., et al. The ATP synthase is involved in generating mitochondrial cristae morphology. EMBO J. 2002, 21:221-230.
    • (2002) EMBO J. , vol.21 , pp. 221-230
    • Paumard, P.1
  • 32
    • 4644273159 scopus 로고    scopus 로고
    • The modulation in subunits e and g amounts of yeast ATP synthase modifies mitochondrial cristae morphology
    • Arselin G., et al. The modulation in subunits e and g amounts of yeast ATP synthase modifies mitochondrial cristae morphology. J. Biol. Chem. 2004, 279:40392-40399.
    • (2004) J. Biol. Chem. , vol.279 , pp. 40392-40399
    • Arselin, G.1
  • 33
    • 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. Formation of cristae and crista junctions in mitochondria depends on antagonism between Fcj1 and Su e/g. J. Cell Biol. 2009, 185:1047-1063.
    • (2009) J. Cell Biol. , vol.185 , pp. 1047-1063
    • Rabl, R.1
  • 34
    • 35349015148 scopus 로고    scopus 로고
    • Rows of ATP synthase dimers in native mitochondrial inner membranes
    • Buzhynskyy N., et al. Rows of ATP synthase dimers in native mitochondrial inner membranes. Biophys. J. 2007, 93:2870-2876.
    • (2007) Biophys. J. , vol.93 , pp. 2870-2876
    • Buzhynskyy, N.1
  • 35
    • 0038376024 scopus 로고    scopus 로고
    • Mgm1p, a dynamin-related GTPase, is essential for fusion of the mitochondrial outer membrane
    • Sesaki H., et al. Mgm1p, a dynamin-related GTPase, is essential for fusion of the mitochondrial outer membrane. Mol. Biol. Cell 2003, 14:2342-2356.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2342-2356
    • Sesaki, H.1
  • 36
    • 8644270474 scopus 로고    scopus 로고
    • OPA1 requires mitofusin 1 to promote mitochondrial fusion
    • Cipolat S., et al. OPA1 requires mitofusin 1 to promote mitochondrial fusion. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:15927-15932.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 15927-15932
    • Cipolat, S.1
  • 37
    • 33749991592 scopus 로고    scopus 로고
    • Mitochondrial inner-membrane fusion and crista maintenance requires the dynamin-related GTPase Mgm1
    • Meeusen S., et al. Mitochondrial inner-membrane fusion and crista maintenance requires the dynamin-related GTPase Mgm1. Cell 2006, 127:383-395.
    • (2006) Cell , vol.127 , pp. 383-395
    • Meeusen, S.1
  • 38
    • 33746299692 scopus 로고    scopus 로고
    • Regulation of mitochondrial morphology through proteolytic cleavage of OPA1
    • Ishihara N., et al. Regulation of mitochondrial morphology through proteolytic cleavage of OPA1. EMBO J. 2006, 25:2966-2977.
    • (2006) EMBO J. , vol.25 , pp. 2966-2977
    • Ishihara, N.1
  • 39
    • 70349930116 scopus 로고    scopus 로고
    • Coassembly of Mgm1 isoforms requires cardiolipin and mediates mitochondrial inner membrane fusion
    • DeVay R.M., et al. Coassembly of Mgm1 isoforms requires cardiolipin and mediates mitochondrial inner membrane fusion. J. Cell Biol. 2009, 186:793-803.
    • (2009) J. Cell Biol. , vol.186 , pp. 793-803
    • DeVay, R.M.1
  • 40
    • 33745699393 scopus 로고    scopus 로고
    • OPA1 controls apoptotic cristae remodeling independently from mitochondrial fusion
    • Frezza C., et al. OPA1 controls apoptotic cristae remodeling independently from mitochondrial fusion. Cell 2006, 126:177-189.
    • (2006) Cell , vol.126 , pp. 177-189
    • Frezza, C.1
  • 41
    • 0037450656 scopus 로고    scopus 로고
    • The inner membrane protein Mdm33 controls mitochondrial morphology in yeast
    • Messerschmitt M., et al. The inner membrane protein Mdm33 controls mitochondrial morphology in yeast. J. Cell Biol. 2003, 160:553-564.
