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Volumn 1763, Issue 5-6, 2006, Pages 482-489

Molecular mechanism of mitochondrial membrane fusion

Author keywords

GTPase; Membrane fusion; Mitochondrial dynamics; Mitochondrial fusion; Organelles

Indexed keywords

CARBONYL CYANIDE CHLOROPHENYLHYDRAZONE; DYNAMIN; ERGOSTEROL; FUZZY ONION; GLYCOPROTEIN; GUANOSINE TRIPHOSPHATASE; MEMBRANE PROTEIN; MITOFUSIN; MITOFUSIN 1; MITOFUSIN 2; PROTEIN; PROTEIN OPA1; SNARE PROTEIN; UNCLASSIFIED DRUG; VALINOMYCIN;

EID: 33745758647     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2006.02.003     Document Type: Review
Times cited : (52)

References (63)
  • 2
    • 0031440879 scopus 로고    scopus 로고
    • Developmentally regulated mitochondrial fusion mediated by a conserved, novel, predicted GTPase
    • Hales K.G., and Fuller M.T. Developmentally regulated mitochondrial fusion mediated by a conserved, novel, predicted GTPase. Cell 90 (1997) 121-129
    • (1997) Cell , vol.90 , pp. 121-129
    • Hales, K.G.1    Fuller, M.T.2
  • 4
    • 0037455575 scopus 로고    scopus 로고
    • Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development
    • Chen H., Detmer S.A., Ewald A.J., Griffin E.E., Fraser S.E., and Chan D.C. Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development. J. Cell Biol. 160 (2003) 189-200
    • (2003) J. Cell Biol. , vol.160 , pp. 189-200
    • Chen, H.1    Detmer, S.A.2    Ewald, A.J.3    Griffin, E.E.4    Fraser, S.E.5    Chan, D.C.6
  • 5
    • 22544451586 scopus 로고    scopus 로고
    • Disruption of fusion results in mitochondrial heterogeneity and dysfunction
    • Chen H., Chomyn A., and Chan D.C. Disruption of fusion results in mitochondrial heterogeneity and dysfunction. J. Biol. Chem. 280 (2005) 26185-26192
    • (2005) J. Biol. Chem. , vol.280 , pp. 26185-26192
    • Chen, H.1    Chomyn, A.2    Chan, D.C.3
  • 6
    • 0032493625 scopus 로고    scopus 로고
    • Fzo1p is a mitochondrial outer membrane protein essential for the biogenesis of functional mitochondria in Saccharomyces cerevisiae
    • Rapaport D., Brunner M., Neupert W., and Westermann B. Fzo1p is a mitochondrial outer membrane protein essential for the biogenesis of functional mitochondria in Saccharomyces cerevisiae. J. Biol. Chem. 273 (1998) 20150-20155
    • (1998) J. Biol. Chem. , vol.273 , pp. 20150-20155
    • Rapaport, D.1    Brunner, M.2    Neupert, W.3    Westermann, B.4
  • 10
    • 22544465572 scopus 로고    scopus 로고
    • Clinical and electrophysiologic features of CMT2A with mutations in the mitofusin 2 gene
    • Lawson V.H., Graham B.V., and Flanigan K.M. Clinical and electrophysiologic features of CMT2A with mutations in the mitofusin 2 gene. Neurology 65 (2005) 197-204
    • (2005) Neurology , vol.65 , pp. 197-204
    • Lawson, V.H.1    Graham, B.V.2    Flanigan, K.M.3
  • 12
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert D.M., and Kim P.S. Mechanisms of viral membrane fusion and its inhibition. Annu. Rev. Biochem. 70 (2001) 777-810
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 13
    • 0032431055 scopus 로고    scopus 로고
    • Coiled coils in both intracellular vesicle and viral membrane fusion
    • Skehel J.J., and Wiley D.C. Coiled coils in both intracellular vesicle and viral membrane fusion. Cell 95 (1998) 871-874
    • (1998) Cell , vol.95 , pp. 871-874
    • Skehel, J.J.1    Wiley, D.C.2
  • 14
    • 0842324801 scopus 로고    scopus 로고
    • The mechanisms of vesicle budding and fusion
    • Bonifacino J.S., and Glick B.S. The mechanisms of vesicle budding and fusion. Cell 116 (2004) 153-166
    • (2004) Cell , vol.116 , pp. 153-166
    • Bonifacino, J.S.1    Glick, B.S.2
  • 20
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution
    • Sutton R.B., Fasshauer D., Jahn R., and Brunger A.T. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution. Nature 395 (1998) 347-353
