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Volumn 1833, Issue 5, 2013, Pages 1256-1268

New insights into the function and regulation of mitochondrial fission

Author keywords

Apoptosis; Drp1; Mitochondrial fission; Mitophagy; Neurodegenerative disease; Post translational modification

Indexed keywords

DYNAMIN I; ELONGATION FACTOR 1; GUANOSINE TRIPHOSPHATASE; HUNTINGTIN; LEUCINE RICH REPEAT KINASE 2; MITOCHONDRIAL DNA;

EID: 84875273810     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2013.02.002     Document Type: Review
Times cited : (378)

References (189)
  • 3
    • 23844558266 scopus 로고    scopus 로고
    • A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine
    • Wallace D.C. A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine. Annu. Rev. Genet. 2005, 39:359-407.
    • (2005) Annu. Rev. Genet. , vol.39 , pp. 359-407
    • Wallace, D.C.1
  • 4
    • 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
  • 5
    • 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
  • 6
    • 34250204271 scopus 로고    scopus 로고
    • The machines that divide and fuse mitochondria
    • Hoppins S., Lackner L., Nunnari J. The machines that divide and fuse mitochondria. Annu. Rev. Biochem. 2007, 76:751-780.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 751-780
    • Hoppins, S.1    Lackner, L.2    Nunnari, J.3
  • 7
    • 67650868959 scopus 로고    scopus 로고
    • Mitochondrial dynamics in mammalian health and disease
    • Liesa M., Palacin M., Zorzano A. Mitochondrial dynamics in mammalian health and disease. Physiol. Rev. 2009, 89:799-845.
    • (2009) Physiol. Rev. , vol.89 , pp. 799-845
    • Liesa, M.1    Palacin, M.2    Zorzano, A.3
  • 8
    • 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
  • 9
    • 45349094984 scopus 로고    scopus 로고
    • Mitochondrial dynamics and apoptosis
    • Suen D.F., Norris K.L., Youle R.J. Mitochondrial dynamics and apoptosis. Genes Dev. 2008, 22:1577-1590.
    • (2008) Genes Dev. , vol.22 , pp. 1577-1590
    • Suen, D.F.1    Norris, K.L.2    Youle, R.J.3
  • 10
    • 33745952665 scopus 로고    scopus 로고
    • Mitochondrial trafficking to synapse in cultured primary cortical neurons
    • Chang D.T., Honick A.S., Reynolds I.J. Mitochondrial trafficking to synapse in cultured primary cortical neurons. J. Neurosci. 2006, 26:7035-7045.
    • (2006) J. Neurosci. , vol.26 , pp. 7035-7045
    • Chang, D.T.1    Honick, A.S.2    Reynolds, I.J.3
  • 11
    • 10944269186 scopus 로고    scopus 로고
    • The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapse
    • Li Z., Okamoto K., Hayashi Y., Sheng M. The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapse. Cell 2004, 119:873-887.
    • (2004) Cell , vol.119 , pp. 873-887
    • Li, Z.1    Okamoto, K.2    Hayashi, Y.3    Sheng, M.4
  • 12
    • 30544452263 scopus 로고    scopus 로고
    • The axonal transport of mitochondria
    • Hollenbeck P.J., Saxton W.M. The axonal transport of mitochondria. J. Cell Sci. 2005, 118:5411-5419.
    • (2005) J. Cell Sci. , vol.118 , pp. 5411-5419
    • Hollenbeck, P.J.1    Saxton, W.M.2
  • 13
    • 84862870271 scopus 로고    scopus 로고
    • The axonal transport of mitochondria
    • Saxton W.M., Hollenbeck P.J. The axonal transport of mitochondria. J. Cell Sci. 2012, 125:2095-2104.
    • (2012) J. Cell Sci. , vol.125 , pp. 2095-2104
    • Saxton, W.M.1    Hollenbeck, P.J.2
  • 14
    • 0035057837 scopus 로고    scopus 로고
    • Control of mitochondrial morphology by a human mitofusin
    • Santel A., Fuller M.T. Control of mitochondrial morphology by a human mitofusin. J. Cell Sci. 2001, 114:867-874.
    • (2001) J. Cell Sci. , vol.114 , pp. 867-874
    • Santel, A.1    Fuller, M.T.2
  • 15
    • 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., Rojo M. Mitochondrial fusion in human cells is efficient, requires the inner membrane potential, and is mediated by mitofusins. Mol. Biol. Cell 2002, 12:4343-4354.
    • (2002) Mol. Biol. Cell , vol.12 , pp. 4343-4354
    • Legros, F.1    Lombes, A.2    Frachon, P.3    Rojo, M.4
  • 16
    • 0038783254 scopus 로고    scopus 로고
    • Mitofusin-1 is a generally expressed mediator of mitochondrial fusion in mammalian cells
    • Santel A., Frank S., Gaume B., Herrler M., Youle R.J., Fuller M.T. Mitofusin-1 is a generally expressed mediator of mitochondrial fusion in mammalian cells. J. Cell Sci. 2003, 116:2763-2774.
    • (2003) J. Cell Sci. , vol.116 , pp. 2763-2774
    • Santel, A.1    Frank, S.2    Gaume, B.3    Herrler, M.4    Youle, R.J.5    Fuller, M.T.6
  • 17
    • 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., Mihara K. Two mitofusin proteins, mammalian homologues of FZO, with distinct functions are both required for mitochondrial fusion. J. Biochem. 2003, 134:333-344.
    • (2003) J. Biochem. , vol.134 , pp. 333-344
    • Eura, Y.1    Ishihara, N.2    Yokota, S.3    Mihara, K.4
  • 18
    • 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., Chan D.C. Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development. J. Cell Biol. 2003, 160:189-200.