    • (2003) J. Cell Biol. , vol.160 , pp. 553-564
    • Messerschmitt, M.1
  • 42
    • 14844314135 scopus 로고    scopus 로고
    • The mitochondrial inner membrane protein mitofilin controls cristae morphology
    • John G.B., et al. The mitochondrial inner membrane protein mitofilin controls cristae morphology. Mol. Biol. Cell 2005, 16:1543-1554.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1543-1554
    • John, G.B.1
  • 43
    • 77954573806 scopus 로고    scopus 로고
    • Caenorhabditis elegans mitofilin homologs control the morphology of mitochondrial cristae and influence reproduction and physiology
    • Mun J.Y., et al. Caenorhabditis elegans mitofilin homologs control the morphology of mitochondrial cristae and influence reproduction and physiology. J. Cell. Physiol. 2010, 224:748-756.
    • (2010) J. Cell. Physiol. , vol.224 , pp. 748-756
    • Mun, J.Y.1
  • 44
    • 79952844048 scopus 로고    scopus 로고
    • A novel mitochondrial outer membrane protein, MOMA-1, that affects cristae morphology in Caenorhabditis elegans
    • Head B.P., et al. A novel mitochondrial outer membrane protein, MOMA-1, that affects cristae morphology in Caenorhabditis elegans. Mol. Biol. Cell 2011, 22:831-841.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 831-841
    • Head, B.P.1
  • 45
    • 0027980493 scopus 로고
    • A novel human gene that is preferentially transcribed in heart muscle
    • Icho T., et al. A novel human gene that is preferentially transcribed in heart muscle. Gene 1994, 144:301-306.
    • (1994) Gene , vol.144 , pp. 301-306
    • Icho, T.1
  • 46
    • 0029815971 scopus 로고    scopus 로고
    • Molecular characterization of mitofilin (HMP), a mitochondria-associated protein with predicted coiled coil and intermembrane space targeting domains
    • Odgren P.R., et al. Molecular characterization of mitofilin (HMP), a mitochondria-associated protein with predicted coiled coil and intermembrane space targeting domains. J. Cell Sci. 1996, 109:2253-2264.
    • (1996) J. Cell Sci. , vol.109 , pp. 2253-2264
    • Odgren, P.R.1
  • 47
    • 0345687191 scopus 로고    scopus 로고
    • The proteome of Saccharomyces cerevisiae mitochondria
    • Sickmann A., et al. The proteome of Saccharomyces cerevisiae mitochondria. Proc. Natl. Acad. Sci. U.S.A. 2003, 100:13207-13212.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 13207-13212
    • Sickmann, A.1
  • 48
    • 0037336905 scopus 로고    scopus 로고
    • Characterization of the human heart mitochondrial proteome
    • Taylor S.W., et al. Characterization of the human heart mitochondrial proteome. Nat. Biotechnol. 2003, 21:281-286.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 281-286
    • Taylor, S.W.1
  • 49
    • 63449085311 scopus 로고    scopus 로고
    • Computationally driven, quantitative experiments discover genes required for mitochondrial biogenesis
    • Hess D.C., et al. Computationally driven, quantitative experiments discover genes required for mitochondrial biogenesis. PLoS Genet. 2009, 5:e1000407.
    • (2009) PLoS Genet. , vol.5
    • Hess, D.C.1
  • 50
    • 79851513761 scopus 로고    scopus 로고
    • Multiple pathways in the integration of proteins into the mitochondrial outer membrane
    • Dukanovic J., Rapaport D. Multiple pathways in the integration of proteins into the mitochondrial outer membrane. Biochim. Biophys. Acta 2011, 1808:971-980.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 971-980
    • Dukanovic, J.1    Rapaport, D.2
  • 51
    • 34447268008 scopus 로고    scopus 로고
    • The mitochondrial inner membrane protein mitofilin exists as a complex with SAM50, metaxins 1 and 2, coiled-coil-helix coiled-coil-helix domain-containing protein 3 and 6 and DnaJC11
    • Xie J., et al. The mitochondrial inner membrane protein mitofilin exists as a complex with SAM50, metaxins 1 and 2, coiled-coil-helix coiled-coil-helix domain-containing protein 3 and 6 and DnaJC11. FEBS Lett. 2007, 581:3545-3549.