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 21
    • 0030841103 scopus 로고    scopus 로고
    • Mitochondrial transmission during mating in Saccharomyces cerevisiae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA
    • Nunnari J., Marshall W.F., Straight A., Murray A., Sedat J.W., and Walter P. Mitochondrial transmission during mating in Saccharomyces cerevisiae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA. Mol. Biol. Cell 8 (1997) 1233-1242
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1233-1242
    • Nunnari, J.1    Marshall, W.F.2    Straight, A.3    Murray, A.4    Sedat, J.W.5    Walter, P.6
  • 22
    • 33644843425 scopus 로고    scopus 로고
    • Mitochondria as a connected population: ensuring continuity of the mitochondrial genome during plant cell dedifferentiation through massive mitochondrial fusion
    • Sheahan M.B., McCurdy D.W., and Rose R.J. Mitochondria as a connected population: ensuring continuity of the mitochondrial genome during plant cell dedifferentiation through massive mitochondrial fusion. Plant J. 44 (2005) 744-755
    • (2005) Plant J. , vol.44 , pp. 744-755
    • Sheahan, M.B.1    McCurdy, D.W.2    Rose, R.J.3
  • 23
    • 0036906665 scopus 로고    scopus 로고
    • Mitochondrial fusion in human cells is efficient, requires the inner membrane potential, and is mediated by mitofusins
    • Legros F., Lombes A., Frachon P., and Rojo M. Mitochondrial fusion in human cells is efficient, requires the inner membrane potential, and is mediated by mitofusins. Mol. Biol. Cell 13 (2002) 4343-4354
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4343-4354
    • Legros, F.1    Lombes, A.2    Frachon, P.3    Rojo, M.4
  • 24
    • 0037434879 scopus 로고    scopus 로고
    • Fusion of mitochondria in mammalian cells is dependent on the mitochondrial inner membrane potential and independent of microtubules or actin
    • Mattenberger Y., James D.I., and Martinou J.C. Fusion of mitochondria in mammalian cells is dependent on the mitochondrial inner membrane potential and independent of microtubules or actin. FEBS Lett. 538 (2003) 53-59
    • (2003) FEBS Lett. , vol.538 , pp. 53-59
    • Mattenberger, Y.1    James, D.I.2    Martinou, J.C.3
  • 25
    • 1242307475 scopus 로고    scopus 로고
    • Quantitation of mitochondrial dynamics by photolabeling of individual organelles shows that mitochondrial fusion is blocked during the Bax activation phase of apoptosis
    • Karbowski M., Arnoult D., Chen H., Chan D.C., Smith C.L., and Youle R.J. Quantitation of mitochondrial dynamics by photolabeling of individual organelles shows that mitochondrial fusion is blocked during the Bax activation phase of apoptosis. J. Cell Biol. 164 (2004) 493-499
    • (2004) J. Cell Biol. , vol.164 , pp. 493-499
    • Karbowski, M.1    Arnoult, D.2    Chen, H.3    Chan, D.C.4    Smith, C.L.5    Youle, R.J.6
  • 26
    • 4544378532 scopus 로고    scopus 로고
    • Mitochondrial fusion intermediates revealed in vitro
    • Meeusen S., McCaffery J.M., and Nunnari J. Mitochondrial fusion intermediates revealed in vitro. Science 305 (2004) 1747-1752
    • (2004) Science , vol.305 , pp. 1747-1752
    • Meeusen, S.1    McCaffery, J.M.2    Nunnari, J.3
  • 27
    • 0035911154 scopus 로고    scopus 로고
    • Connection of the mitochondrial outer and inner membranes by Fzo1 is critical for organellar fusion
    • Fritz S., Rapaport D., Klanner E., Neupert W., and Westermann B. Connection of the mitochondrial outer and inner membranes by Fzo1 is critical for organellar fusion. J. Cell Biol. 152 (2001) 683-692
    • (2001) J. Cell Biol. , vol.152 , pp. 683-692
    • Fritz, S.1    Rapaport, D.2    Klanner, E.3    Neupert, W.4    Westermann, B.5
  • 28
    • 0742288598 scopus 로고    scopus 로고
    • The dynamin superfamily: universal membrane tubulation and fission molecules?