    • (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
  • 19
    • 0037424239 scopus 로고    scopus 로고
    • Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis
    • Olichon A., Baricault L., Gas N., Guillou E., Valette A., Belenguer P., Lenaers G. Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis. J. Biol. Chem. 2003, 278:7743-7746.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7743-7746
    • Olichon, A.1    Baricault, L.2    Gas, N.3    Guillou, E.4    Valette, A.5    Belenguer, P.6    Lenaers, G.7
  • 23
    • 0035166814 scopus 로고    scopus 로고
    • Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells
    • Smirnova E., Griparic L., Shurland D.L., van der Bliek A.M. Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells. Mol. Biol. Cell 2001, 12:2245-2256.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2245-2256
    • Smirnova, E.1    Griparic, L.2    Shurland, D.L.3    van der Bliek, A.M.4
  • 24
    • 0035166812 scopus 로고    scopus 로고
    • Mammalian dynamin-like protein DLP1 tubulates membranes
    • Yoon Y., Pitts K.R., McNiven M.A. Mammalian dynamin-like protein DLP1 tubulates membranes. Mol. Biol. Cell 2001, 12:2894-2905.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2894-2905
    • Yoon, Y.1    Pitts, K.R.2    McNiven, M.A.3
  • 26
    • 0033571410 scopus 로고    scopus 로고
    • Division versus fusion: Dnm1 and Fzo1 antagonistically regulate mitochondrial shape
    • Sesaki H., Jesen R.E. Division versus fusion: Dnm1 and Fzo1 antagonistically regulate mitochondrial shape. J. Cell Biol. 1999, 147:699-706.
    • (1999) J. Cell Biol. , vol.147 , pp. 699-706
    • Sesaki, H.1    Jesen, R.E.2
  • 27
    • 79958819666 scopus 로고    scopus 로고
    • Discovery of membrane receptor for mitochondrial fission GTPase Drp1
    • Otera H., Mihara K. Discovery of membrane receptor for mitochondrial fission GTPase Drp1. Small GTPases 2011, 3:167-172.
    • (2011) Small GTPases , vol.3 , pp. 167-172
    • Otera, H.1    Mihara, K.2
  • 28
    • 84871802627 scopus 로고    scopus 로고
    • Recent advances into the understanding of mitochondrial fission
    • Elgass K., Pakay J., Ryan M.T., Palmer C.S. Recent advances into the understanding of mitochondrial fission. Biochim. Biophys. Acta 2013, 1833:150-161.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 150-161
    • Elgass, K.1    Pakay, J.2    Ryan, M.T.3    Palmer, C.S.4
  • 29
    • 84875213589 scopus 로고    scopus 로고
    • Regulation of mitochondrial dynamics: convergences an divergences between yeast and vertebrates
    • Zhao J., Lendahl U., Nister M. Regulation of mitochondrial dynamics: convergences an divergences between yeast and vertebrates. Cell. Mol. Life Sci. 2012, 10.1007/s00018-012-1066-6.
    • (2012) Cell. Mol. Life Sci.
    • Zhao, J.1    Lendahl, U.2    Nister, M.3
  • 30
    • 77955298543 scopus 로고    scopus 로고
    • Dynamic regulation of mitochondrial fission through modification of the dynamin-related protein Drp1
    • Chang C.R., Blackstone C. Dynamic regulation of mitochondrial fission through modification of the dynamin-related protein Drp1. Ann. N. Y. Acad. Sci. 2010, 1201:34-39.
    • (2010) Ann. N. Y. Acad. Sci. , vol.1201 , pp. 34-39
    • Chang, C.R.1    Blackstone, C.2
  • 31
    • 84875250591 scopus 로고    scopus 로고
    • Mitochondrial morphology in metabolic diseases, Antioxid. Redox Signal. (in press) (August 2012, ahead of print).
    • C.A. Galloway, Y. Yoon, Mitochondrial morphology in metabolic diseases, Antioxid. Redox Signal. (in press) (August 2012, ahead of print).
    • Galloway, C.A.1    Yoon, Y.2
  • 32
    • 77951096150 scopus 로고    scopus 로고
    • Mitochondrial dynamics-fusion, fission, movement, and mitophagy-in neurodegenerative diseases
    • Chen M., Chan D.C. Mitochondrial dynamics-fusion, fission, movement, and mitophagy-in neurodegenerative diseases. Hum. Mol. Genet. 2009, 18:R169-R176.
    • (2009) Hum. Mol. Genet. , vol.18
    • Chen, M.1    Chan, D.C.2
  • 33
    • 0034676096 scopus 로고    scopus 로고
    • Dnm1 GTPase-mediated mitochondrial fission is a multistep process requiring the novel integral membrane component Fis1p
    • Mozdy A.D., McCaffery J.M., Shaw J.M. Dnm1 GTPase-mediated mitochondrial fission is a multistep process requiring the novel integral membrane component Fis1p. J. Cell Biol. 2000, 151:367-380.
    • (2000) J. Cell Biol. , vol.151 , pp. 367-380
    • Mozdy, A.D.1    McCaffery, J.M.2    Shaw, J.M.3
  • 36
    • 27544450920 scopus 로고    scopus 로고
    • The role of Fis1p-Mdv1p interactions in mitochondrial fission complex assembly
    • Karren M.A., Coonrod E.M., Anderson T.K., Shaw J.M. The role of Fis1p-Mdv1p interactions in mitochondrial fission complex assembly. J. Cell Biol. 2005, 171:291-301.
    • (2005) J. Cell Biol. , vol.171 , pp. 291-301
    • Karren, M.A.1    Coonrod, E.M.2    Anderson, T.K.3    Shaw, J.M.4
  • 37
    • 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., Nunnari J. Mdv1p is a WD repeat protein that interacts with the dynamin-related GTPase, Dnm1p, to trigger mitochondrial division. J. Cell Biol. 2000, 151:353-366.