    • (2007) FEBS Lett. , vol.581 , pp. 3545-3549
    • Xie, J.1
  • 52
    • 78951493639 scopus 로고    scopus 로고
    • ChChd3, an inner mitochondrial membrane protein, is essential for maintaining crista integrity and mitochondrial function
    • Darshi M., et al. ChChd3, an inner mitochondrial membrane protein, is essential for maintaining crista integrity and mitochondrial function. J. Biol. Chem. 2011, 286:2918-2932.
    • (2011) J. Biol. Chem. , vol.286 , pp. 2918-2932
    • Darshi, M.1
  • 53
    • 84857869559 scopus 로고    scopus 로고
    • Sam50 functions in mitochondrial intermembrane space bridging and biogenesis of respiratory complexes
    • Ott C., et al. Sam50 functions in mitochondrial intermembrane space bridging and biogenesis of respiratory complexes. Mol. Cell. Biol. 2012, 32:1173-1188.
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 1173-1188
    • Ott, C.1
  • 54
    • 56349110790 scopus 로고    scopus 로고
    • Redox regulation of protein folding in the mitochondrial intermembrane space
    • Koehler C.M., Tienson H.L. Redox regulation of protein folding in the mitochondrial intermembrane space. Biochim. Biophys. Acta 2009, 1793:139-145.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 139-145
    • Koehler, C.M.1    Tienson, H.L.2
  • 55
    • 84856853161 scopus 로고    scopus 로고
    • The mitochondrial disulfide relay: redox-regulated protein import into the intermembrane space
    • Herrmann J.M., Riemer J. The mitochondrial disulfide relay: redox-regulated protein import into the intermembrane space. J. Biol. Chem. 2012, 287:4426-4433.
    • (2012) J. Biol. Chem. , vol.287 , pp. 4426-4433
    • Herrmann, J.M.1    Riemer, J.2
  • 56
    • 77956309299 scopus 로고    scopus 로고
    • Oxidative protein folding in the mitochondrial intermembrane space
    • Sideris D.P., Tokatlidis K. Oxidative protein folding in the mitochondrial intermembrane space. Antioxid. Redox Signal. 2010, 13:1189-1204.
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 1189-1204
    • Sideris, D.P.1    Tokatlidis, K.2
  • 57
    • 77957024844 scopus 로고    scopus 로고
    • Structural basis for the disulfide relay system in the mitochondrial intermembrane space
    • Endo T., et al. Structural basis for the disulfide relay system in the mitochondrial intermembrane space. Antioxid. Redox Signal. 2010, 13:1359-1373.
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 1359-1373
    • Endo, T.1
  • 58
    • 84864285654 scopus 로고    scopus 로고
    • Anomalous diffusion induced by cristae geometry in the inner mitochondrial membrane
    • Sukhorukov V.M., Bereiter-Hahn J. Anomalous diffusion induced by cristae geometry in the inner mitochondrial membrane. PLoS ONE 2009, 4:e4604.
    • (2009) PLoS ONE , vol.4
    • Sukhorukov, V.M.1    Bereiter-Hahn, J.2
  • 59
    • 3142546895 scopus 로고    scopus 로고
    • Ugo1p links the Fzo1p and Mgm1p GTPases for mitochondrial fusion
    • Sesaki H., Jensen R.E. Ugo1p links the Fzo1p and Mgm1p GTPases for mitochondrial fusion. J. Biol. Chem. 2004, 279:28298-28303.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28298-28303
    • Sesaki, H.1    Jensen, R.E.2
  • 60
    • 61449256510 scopus 로고    scopus 로고
    • Mitochondrial outer and inner membrane fusion requires a modified carrier protein
    • Hoppins S., et al. Mitochondrial outer and inner membrane fusion requires a modified carrier protein. J. Cell Biol. 2009, 184:569-581.