    • Praefcke G.J., and McMahon H.T. The dynamin superfamily: universal membrane tubulation and fission molecules?. Nat. Rev., Mol. Cell Biol. 5 (2004) 133-147
    • (2004) Nat. Rev., Mol. Cell Biol. , vol.5 , pp. 133-147
    • Praefcke, G.J.1    McMahon, H.T.2
  • 29
    • 0142058391 scopus 로고    scopus 로고
    • Two mitofusin proteins, mammalian homologues of FZO, with distinct functions are both required for mitochondrial fusion
    • Eura Y., Ishihara N., Yokota S., and Mihara K. Two mitofusin proteins, mammalian homologues of FZO, with distinct functions are both required for mitochondrial fusion. J. Biochem. (Tokyo) 134 (2003) 333-344
    • (2003) J. Biochem. (Tokyo) , vol.134 , pp. 333-344
    • Eura, Y.1    Ishihara, N.2    Yokota, S.3    Mihara, K.4
  • 30
    • 0037089084 scopus 로고    scopus 로고
    • Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo
    • Rojo M., Legros F., Chateau D., and Lombes A. Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo. J. Cell Sci. 115 (2002) 1663-1674
    • (2002) J. Cell Sci. , vol.115 , pp. 1663-1674
    • Rojo, M.1    Legros, F.2    Chateau, D.3    Lombes, A.4
  • 31
    • 23844545553 scopus 로고    scopus 로고
    • Mutational analysis of action of mitochondrial fusion factor mitofusin-2
    • Honda S., Aihara T., Hontani M., Okubo K., and Hirose S. Mutational analysis of action of mitochondrial fusion factor mitofusin-2. J. Cell Sci. 118 (2005) 3153-3161
    • (2005) J. Cell Sci. , vol.118 , pp. 3153-3161
    • Honda, S.1    Aihara, T.2    Hontani, M.3    Okubo, K.4    Hirose, S.5
  • 33
    • 13444287961 scopus 로고    scopus 로고
    • Mitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity
    • Ishihara N., Eura Y., and Mihara K. Mitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity. J. Cell Sci. 117 (2004) 6535-6546
    • (2004) J. Cell Sci. , vol.117 , pp. 6535-6546
    • Ishihara, N.1    Eura, Y.2    Mihara, K.3
  • 35
    • 0033279836 scopus 로고    scopus 로고
    • SCF and Cullin/Ring H2-based ubiquitin ligases
    • Deshaies R.J. SCF and Cullin/Ring H2-based ubiquitin ligases. Annu. Rev. Cell Dev. Biol. 15 (1999) 435-467
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 435-467
    • Deshaies, R.J.1
  • 36
    • 0038037754 scopus 로고    scopus 로고
    • Mdm30 is an F-box protein required for maintenance of fusion-competent mitochondria in yeast
    • Fritz S., Weinbach N., and Westermann B. Mdm30 is an F-box protein required for maintenance of fusion-competent mitochondria in yeast. Mol. Biol. Cell 14 (2003) 2303-2313
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2303-2313
    • Fritz, S.1    Weinbach, N.2    Westermann, B.3
  • 37
    • 21444442598 scopus 로고    scopus 로고
    • Instability of the mitofusin Fzo1 regulates mitochondrial morphology during the mating response of the yeast Saccharomyces cerevisiae
    • Neutzner A., and Youle R.J. Instability of the mitofusin Fzo1 regulates mitochondrial morphology during the mating response of the yeast Saccharomyces cerevisiae. J. Biol. Chem. 280 (2005) 18598-18603
    • (2005) J. Biol. Chem. , vol.280 , pp. 18598-18603
    • Neutzner, A.1    Youle, R.J.2
  • 38
    • 0038376024 scopus 로고    scopus 로고
    • Mgm1p, a dynamin-related GTPase, is essential for fusion of the mitochondrial outer membrane