    • (2000) J. Cell Biol. , vol.151 , pp. 353-366
    • Tieu, Q.1    Nunnari, J.2
  • 38
    • 22944440071 scopus 로고    scopus 로고
    • The WD40 protein Caf4p is a component of the mitochondrial fission machinery and recruits Dnm1p to mitochondria
    • Griffin E.E., Graumann J., Chan D.C. The WD40 protein Caf4p is a component of the mitochondrial fission machinery and recruits Dnm1p to mitochondria. J. Cell Biol. 2005, 170:237-248.
    • (2005) J. Cell Biol. , vol.170 , pp. 237-248
    • Griffin, E.E.1    Graumann, J.2    Chan, D.C.3
  • 39
    • 71849086878 scopus 로고    scopus 로고
    • The molecular mechanism and cellular functions of mitochondrial division
    • Lackner L.L., Nunnari J.M. The molecular mechanism and cellular functions of mitochondrial division. Biochim. Biophys. Acta 2009, 1792:1138-1144.
    • (2009) Biochim. Biophys. Acta , vol.1792 , pp. 1138-1144
    • Lackner, L.L.1    Nunnari, J.M.2
  • 40
    • 68949217889 scopus 로고    scopus 로고
    • Mechanistic analysis of a dynamin effector
    • Lackner L.L., Horner J.S., Nunnari J. Mechanistic analysis of a dynamin effector. Science 2009, 325:874-877.
    • (2009) Science , vol.325 , pp. 874-877
    • Lackner, L.L.1    Horner, J.S.2    Nunnari, J.3
  • 41
    • 78650155696 scopus 로고    scopus 로고
    • Molecular architecture of a dynamin adaptor: implications for assembly of mitochondrial fission complexes
    • Koirala S., Bui H.T., Schubert H.L., Eckert D.M., Hill C.P., Kay M.S., Shaw J.M. Molecular architecture of a dynamin adaptor: implications for assembly of mitochondrial fission complexes. J. Cell Biol. 2010, 191:1127-1139.
    • (2010) J. Cell Biol. , vol.191 , pp. 1127-1139
    • Koirala, S.1    Bui, H.T.2    Schubert, H.L.3    Eckert, D.M.4    Hill, C.P.5    Kay, M.S.6    Shaw, J.M.7
  • 42
    • 84858966461 scopus 로고    scopus 로고
    • Crystal structure of mitochondrial fission complex reveals scaffolding function for mitochondrial division 1 (Mdv1) coiled coil
    • Zhang Y., Chan N.C., Ngo H.B., Gristich H., Chan D.C. Crystal structure of mitochondrial fission complex reveals scaffolding function for mitochondrial division 1 (Mdv1) coiled coil. J. Biol. Chem. 2012, 287:9855-9861.
    • (2012) J. Biol. Chem. , vol.287 , pp. 9855-9861
    • Zhang, Y.1    Chan, N.C.2    Ngo, H.B.3    Gristich, H.4    Chan, D.C.5
  • 43
    • 0036322806 scopus 로고    scopus 로고
    • The WD repeat protein, Mdv1p, functions as a molecular adaptor by interacting with Dnm1p and Fis1p during mitochondrial fission
    • Tieu Q., Okreglak V., Naylor K., Nunnari J. The WD repeat protein, Mdv1p, functions as a molecular adaptor by interacting with Dnm1p and Fis1p during mitochondrial fission. J. Cell Biol. 2002, 158:445-452.
    • (2002) J. Cell Biol. , vol.158 , pp. 445-452
    • Tieu, Q.1    Okreglak, V.2    Naylor, K.3    Nunnari, J.4
  • 44
    • 84872012439 scopus 로고    scopus 로고
    • A novel motif in the yeast mitochondrial dynamin Dnm1 is essential for adaptor binding and membrane recruitment
    • Bui H.T., Karren M.A., Bhar D., Shaw J.M. A novel motif in the yeast mitochondrial dynamin Dnm1 is essential for adaptor binding and membrane recruitment. J. Cell Biol. 2012, 199:613-622.
    • (2012) J. Cell Biol. , vol.199 , pp. 613-622
    • Bui, H.T.1    Karren, M.A.2    Bhar, D.3    Shaw, J.M.4
  • 45
    • 33745221197 scopus 로고    scopus 로고
    • Dimeric Dnm1-G385D interacts with Mdv1 on mitochondria and can be stimulated to assemble into fission complexes containing Mdv1 and Fis1
    • Bhar D., Karren M.A., Babst M., Shaw J.M. Dimeric Dnm1-G385D interacts with Mdv1 on mitochondria and can be stimulated to assemble into fission complexes containing Mdv1 and Fis1. J. Biol. Chem. 2006, 281:17312-17320.
    • (2006) J. Biol. Chem. , vol.281 , pp. 17312-17320
    • Bhar, D.1    Karren, M.A.2    Babst, M.3    Shaw, J.M.4
  • 46
    • 33847212405 scopus 로고    scopus 로고
    • Yeast mitochondrial division and distribution require the cortical num1 protein
    • Cerveny K.L., Studer S.L., Jensen R.E., Sesaki H. Yeast mitochondrial division and distribution require the cortical num1 protein. Dev. Cell 2007, 12:363-375.
    • (2007) Dev. Cell , vol.12 , pp. 363-375
    • Cerveny, K.L.1    Studer, S.L.2    Jensen, R.E.3    Sesaki, H.4
  • 47
    • 77954644760 scopus 로고    scopus 로고
    • Mdm36 is a mitochondrial fission-promoting protein in Saccharomyces cerevisiae
    • Hammermeister M., Schodel K., Westermann B. Mdm36 is a mitochondrial fission-promoting protein in Saccharomyces cerevisiae. Mol. Biol. Cell 2010, 21:2443-2452.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2443-2452
    • Hammermeister, M.1    Schodel, K.2    Westermann, B.3
  • 49
    • 0033105560 scopus 로고    scopus 로고
    • Functional diversity in the dynamin family
    • van der Bliek A.M. Functional diversity in the dynamin family. Trends Cell Biol. 1999, 9:96-102.