    • (2009) J. Cell Biol. , vol.184 , pp. 569-581
    • Hoppins, S.1
  • 61
    • 13444287961 scopus 로고    scopus 로고
    • Mitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity
    • Ishihara N., et al. Mitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity. J. Cell Sci. 2004, 117:6535-6546.
    • (2004) J. Cell Sci. , vol.117 , pp. 6535-6546
    • Ishihara, N.1
  • 62
    • 67749122635 scopus 로고    scopus 로고
    • An ER-mitochondrial tethering complex revealed by a synthetic biology screen
    • Kornmann B., et al. An ER-mitochondrial tethering complex revealed by a synthetic biology screen. Science 2009, 325:477-481.
    • (2009) Science , vol.325 , pp. 477-481
    • Kornmann, B.1
  • 63
    • 67749091371 scopus 로고    scopus 로고
    • Cell biology: connecting organelles
    • Wiedemann N., et al. Cell biology: connecting organelles. Science 2009, 325:403-404.
    • (2009) Science , vol.325 , pp. 403-404
    • Wiedemann, N.1
  • 64
    • 77951716870 scopus 로고    scopus 로고
    • ERMES-mediated ER-mitochondria contacts: molecular hubs for the regulation of mitochondrial biology
    • Kornmann B., Walter P. ERMES-mediated ER-mitochondria contacts: molecular hubs for the regulation of mitochondrial biology. J. Cell Sci. 2010, 123:1389-1393.
    • (2010) J. Cell Sci. , vol.123 , pp. 1389-1393
    • Kornmann, B.1    Walter, P.2
  • 65
    • 80755153578 scopus 로고    scopus 로고
    • Staying in touch: the molecular era of organelle contact sites
    • Elbaz Y., Schuldiner M. Staying in touch: the molecular era of organelle contact sites. Trends Biochem. Sci. 2011, 36:616-623.
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 616-623
    • Elbaz, Y.1    Schuldiner, M.2
  • 66
    • 4344640696 scopus 로고    scopus 로고
    • The mitochondrial morphology protein Mdm10 functions in assembly of the preprotein translocase of the outer membrane
    • Meisinger C., et al. The mitochondrial morphology protein Mdm10 functions in assembly of the preprotein translocase of the outer membrane. Dev. Cell 2004, 7:61-71.
    • (2004) Dev. Cell , vol.7 , pp. 61-71
    • Meisinger, C.1
  • 67
    • 33747353837 scopus 로고    scopus 로고
    • Mitochondrial protein sorting: differentiation of β-barrel assembly by Tom7-mediated segregation of Mdm10
    • Meisinger C., et al. Mitochondrial protein sorting: differentiation of β-barrel assembly by Tom7-mediated segregation of Mdm10. J. Biol. Chem. 2006, 281:22819-22826.
    • (2006) J. Biol. Chem. , vol.281 , pp. 22819-22826
    • Meisinger, C.1
  • 68
    • 34247583466 scopus 로고    scopus 로고
    • The morphology proteins Mdm12/Mmm1 function in the major β-barrel assembly pathway of mitochondria
    • Meisinger C., et al. The morphology proteins Mdm12/Mmm1 function in the major β-barrel assembly pathway of mitochondria. EMBO J. 2007, 26:2229-2239.
    • (2007) EMBO J. , vol.26 , pp. 2229-2239
    • Meisinger, C.1
  • 69
    • 78650658645 scopus 로고    scopus 로고
    • Tom7 regulates Mdm10-mediated assembly of the mitochondrial import channel protein Tom40
    • Yamano K., et al. Tom7 regulates Mdm10-mediated assembly of the mitochondrial import channel protein Tom40. J. Biol. Chem. 2010, 285:41222-41231.