    • Sesaki H., Southard S.M., Yaffe M.P., and Jensen R.E. Mgm1p, a dynamin-related GTPase, is essential for fusion of the mitochondrial outer membrane. Mol. Biol. Cell 14 (2003) 2342-2356
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2342-2356
    • Sesaki, H.1    Southard, S.M.2    Yaffe, M.P.3    Jensen, R.E.4
  • 39
    • 0037415638 scopus 로고    scopus 로고
    • The intramitochondrial dynamin-related GTPase, Mgm1p, is a component of a protein complex that mediates mitochondrial fusion
    • Wong E.D., Wagner J.A., Scott S.V., Okreglak V., Holewinske T.J., Cassidy-Stone A., and Nunnari J. The intramitochondrial dynamin-related GTPase, Mgm1p, is a component of a protein complex that mediates mitochondrial fusion. J. Cell. Biol. 160 (2003) 303-311
    • (2003) J. Cell. Biol. , vol.160 , pp. 303-311
    • Wong, E.D.1    Wagner, J.A.2    Scott, S.V.3    Okreglak, V.4    Holewinske, T.J.5    Cassidy-Stone, A.6    Nunnari, J.7
  • 40
    • 2442421118 scopus 로고    scopus 로고
    • Loss of the intermembrane space protein Mgm1/OPA1 induces swelling and localized constrictions along the lengths of mitochondria
    • Griparic L., van der Wel N.N., Orozco I.J., Peters P.J., and van der Bliek A.M. Loss of the intermembrane space protein Mgm1/OPA1 induces swelling and localized constrictions along the lengths of mitochondria. J. Biol. Chem. 279 (2004) 18792-18798
    • (2004) J. Biol. Chem. , vol.279 , pp. 18792-18798
    • Griparic, L.1    van der Wel, N.N.2    Orozco, I.J.3    Peters, P.J.4    van der Bliek, A.M.5
  • 43
    • 0042526632 scopus 로고    scopus 로고
    • Processing of Mgm1 by the rhomboid-type protease Pcp1 is required for maintenance of mitochondrial morphology and of mitochondrial DNA
    • Herlan M., Vogel F., Bornhovd C., Neupert W., and Reichert A.S. Processing of Mgm1 by the rhomboid-type protease Pcp1 is required for maintenance of mitochondrial morphology and of mitochondrial DNA. J. Biol. Chem. 278 (2003) 27781-27788
    • (2003) J. Biol. Chem. , vol.278 , pp. 27781-27788
    • Herlan, M.1    Vogel, F.2    Bornhovd, C.3    Neupert, W.4    Reichert, A.S.5
  • 44
    • 0038700756 scopus 로고    scopus 로고
    • Mitochondrial membrane remodelling regulated by a conserved rhomboid protease
    • McQuibban G.A., Saurya S., and Freeman M. Mitochondrial membrane remodelling regulated by a conserved rhomboid protease. Nature 423 (2003) 537-541
    • (2003) Nature , vol.423 , pp. 537-541
    • McQuibban, G.A.1    Saurya, S.2    Freeman, M.3
  • 45
    • 0043095416 scopus 로고    scopus 로고
    • Cells lacking Pcp1p/Ugo2p, a rhomboid-like protease required for Mgm1p processing, lose mtDNA and mitochondrial structure in a Dnm1p-dependent manner, but remain competent for mitochondrial fusion
    • Sesaki H., Southard S.M., Hobbs A.E., and Jensen R.E. Cells lacking Pcp1p/Ugo2p, a rhomboid-like protease required for Mgm1p processing, lose mtDNA and mitochondrial structure in a Dnm1p-dependent manner, but remain competent for mitochondrial fusion. Biochem. Biophys. Res. Commun. 308 (2003) 276-283
    • (2003) Biochem. Biophys. Res. Commun. , vol.308 , pp. 276-283
    • Sesaki, H.1    Southard, S.M.2    Hobbs, A.E.3    Jensen, R.E.4
  • 46
    • 2142710081 scopus 로고    scopus 로고
    • Alternative topogenesis of Mgm1 and mitochondrial morphology depend on ATP and a functional import motor
    • Herlan M., Bornhovd C., Hell K., Neupert W., and Reichert A.S. Alternative topogenesis of Mgm1 and mitochondrial morphology depend on ATP and a functional import motor. J. Cell Biol. 165 (2004) 167-173