    • (1999) Trends Cell Biol. , vol.9 , pp. 96-102
    • van der Bliek, A.M.1
  • 50
    • 80052248915 scopus 로고    scopus 로고
    • Dynamin: functional design of a membrane fission catalyst
    • Schmid S.L., Frolov V.A. Dynamin: functional design of a membrane fission catalyst. Annu. Rev. Cell Dev. Biol. 2011, 27:79-105.
    • (2011) Annu. Rev. Cell Dev. Biol. , vol.27 , pp. 79-105
    • Schmid, S.L.1    Frolov, V.A.2
  • 51
    • 79960720320 scopus 로고    scopus 로고
    • Molecular mechanism and physiological functions of clathrin-mediated endocytosis
    • McMahon H.T., Boucrot E. Molecular mechanism and physiological functions of clathrin-mediated endocytosis. Nat. Rev. Mol. Cell Biol. 2011, 12:517-533.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 517-533
    • McMahon, H.T.1    Boucrot, E.2
  • 52
    • 0034784987 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of dynamin in the constricted state
    • Zhang P., Hinshaw J.E. Three-dimensional reconstruction of dynamin in the constricted state. Nat. Cell Biol. 2001, 10:922-926.
    • (2001) Nat. Cell Biol. , vol.10 , pp. 922-926
    • Zhang, P.1    Hinshaw, J.E.2
  • 53
  • 54
    • 80053376521 scopus 로고    scopus 로고
    • The crystal structure of dynamin
    • Ford M.G., Jenni S., Nunnari J. The crystal structure of dynamin. Nature 2011, 477:561-566.
    • (2011) Nature , vol.477 , pp. 561-566
    • Ford, M.G.1    Jenni, S.2    Nunnari, J.3
  • 56
    • 77953023419 scopus 로고    scopus 로고
    • G domain dimerization controls dynamin's assembly-stimulated GTPase activity
    • Chappie J.S., Acharya S., Leonard M., Schmid S.L., Dyda F. G domain dimerization controls dynamin's assembly-stimulated GTPase activity. Nature 2010, 465:435-440.
    • (2010) Nature , vol.465 , pp. 435-440
    • Chappie, J.S.1    Acharya, S.2    Leonard, M.3    Schmid, S.L.4    Dyda, F.5
  • 57
    • 64649093555 scopus 로고    scopus 로고
    • Mitochondrial fusion and division: regulation and role in cell viability
    • Benard G., Karbowski M. Mitochondrial fusion and division: regulation and role in cell viability. Semin. Cell Dev. Biol. 2009, 20:365-374.
    • (2009) Semin. Cell Dev. Biol. , vol.20 , pp. 365-374
    • Benard, G.1    Karbowski, M.2
  • 59
    • 81855189620 scopus 로고    scopus 로고
    • Organelle dynamics: ER embraces mitochondria for fission
    • Westermann B. Organelle dynamics: ER embraces mitochondria for fission. Curr. Biol. 2011, 21:R922-R924.
    • (2011) Curr. Biol. , vol.21
    • Westermann, B.1
  • 60
    • 84866728707 scopus 로고    scopus 로고
    • Endoplasmic reticulum-mitochondria contacts: function of the junction
    • Rowland A.A., Voeltz G.K. Endoplasmic reticulum-mitochondria contacts: function of the junction. Nat. Rev. Mol. Cell Biol. 2012, 13:607-625.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 607-625
    • Rowland, A.A.1    Voeltz, G.K.2
  • 61
    • 4143088384 scopus 로고    scopus 로고
    • Intra- and intermolecular domain interactions of the C-terminal GTPase effector domain of the multimeric dynamin-like GTPase Drp1
    • Zhu P.P., Patterson A., Stadler J., Seeburg D.P., Sheng M., Blackstone C. Intra- and intermolecular domain interactions of the C-terminal GTPase effector domain of the multimeric dynamin-like GTPase Drp1. J. Biol. Chem. 2004, 279:35967-35974.
    • (2004) J. Biol. Chem. , vol.279 , pp. 35967-35974
    • Zhu, P.P.1    Patterson, A.2    Stadler, J.3    Seeburg, D.P.4    Sheng, M.5    Blackstone, C.6
  • 62
    • 82955201673 scopus 로고    scopus 로고
    • Biochemical characterization of human dynamin-like protein 1
    • Zhang Y., Gao X., Garavito R.M. Biochemical characterization of human dynamin-like protein 1. J. Biochem. 2011, 150:627-633.
    • (2011) J. Biochem. , vol.150 , pp. 627-633
    • Zhang, Y.1    Gao, X.2    Garavito, R.M.3
  • 63
    • 0032937051 scopus 로고    scopus 로고
    • Essential role of the dynamin pleckstrin homology domain in receptor-mediated endocytosis
    • Achiriloaie M., Barylko B., Albanesi J.P. Essential role of the dynamin pleckstrin homology domain in receptor-mediated endocytosis. Mol. Cell. Biol. 1999, 19:1410-1415.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1410-1415
    • Achiriloaie, M.1    Barylko, B.2    Albanesi, J.P.3
  • 64
    • 0029978885 scopus 로고    scopus 로고
    • Identification of the binding site for acidic phospholipids on the pH domain of dynamin: implications for stimulation of GTPase activity
    • Zheng J., Cahill S.M., Lemmon M.A., Fushman D., Schlessinger J., Cowburn D. Identification of the binding site for acidic phospholipids on the pH domain of dynamin: implications for stimulation of GTPase activity. J. Mol. Biol. 1996, 255:14-21.