    • (2010) J. Biol. Chem. , vol.285 , pp. 41222-41231
    • Yamano, K.1
  • 70
    • 77952395425 scopus 로고    scopus 로고
    • Roles of the Mdm10, Tom7, Mdm12, and Mmm1 proteins in the assembly of mitochondrial outer membrane proteins in Neurospora crassa
    • Wideman J.G., et al. Roles of the Mdm10, Tom7, Mdm12, and Mmm1 proteins in the assembly of mitochondrial outer membrane proteins in Neurospora crassa. Mol. Biol. Cell 2010, 21:1725-1736.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1725-1736
    • Wideman, J.G.1
  • 71
    • 78650418885 scopus 로고    scopus 로고
    • Biogenesis of mitochondria: dual role of Tom7 in modulating assembly of the preprotein translocase of the outer membrane
    • Becker T., et al. Biogenesis of mitochondria: dual role of Tom7 in modulating assembly of the preprotein translocase of the outer membrane. J. Mol. Biol. 2011, 405:113-124.
    • (2011) J. Mol. Biol. , vol.405 , pp. 113-124
    • Becker, T.1
  • 72
    • 0028129071 scopus 로고
    • MMM1 encodes a mitochondrial outer membrane protein essential for establishing and maintaining the structure of yeast mitochondria
    • Burgess S.M., et al. MMM1 encodes a mitochondrial outer membrane protein essential for establishing and maintaining the structure of yeast mitochondria. J. Cell Biol. 1994, 126:1375-1391.
    • (1994) J. Cell Biol. , vol.126 , pp. 1375-1391
    • Burgess, S.M.1
  • 73
    • 0028024592 scopus 로고
    • Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane
    • Sogo L.F., Yaffe M.P. Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane. J. Cell Biol. 1994, 126:1361-1373.
    • (1994) J. Cell Biol. , vol.126 , pp. 1361-1373
    • Sogo, L.F.1    Yaffe, M.P.2
  • 74
    • 0031059722 scopus 로고    scopus 로고
    • Mdm12p, a component required for mitochondrial inheritance that is conserved between budding and fission yeast
    • Berger K.H., et al. Mdm12p, a component required for mitochondrial inheritance that is conserved between budding and fission yeast. J. Cell Biol. 1997, 136:545-553.
    • (1997) J. Cell Biol. , vol.136 , pp. 545-553
    • Berger, K.H.1
  • 75
    • 0344392841 scopus 로고    scopus 로고
    • A protein complex containing Mdm10p, Mdm12p, and Mmm1p links mitochondrial membranes and DNA to the cytoskeleton-based segregation machinery
    • Boldogh I.R., et al. A protein complex containing Mdm10p, Mdm12p, and Mmm1p links mitochondrial membranes and DNA to the cytoskeleton-based segregation machinery. Mol. Biol. Cell 2003, 14:4618-4627.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4618-4627
    • Boldogh, I.R.1
  • 76
    • 1442337560 scopus 로고    scopus 로고
    • Mmm1p spans both the outer and inner mitochondrial membranes and contains distinct domains for targeting and foci formation
    • Kondo-Okamoto N., et al. Mmm1p spans both the outer and inner mitochondrial membranes and contains distinct domains for targeting and foci formation. J. Biol. Chem. 2003, 278:48997-49005.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48997-49005
    • Kondo-Okamoto, N.1
  • 77
    • 5444257615 scopus 로고    scopus 로고
    • Yeast Miro GTPase, Gem1p, regulates mitochondrial morphology via a novel pathway
    • Frederick R.L., et al. Yeast Miro GTPase, Gem1p, regulates mitochondrial morphology via a novel pathway. J. Cell Biol. 2004, 167:87-98.
    • (2004) J. Cell Biol. , vol.167 , pp. 87-98
    • Frederick, R.L.1
  • 78
    • 1442309968 scopus 로고    scopus 로고
    • Mmm2p, a mitochondrial outer membrane protein required for yeast mitochondrial shape and maintenance of mtDNA nucleoids
    • Youngman M.J., et al. Mmm2p, a mitochondrial outer membrane protein required for yeast mitochondrial shape and maintenance of mtDNA nucleoids. J. Cell Biol. 2004, 164:677-688.