    • (2004) J. Cell Biol. , vol.165 , pp. 167-173
    • Herlan, M.1    Bornhovd, C.2    Hell, K.3    Neupert, W.4    Reichert, A.S.5
  • 47
    • 0035913908 scopus 로고    scopus 로고
    • Drosophila rhomboid-1 defines a family of putative intramembrane serine proteases
    • Urban S., Lee J.R., and Freeman M. Drosophila rhomboid-1 defines a family of putative intramembrane serine proteases. Cell 107 (2001) 173-182
    • (2001) Cell , vol.107 , pp. 173-182
    • Urban, S.1    Lee, J.R.2    Freeman, M.3
  • 48
    • 0033593816 scopus 로고    scopus 로고
    • The yeast dynamin-like protein, Mgm1p, functions on the mitochondrial outer membrane to mediate mitochondrial inheritance
    • Shepard K.A., and Yaffe M.P. The yeast dynamin-like protein, Mgm1p, functions on the mitochondrial outer membrane to mediate mitochondrial inheritance. J. Cell Biol. 144 (1999) 711-720
    • (1999) J. Cell Biol. , vol.144 , pp. 711-720
    • Shepard, K.A.1    Yaffe, M.P.2
  • 49
    • 27444446030 scopus 로고    scopus 로고
    • Release of OPA1 during apoptosis participates in the rapid and complete release of cytochrome c and subsequent mitochondrial fragmentation
    • Arnoult D., Grodet A., Lee Y.J., Estaquier J., and Blackstone C. Release of OPA1 during apoptosis participates in the rapid and complete release of cytochrome c and subsequent mitochondrial fragmentation. J. Biol. Chem. 280 (2005) 35742-35750
    • (2005) J. Biol. Chem. , vol.280 , pp. 35742-35750
    • Arnoult, D.1    Grodet, A.2    Lee, Y.J.3    Estaquier, J.4    Blackstone, C.5
  • 50
    • 0037427529 scopus 로고    scopus 로고
    • Differential sublocalization of the dynamin-related protein OPA1 isoforms in mitochondria
    • Satoh M., Hamamoto T., Seo N., Kagawa Y., and Endo H. Differential sublocalization of the dynamin-related protein OPA1 isoforms in mitochondria. Biochem. Biophys. Res. Commun. 300 (2003) 482-493
    • (2003) Biochem. Biophys. Res. Commun. , vol.300 , pp. 482-493
    • Satoh, M.1    Hamamoto, T.2    Seo, N.3    Kagawa, Y.4    Endo, H.5
  • 51
    • 0035149539 scopus 로고    scopus 로고
    • Division of mitochondria requires a novel DMN1-interacting protein, Net2p
    • Cerveny K.L., McCaffery J.M., and Jensen R.E. Division of mitochondria requires a novel DMN1-interacting protein, Net2p. Mol. Biol. Cell 12 (2001) 309-321
    • (2001) Mol. Biol. Cell , vol.12 , pp. 309-321
    • Cerveny, K.L.1    McCaffery, J.M.2    Jensen, R.E.3
  • 52
    • 0034676062 scopus 로고    scopus 로고
    • Gag3p, an outer membrane protein required for fission of mitochondrial tubules
    • Fekkes P., Shepard K.A., and Yaffe M.P. Gag3p, an outer membrane protein required for fission of mitochondrial tubules. J. Cell Biol. 151 (2000) 333-340
    • (2000) J. Cell Biol. , vol.151 , pp. 333-340
    • Fekkes, P.1    Shepard, K.A.2    Yaffe, M.P.3
  • 53
    • 0034676096 scopus 로고    scopus 로고
    • Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p
    • Mozdy A.D., McCaffery J.M., and Shaw J.M. Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p. J. Cell Biol. 151 (2000) 367-380
    • (2000) J. Cell Biol. , vol.151 , pp. 367-380
    • Mozdy, A.D.1    McCaffery, J.M.2    Shaw, J.M.3
  • 54
    • 0034676101 scopus 로고    scopus 로고