    • (1996) J. Mol. Biol. , vol.255 , pp. 14-21
    • Zheng, J.1    Cahill, S.M.2    Lemmon, M.A.3    Fushman, D.4    Schlessinger, J.5    Cowburn, D.6
  • 65
    • 73949099250 scopus 로고    scopus 로고
    • Membrane insertion of the pleckstrin homology domain variable loop 1 is critical for dynamin-catalyzed vesicle scission
    • Ramachandran R., Pucadyil T.J., Liu Y.W., Acharya S., Leonard M., Lukiyanchuk V., Schmid S.L. Membrane insertion of the pleckstrin homology domain variable loop 1 is critical for dynamin-catalyzed vesicle scission. Mol. Biol. Cell 2009, 20:4630-4639.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4630-4639
    • Ramachandran, R.1    Pucadyil, T.J.2    Liu, Y.W.3    Acharya, S.4    Leonard, M.5    Lukiyanchuk, V.6    Schmid, S.L.7
  • 66
    • 84858434492 scopus 로고    scopus 로고
    • Allosteric modulation of Drp1 mechanoenzyme assembly and mitochondrial fission by the variable domain
    • Strack S., Cribbs J.T. Allosteric modulation of Drp1 mechanoenzyme assembly and mitochondrial fission by the variable domain. J. Biol. Chem. 2012, 287:10990-101001.
    • (2012) J. Biol. Chem. , vol.287 , pp. 10990-101001
    • Strack, S.1    Cribbs, J.T.2
  • 67
    • 17144429793 scopus 로고    scopus 로고
    • Mitochondrial function and actin regulate dynamin-related protein 1-dependent mitochondrial fission
    • De Vos K.J., Allan V.J., Grierson A.J., Sheetz M.P. Mitochondrial function and actin regulate dynamin-related protein 1-dependent mitochondrial fission. Curr. Biol. 2005, 115:678-683.
    • (2005) Curr. Biol. , vol.115 , pp. 678-683
    • De Vos, K.J.1    Allan, V.J.2    Grierson, A.J.3    Sheetz, M.P.4
  • 68
    • 84865352799 scopus 로고    scopus 로고
    • Tau promotes neurodegeneration via DRP1 mislocalization in vivo
    • Duboff B., Gotz J., Feany M.B. Tau promotes neurodegeneration via DRP1 mislocalization in vivo. Neuron 2012, 75:618-632.
    • (2012) Neuron , vol.75 , pp. 618-632
    • Duboff, B.1    Gotz, J.2    Feany, M.B.3
  • 69
    • 5444236916 scopus 로고    scopus 로고
    • Cytoplasmic dynein regulates the subcellular distribution of mitochondria by controlling the recruitment of the fission factor dynamin-related protein-1
    • Varadi A., Johnson-Cadwell L.I., Cirulli V., Yoon Y., Allan V.J., Rutter G.A. Cytoplasmic dynein regulates the subcellular distribution of mitochondria by controlling the recruitment of the fission factor dynamin-related protein-1. J. Cell Sci. 2004, 117:4389-4400.
    • (2004) J. Cell Sci. , vol.117 , pp. 4389-4400
    • Varadi, A.1    Johnson-Cadwell, L.I.2    Cirulli, V.3    Yoon, Y.4    Allan, V.J.5    Rutter, G.A.6
  • 70
    • 6344274848 scopus 로고    scopus 로고
    • Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis
    • Lee Y.J., Jeong S.Y., Karbowski M., Smith C.L., Youle R.J. Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis. Mol. Biol. Cell 2004, 15:5001-5011.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5001-5011
    • Lee, Y.J.1    Jeong, S.Y.2    Karbowski, M.3    Smith, C.L.4    Youle, R.J.5
  • 71
    • 44649129342 scopus 로고    scopus 로고
    • The novel tail-anchored membrane protein Mff controls mitochondrial and peroxisomal fission in mammalian cells
    • Gandre-Babbe S., van der Bliek A.M. The novel tail-anchored membrane protein Mff controls mitochondrial and peroxisomal fission in mammalian cells. Mol. Biol. Cell 2008, 19:2402-2412.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2402-2412
    • Gandre-Babbe, S.1    van der Bliek, A.M.2
  • 72
    • 78650167618 scopus 로고    scopus 로고
    • Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells
    • Otera H., Wang C., Cleland M.M., Setoguchi K., Yokota S., Youle R.J., Mihara K. Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells. J. Cell Biol. 2010, 191:1141-1158.
    • (2010) J. Cell Biol. , vol.191 , pp. 1141-1158
    • Otera, H.1    Wang, C.2    Cleland, M.M.3    Setoguchi, K.4    Yokota, S.5    Youle, R.J.6    Mihara, K.7
  • 73
    • 33645747175 scopus 로고    scopus 로고
    • BIGYIN, an orthologue of human and yeast FIS1 genes functions in the control of mitochondrial size and number in Arabidopsis thaliana
    • Scott I., Tobin A.K., Logan D.C. BIGYIN, an orthologue of human and yeast FIS1 genes functions in the control of mitochondrial size and number in Arabidopsis thaliana. J. Exp. Bot. 2006, 57:1275-1280.
    • (2006) J. Exp. Bot. , vol.57 , pp. 1275-1280
    • Scott, I.1    Tobin, A.K.2    Logan, D.C.3
  • 74
    • 64649090145 scopus 로고    scopus 로고
    • FISSION1A and FISSION1B proteins mediate the fission of peroxisomes and mitochondria in Arabidopsis
    • Zhang X.C., Hu J.P. FISSION1A and FISSION1B proteins mediate the fission of peroxisomes and mitochondria in Arabidopsis. Mol. Plant 2008, 1:1036-1047.
    • (2008) Mol. Plant , vol.1 , pp. 1036-1047
    • Zhang, X.C.1    Hu, J.P.2
  • 75
    • 57749122081 scopus 로고    scopus 로고
    • Arabidopsis ELONGATED MITOCHONDRIA1 is required for localization of DYNAMIN-RELATED PROTEIN3A to mitochondrial fission sites
    • Arimura S., Fujimoto M., Doniwa Y., Kadoya N., Nakazono M., Sakamoto W., Tsutsumi N. Arabidopsis ELONGATED MITOCHONDRIA1 is required for localization of DYNAMIN-RELATED PROTEIN3A to mitochondrial fission sites. Plant Cell 2008, 20:1555-1566.