    • (2004) J. Cell Biol. , vol.164 , pp. 677-688
    • Youngman, M.J.1
  • 79
    • 12144280303 scopus 로고    scopus 로고
    • Mdm31 and Mdm32 are inner membrane proteins required for maintenance of mitochondrial shape and stability of mitochondrial DNA nucleoids in yeast
    • Dimmer K.S., et al. Mdm31 and Mdm32 are inner membrane proteins required for maintenance of mitochondrial shape and stability of mitochondrial DNA nucleoids in yeast. J. Cell Biol. 2005, 168:103-115.
    • (2005) J. Cell Biol. , vol.168 , pp. 103-115
    • Dimmer, K.S.1
  • 80
    • 0035931747 scopus 로고    scopus 로고
    • Mmm1p, a mitochondrial outer membrane protein, is connected to mitochondrial DNA (mtDNA) nucleoids and required for mtDNA stability
    • Hobbs A.E., et al. Mmm1p, a mitochondrial outer membrane protein, is connected to mitochondrial DNA (mtDNA) nucleoids and required for mtDNA stability. J. Cell Biol. 2001, 152:401-410.
    • (2001) J. Cell Biol. , vol.152 , pp. 401-410
    • Hobbs, A.E.1
  • 81
    • 61449229779 scopus 로고    scopus 로고
    • The genetic interactome of prohibitins: coordinated control of cardiolipin and phosphatidylethanolamine by conserved regulators in mitochondria
    • Osman C., et al. The genetic interactome of prohibitins: coordinated control of cardiolipin and phosphatidylethanolamine by conserved regulators in mitochondria. J. Cell Biol. 2009, 184:583-596.
    • (2009) J. Cell Biol. , vol.184 , pp. 583-596
    • Osman, C.1
  • 82
    • 0033199506 scopus 로고    scopus 로고
    • Association between the endoplasmic reticulum and mitochondria of yeast facilitates interorganelle transport of phospholipids through membrane contact
    • Achleitner G., et al. Association between the endoplasmic reticulum and mitochondria of yeast facilitates interorganelle transport of phospholipids through membrane contact. Eur. J. Biochem. 1999, 264:545-553.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 545-553
    • Achleitner, G.1
  • 83
    • 39449112660 scopus 로고    scopus 로고
    • Prohibitins control cell proliferation and apoptosis by regulating OPA1-dependent cristae morphogenesis in mitochondria
    • Merkwirth C., et al. Prohibitins control cell proliferation and apoptosis by regulating OPA1-dependent cristae morphogenesis in mitochondria. Genes Dev. 2008, 22:476-488.
    • (2008) Genes Dev. , vol.22 , pp. 476-488
    • Merkwirth, C.1
  • 85
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • de Brito O.M., Scorrano L. Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature 2008, 456:605-610.
    • (2008) Nature , vol.456 , pp. 605-610
    • de Brito, O.M.1    Scorrano, L.2
  • 86
    • 80052172908 scopus 로고    scopus 로고
    • The conserved GTPase Gem1 regulates endoplasmic reticulum-mitochondria connections
    • Kornmann B., et al. The conserved GTPase Gem1 regulates endoplasmic reticulum-mitochondria connections. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:14151-14156.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 14151-14156
    • Kornmann, B.1
  • 87
    • 80054847097 scopus 로고    scopus 로고
    • Composition and topology of the endoplasmic reticulum-mitochondria encounter structure
    • Stroud D.A., et al. Composition and topology of the endoplasmic reticulum-mitochondria encounter structure. J. Mol. Biol. 2011, 413:743-750.
    • (2011) J. Mol. Biol. , vol.413 , pp. 743-750
    • Stroud, D.A.1
  • 88
    • 33646768127 scopus 로고    scopus 로고
    • Axonal transport of mitochondria requires milton to recruit kinesin heavy chain and is light chain independent
    • Glater E.E., et al. Axonal transport of mitochondria requires milton to recruit kinesin heavy chain and is light chain independent. J. Cell Biol. 2006, 173:545-557.