    • Mdv1p is a WD repeat protein that interacts with the dynamin-related GTPase, Dnm1p, to trigger mitochondrial division
    • Tieu Q., and Nunnari J. Mdv1p is a WD repeat protein that interacts with the dynamin-related GTPase, Dnm1p, to trigger mitochondrial division. J. Cell Biol. 151 (2000) 353-366
    • (2000) J. Cell Biol. , vol.151 , pp. 353-366
    • Tieu, Q.1    Nunnari, J.2
  • 55
    • 0035911963 scopus 로고    scopus 로고
    • UGO1 encodes an outer membrane protein required for mitochondrial fusion
    • Sesaki H., and Jensen R.E. UGO1 encodes an outer membrane protein required for mitochondrial fusion. J. Cell Biol. 152 (2001) 1123-1134
    • (2001) J. Cell Biol. , vol.152 , pp. 1123-1134
    • Sesaki, H.1    Jensen, R.E.2
  • 56
    • 3142546895 scopus 로고    scopus 로고
    • Ugo1p links the Fzo1p and Mgm1p GTPases for mitochondrial fusion
    • Sesaki H., and Jensen R.E. Ugo1p links the Fzo1p and Mgm1p GTPases for mitochondrial fusion. J. Biol. Chem. 279 (2004) 28298-28303
    • (2004) J. Biol. Chem. , vol.279 , pp. 28298-28303
    • Sesaki, H.1    Jensen, R.E.2
  • 57
    • 11244258475 scopus 로고    scopus 로고
    • Interdependent assembly of specific regulatory lipids and membrane fusion proteins into the vertex ring domain of docked vacuoles
    • Fratti R.A., Jun Y., Merz A.J., Margolis N., and Wickner W. Interdependent assembly of specific regulatory lipids and membrane fusion proteins into the vertex ring domain of docked vacuoles. J. Cell. Biol. 167 (2004) 1087-1098
    • (2004) J. Cell. Biol. , vol.167 , pp. 1087-1098
    • Fratti, R.A.1    Jun, Y.2    Merz, A.J.3    Margolis, N.4    Wickner, W.5
  • 58
    • 0035423116 scopus 로고    scopus 로고
    • Ergosterol is required for the Sec18/ATP-dependent priming step of homotypic vacuole fusion
    • Kato M., and Wickner W. Ergosterol is required for the Sec18/ATP-dependent priming step of homotypic vacuole fusion. EMBO J. 20 (2001) 4035-4040
    • (2001) EMBO J. , vol.20 , pp. 4035-4040
    • Kato, M.1    Wickner, W.2
  • 60
    • 0037459089 scopus 로고    scopus 로고
    • Regulation of mitochondrial morphology by membrane potential, and DRP1-dependent division and FZO1-dependent fusion reaction in mammalian cells
    • Ishihara N., Jofuku A., Eura Y., and Mihara K. Regulation of mitochondrial morphology by membrane potential, and DRP1-dependent division and FZO1-dependent fusion reaction in mammalian cells. Biochem. Biophys. Res. Commun. 301 (2003) 891-898
    • (2003) Biochem. Biophys. Res. Commun. , vol.301 , pp. 891-898
    • Ishihara, N.1    Jofuku, A.2    Eura, Y.3    Mihara, K.4
  • 61
    • 3242884720 scopus 로고    scopus 로고
    • Organization and dynamics of human mitochondrial DNA
    • Legros F., Malka F., Frachon P., Lombes A., and Rojo M. Organization and dynamics of human mitochondrial DNA. J. Cell. Sci. 117 (2004) 2653-2662
    • (2004) J. Cell. Sci. , vol.117 , pp. 2653-2662
    • Legros, F.1    Malka, F.2    Frachon, P.3    Lombes, A.4    Rojo, M.5
  • 63
    • 27644467457 scopus 로고    scopus 로고
    • Role of essential genes in mitochondrial morphogenesis in Saccharomyces cerevisiae
    • Altmann K., and Westermann B. Role of essential genes in mitochondrial morphogenesis in Saccharomyces cerevisiae. Mol. Biol. Cell 16 (2005) 5410-5417
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5410-5417
    • Altmann, K.1    Westermann, B.2


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