    • (2008) Plant Cell , vol.20 , pp. 1555-1566
    • Arimura, S.1    Fujimoto, M.2    Doniwa, Y.3    Kadoya, N.4    Nakazono, M.5    Sakamoto, W.6    Tsutsumi, N.7
  • 77
    • 79960621726 scopus 로고    scopus 로고
    • Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission
    • Zhao J., Liu T., Jin S., Wang X., Qu M., Uhlen P., Tomilin N., Shupliakov O., Lendahl U., Nister M. Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission. EMBO J. 2011, 30:2762-2778.
    • (2011) EMBO J. , vol.30 , pp. 2762-2778
    • Zhao, J.1    Liu, T.2    Jin, S.3    Wang, X.4    Qu, M.5    Uhlen, P.6    Tomilin, N.7    Shupliakov, O.8    Lendahl, U.9    Nister, M.10
  • 78
    • 0043092647 scopus 로고    scopus 로고
    • The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1
    • Yoon Y., Krueger E.W., Oswald B.J., McNiven M.A. The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1. Mol. Cell. Biol. 2003, 23:5409-5420.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5409-5420
    • Yoon, Y.1    Krueger, E.W.2    Oswald, B.J.3    McNiven, M.A.4
  • 79
    • 1842479419 scopus 로고    scopus 로고
    • Levels of human Fis1 at the mitochondrial outer membrane regulate mitochondrial morphology
    • Stojanovski D., Koutsopoulos O.S., Okamoto K., Ryan M.T. Levels of human Fis1 at the mitochondrial outer membrane regulate mitochondrial morphology. J. Cell Sci. 2004, 117:1201-1210.
    • (2004) J. Cell Sci. , vol.117 , pp. 1201-1210
    • Stojanovski, D.1    Koutsopoulos, O.S.2    Okamoto, K.3    Ryan, M.T.4
  • 80
    • 0141592470 scopus 로고    scopus 로고
    • HFis1, a novel component of mammalian mitochondrial fission machinery
    • James D.I., Parone P.A., Mattenberger Y., Martinou J.C. hFis1, a novel component of mammalian mitochondrial fission machinery. J. Biol. Chem. 2003, 278:36373-36379.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36373-36379
    • James, D.I.1    Parone, P.A.2    Mattenberger, Y.3    Martinou, J.C.4
  • 81
    • 0242579164 scopus 로고    scopus 로고
    • The solution structure of human mitochondria fission protein Fis1 reveals a novel TPR-like helix bundle
    • Suzuki M., Jeong S-Y., Karbowski M., Youle R.J., Tjandra N. The solution structure of human mitochondria fission protein Fis1 reveals a novel TPR-like helix bundle. J. Mol. Biol. 2003, 334:445-458.
    • (2003) J. Mol. Biol. , vol.334 , pp. 445-458
    • Suzuki, M.1    Jeong, S.-Y.2    Karbowski, M.3    Youle, R.J.4    Tjandra, N.5
  • 82
    • 58149120882 scopus 로고    scopus 로고
    • Two small protein families, DYNAMIN-RELATED PROTEIN3 and FISSION1, are required for peroxisome fission in Arabidopsis
    • Zhang X., Hu J. Two small protein families, DYNAMIN-RELATED PROTEIN3 and FISSION1, are required for peroxisome fission in Arabidopsis. Plant J. 2009, 57:146-159.
    • (2009) Plant J. , vol.57 , pp. 146-159
    • Zhang, X.1    Hu, J.2
  • 83
    • 49349100454 scopus 로고    scopus 로고
    • Caenorhabditis elegans drp-1 and fis-2 regulate distinct cell-death execution pathways downstream of ced-3 and independent of ced-9
    • Breckenridge D.G., Kang B.H., Kokel D., Mitani S., Staehelin L.A., Xue D. Caenorhabditis elegans drp-1 and fis-2 regulate distinct cell-death execution pathways downstream of ced-3 and independent of ced-9. Mol. Cell 2008, 31:586-597.
    • (2008) Mol. Cell , vol.31 , pp. 586-597
    • Breckenridge, D.G.1    Kang, B.H.2    Kokel, D.3    Mitani, S.4    Staehelin, L.A.5    Xue, D.6
  • 84
    • 79551600416 scopus 로고    scopus 로고
    • Fis1 and Bap31 bridge the mitochondria-ER interface to establish a platform for apoptosis induction
    • Iwasawa R., Mahul-Mellier A.L., Datler C., Pazarentzos E., Grimm S. Fis1 and Bap31 bridge the mitochondria-ER interface to establish a platform for apoptosis induction. EMBO J. 2011, 30:556-568.
    • (2011) EMBO J. , vol.30 , pp. 556-568
    • Iwasawa, R.1    Mahul-Mellier, A.L.2    Datler, C.3    Pazarentzos, E.4    Grimm, S.5
  • 85
    • 0037417334 scopus 로고    scopus 로고
    • Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol
    • Breckenridge D.G., Stojanovic M., Marcellus R.C., Shore G.C. Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol. J. Cell Biol. 2003, 160:1115-1127.
    • (2003) J. Cell Biol. , vol.160 , pp. 1115-1127
    • Breckenridge, D.G.1    Stojanovic, M.2    Marcellus, R.C.3    Shore, G.C.4
  • 86
    • 33750526651 scopus 로고    scopus 로고
    • The mitochondrial fission protein hFis1 requires the endoplasmic reticulum gateway to induce apoptosis
    • Arirol E., James D., Huber D., Marchetto A., Vergani L., Martinou J.C., Scorrano L. The mitochondrial fission protein hFis1 requires the endoplasmic reticulum gateway to induce apoptosis. Mol. Biol. Cell 2006, 11:4593-4605.