    • (2006) J. Cell Biol. , vol.173 , pp. 545-557
    • Glater, E.E.1
  • 89
    • 58149091896 scopus 로고    scopus 로고
    • 2+-dependent regulation of kinesin-mediated mitochondrial motility
    • 2+-dependent regulation of kinesin-mediated mitochondrial motility. Cell 2009, 136:163-174.
    • (2009) Cell , vol.136 , pp. 163-174
    • Wang, X.1    Schwarz, T.L.2
  • 90
    • 78650935783 scopus 로고    scopus 로고
    • Structure-function analysis of the yeast mitochondrial Rho GTPase, Gem1p: implications for mitochondrial inheritance
    • Koshiba T., et al. Structure-function analysis of the yeast mitochondrial Rho GTPase, Gem1p: implications for mitochondrial inheritance. J. Biol. Chem. 2011, 286:354-362.
    • (2011) J. Biol. Chem. , vol.286 , pp. 354-362
    • Koshiba, T.1
  • 91
    • 0242593934 scopus 로고    scopus 로고
    • Evidence for a two membrane-spanning autonomous mitochondrial DNA replisome
    • Meeusen S., Nunnari J. Evidence for a two membrane-spanning autonomous mitochondrial DNA replisome. J. Cell Biol. 2003, 163:503-510.
    • (2003) J. Cell Biol. , vol.163 , pp. 503-510
    • Meeusen, S.1    Nunnari, J.2
  • 92
    • 80054844842 scopus 로고    scopus 로고
    • ER tubules mark sites of mitochondrial division
    • Friedman J.R., et al. ER tubules mark sites of mitochondrial division. Science 2011, 334:358-362.
    • (2011) Science , vol.334 , pp. 358-362
    • Friedman, J.R.1
  • 93
    • 0036007116 scopus 로고    scopus 로고
    • A distinct pathway remodels mitochondrial cristae and mobilizes cytochrome c during apoptosis
    • Scorrano L., et al. A distinct pathway remodels mitochondrial cristae and mobilizes cytochrome c during apoptosis. Dev. Cell 2002, 2:55-67.
    • (2002) Dev. Cell , vol.2 , pp. 55-67
    • Scorrano, L.1
  • 94
    • 0043166392 scopus 로고    scopus 로고
    • Dynamics of mitochondrial morphology in healthy cells and during apoptosis
    • Karbowski M., Youle R.J. Dynamics of mitochondrial morphology in healthy cells and during apoptosis. Cell Death Differ. 2003, 10:870-880.
    • (2003) Cell Death Differ. , vol.10 , pp. 870-880
    • Karbowski, M.1    Youle, R.J.2
  • 95
    • 18444400187 scopus 로고    scopus 로고
    • Endoplasmic reticulum BIK initiates DRP1-regulated remodelling of mitochondrial cristae during apoptosis
    • Germain M., et al. Endoplasmic reticulum BIK initiates DRP1-regulated remodelling of mitochondrial cristae during apoptosis. EMBO J. 2005, 24:1546-1556.
    • (2005) EMBO J. , vol.24 , pp. 1546-1556
    • Germain, M.1
  • 96
    • 49349112331 scopus 로고    scopus 로고
    • Opa1-mediated cristae opening is Bax/Bak and BH3 dependent, required for apoptosis, and independent of Bak oligomerization
    • Yamaguchi R., et al. Opa1-mediated cristae opening is Bax/Bak and BH3 dependent, required for apoptosis, and independent of Bak oligomerization. Mol. Cell 2008, 31:557-569.
    • (2008) Mol. Cell , vol.31 , pp. 557-569
    • Yamaguchi, R.1
  • 97
    • 67649321228 scopus 로고    scopus 로고
    • Distinct roles of the two isoforms of the dynamin-like GTPase Mgm1 in mitochondrial fusion
    • Zick M., et al. Distinct roles of the two isoforms of the dynamin-like GTPase Mgm1 in mitochondrial fusion. FEBS Lett. 2009, 583:2237-2243.
    • (2009) FEBS Lett. , vol.583 , pp. 2237-2243
    • Zick, M.1


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