    • (2006) Mol. Biol. Cell , vol.11 , pp. 4593-4605
    • Arirol, E.1    James, D.2    Huber, D.3    Marchetto, A.4    Vergani, L.5    Martinou, J.C.6    Scorrano, L.7
  • 87
    • 50949115617 scopus 로고    scopus 로고
    • High levels of Fis1, a pro-fission mitochondrial protein, trigger autophagy
    • Gomes L.C., Scorrano L. High levels of Fis1, a pro-fission mitochondrial protein, trigger autophagy. Biochim. Biophys. Acta 2008, 1777:860-866.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 860-866
    • Gomes, L.C.1    Scorrano, L.2
  • 88
    • 49349102894 scopus 로고    scopus 로고
    • Mitochondrial fusion, fission and autophagy as a quality control axis: the bioenergetic view
    • Twig G., Hyde B., Shirihai O.S. Mitochondrial fusion, fission and autophagy as a quality control axis: the bioenergetic view. Biochim. Biophys. Acta 2008, 1777:1092-1097.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1092-1097
    • Twig, G.1    Hyde, B.2    Shirihai, O.S.3
  • 90
    • 25144476558 scopus 로고    scopus 로고
    • TBC domain family, member 15 is a novel mammalian Rab GTPase-activating protein with substrate preference for Rab7
    • Zhang X.M., Walsh B., Mitchell C.A., Rowe T. TBC domain family, member 15 is a novel mammalian Rab GTPase-activating protein with substrate preference for Rab7. Biochem. Biophys. Res. Commun. 2005, 335:154-161.
    • (2005) Biochem. Biophys. Res. Commun. , vol.335 , pp. 154-161
    • Zhang, X.M.1    Walsh, B.2    Mitchell, C.A.3    Rowe, T.4
  • 91
    • 77952764666 scopus 로고    scopus 로고
    • Differential effects of TBC1D15 and mammalian Vps39 on Rab7 activation state, lysosomal morphology, and growth factor dependence
    • Peralta E.R., Martin B.C., Edinger A.L. Differential effects of TBC1D15 and mammalian Vps39 on Rab7 activation state, lysosomal morphology, and growth factor dependence. J. Biol. Chem. 2010, 285:16814-16821.
    • (2010) J. Biol. Chem. , vol.285 , pp. 16814-16821
    • Peralta, E.R.1    Martin, B.C.2    Edinger, A.L.3
  • 93
    • 25444514731 scopus 로고    scopus 로고
    • Ganglioside-induced differentiation associated protein 1 is a regulator of the mitochondrial network: new implications for Charcot-Marie-Tooth disease
    • Niemann A., Ruegg M., La Padula V., Schenone A., Suter U. Ganglioside-induced differentiation associated protein 1 is a regulator of the mitochondrial network: new implications for Charcot-Marie-Tooth disease. J. Cell Biol. 2005, 170:1067-1078.
    • (2005) J. Cell Biol. , vol.170 , pp. 1067-1078
    • Niemann, A.1    Ruegg, M.2    La Padula, V.3    Schenone, A.4    Suter, U.5
  • 94
    • 17744376804 scopus 로고    scopus 로고
    • GDAP1, the protein causing Charcot-Marie-Tooth disease type 4A, is expressed in neurons and is associated with mitochondria
    • Pedrola L., Espert A., Wu X., Claramunt R., Shy M.E., Palau F. GDAP1, the protein causing Charcot-Marie-Tooth disease type 4A, is expressed in neurons and is associated with mitochondria. Hum. Mol. Genet. 2005, 14:1087-1094.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 1087-1094
    • Pedrola, L.1    Espert, A.2    Wu, X.3    Claramunt, R.4    Shy, M.E.5    Palau, F.6
  • 95
    • 33746353696 scopus 로고    scopus 로고
    • Functional characterization of ganglioside-induced differentiation-associated protein 1 as a glutathione transferase
    • Shield A.J., Murray T.P., Board P.G. Functional characterization of ganglioside-induced differentiation-associated protein 1 as a glutathione transferase. Biochem. Biophys. Res. Commun. 2006, 346:859-866.
    • (2006) Biochem. Biophys. Res. Commun. , vol.346 , pp. 859-866
    • Shield, A.J.1    Murray, T.P.2    Board, P.G.3
  • 97
    • 0029609895 scopus 로고
    • Functional role of glycosphingolipids in cell recognition and signaling
    • Hakomori S., Igarashi Y. Functional role of glycosphingolipids in cell recognition and signaling. J. Biochem. 1995, 118:1091-1103.
    • (1995) J. Biochem. , vol.118 , pp. 1091-1103
    • Hakomori, S.1    Igarashi, Y.2
  • 100
    • 0034526495 scopus 로고    scopus 로고
    • Dynamin and its role in membrane fission
    • Hinshaw J.E. Dynamin and its role in membrane fission. Annu. Rev. Cell Dev. Biol. 2000, 16:483-519.
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 483-519
    • Hinshaw, J.E.1
  • 103
    • 0033749675 scopus 로고    scopus 로고
    • Lipids, lipid modification and lipid-protein interaction in membrane budding and fission-insights from the roles of endophilin A1 and synaptophysin in synaptic vesicle endocytosis
    • Huttner W.B., Schmidt A. Lipids, lipid modification and lipid-protein interaction in membrane budding and fission-insights from the roles of endophilin A1 and synaptophysin in synaptic vesicle endocytosis. Curr. Opin. Neurobiol. 2000, 10:543-551.
    • (2000) Curr. Opin. Neurobiol. , vol.10 , pp. 543-551
    • Huttner, W.B.1    Schmidt, A.2
  • 104
    • 0035827622 scopus 로고    scopus 로고
    • Molecular cloning and characterization of Bif-1. A novel Src homology 3 domain-containing protein that associates with Bax
    • Cuddeback S.M., Yamaguchi H., Komatsu K., Miyashita T., Yamada M., Wu C., Singh S., Wang H.G. Molecular cloning and characterization of Bif-1. A novel Src homology 3 domain-containing protein that associates with Bax. J. Biol. Chem. 2001, 276:20559-20565.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20559-20565
    • Cuddeback, S.M.1    Yamaguchi, H.2    Komatsu, K.3    Miyashita, T.4    Yamada, M.5    Wu, C.6    Singh, S.7    Wang, H.G.8
  • 106
    • 4644242944 scopus 로고    scopus 로고
    • Endophilin B1 is required for the maintenance of mitochondrial morphology
    • Karbowski M., Jeong S.Y., Youle R.J. Endophilin B1 is required for the maintenance of mitochondrial morphology. J. Cell Biol. 2004, 166:1027-1039.
    • (2004) J. Cell Biol. , vol.166 , pp. 1027-1039
    • Karbowski, M.1    Jeong, S.Y.2    Youle, R.J.3
  • 108
    • 77954385279 scopus 로고    scopus 로고
    • The sacsin repeating region (SRR): A novel Hsp90-related supra-domain associated with neurodegeneration
    • Anderson J.F., Siller E., Barral J.M. The sacsin repeating region (SRR): A novel Hsp90-related supra-domain associated with neurodegeneration. J. Mol. Biol. 2010, 400:665-674.
    • (2010) J. Mol. Biol. , vol.400 , pp. 665-674
    • Anderson, J.F.1    Siller, E.2    Barral, J.M.3
  • 112
    • 84863728713 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 disturbs mitochondrial dynamics via Dynamin-like protein
    • Niu J., Yu M., Wang C., Xu Z. Leucine-rich repeat kinase 2 disturbs mitochondrial dynamics via Dynamin-like protein. J. Neurochem. 2012, 122:650-658.
    • (2012) J. Neurochem. , vol.122 , pp. 650-658
    • Niu, J.1    Yu, M.2    Wang, C.3    Xu, Z.4
  • 122
    • 84858791998 scopus 로고    scopus 로고
    • Mitochondrial quality control: a matter of life and death for neurons
    • Rugarli E.I., Langer T. Mitochondrial quality control: a matter of life and death for neurons. EMBO J. 2012, 31:1336-1349.
    • (2012) EMBO J. , vol.31 , pp. 1336-1349
    • Rugarli, E.I.1    Langer, T.2
  • 123
    • 79960230433 scopus 로고    scopus 로고
    • Mitochondria in apoptosis: Bcl-2 family members and mitochondrial dynamics
    • Martinou J.C., Youle R.J. Mitochondria in apoptosis: Bcl-2 family members and mitochondrial dynamics. Dev. Cell 2011, 21:92-101.
    • (2011) Dev. Cell , vol.21 , pp. 92-101
    • Martinou, J.C.1    Youle, R.J.2
  • 125
    • 1242307475 scopus 로고    scopus 로고
    • Quantification 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., Youle R.J. Quantification of mitochondrial dynamics by photolabeling of individual organelles shows that mitochondrial fusion is blocked during the Bax activation phase of apoptosis. J. Cell Biol. 2004, 164:493-499.
    • (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
  • 126
    • 34547442346 scopus 로고    scopus 로고
    • Bak regulates mitochondrial morphology and pathology during apoptosis by interacting with mitofusins
    • Brooks C., Wei Q., Feng L., Dong G., Tao Y., Mei L., Xie Z.J., Dong Z. Bak regulates mitochondrial morphology and pathology during apoptosis by interacting with mitofusins. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:11649-11654.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 11649-11654
    • Brooks, C.1    Wei, Q.2    Feng, L.3    Dong, G.4    Tao, Y.5    Mei, L.6    Xie, Z.J.7    Dong, Z.8
  • 127
    • 34248182897 scopus 로고    scopus 로고
    • "Bax/Bak promote sumoylation of DRP1 and its stable association with mitochondria during apoptotic cell death
    • Wasiak S., Zunino R., McBride H.M. "Bax/Bak promote sumoylation of DRP1 and its stable association with mitochondria during apoptotic cell death. J. Cell Biol. 2007, 177:439-450.
    • (2007) J. Cell Biol. , vol.177 , pp. 439-450
    • Wasiak, S.1    Zunino, R.2    McBride, H.M.3
  • 131
    • 84860339096 scopus 로고    scopus 로고
    • Depletion of mitochondrial fission factor DRP1 causes increased apoptosis in human colon cancer cells
    • Inoue-Yamauchi A., Oda H. Depletion of mitochondrial fission factor DRP1 causes increased apoptosis in human colon cancer cells. Biochem. Biophys. Res. Commun. 2012, 421:81-85.
    • (2012) Biochem. Biophys. Res. Commun. , vol.421 , pp. 81-85
    • Inoue-Yamauchi, A.1    Oda, H.2
  • 133
    • 77953696905 scopus 로고    scopus 로고
    • Small molecule inhibitors of mitochondrial division: tools that translate basic biological research into medicine
    • Lackner L.L., Nunnari J. Small molecule inhibitors of mitochondrial division: tools that translate basic biological research into medicine. Chem. Biol. 2010, 17:578-583.
    • (2010) Chem. Biol. , vol.17 , pp. 578-583
    • Lackner, L.L.1    Nunnari, J.2
  • 136
    • 77951235489 scopus 로고    scopus 로고
    • Perturbations in mitochondrial dynamics induced by human mutant PINK1 can be rescued by the mitochondrial division inhibitor mdivi-1
    • Cui M., Tang X., Christian W.V., Yoon Y., Tieu K. Perturbations in mitochondrial dynamics induced by human mutant PINK1 can be rescued by the mitochondrial division inhibitor mdivi-1. J. Biol. Chem. 2010, 285:11740-11752.
    • (2010) J. Biol. Chem. , vol.285 , pp. 11740-11752
    • Cui, M.1    Tang, X.2    Christian, W.V.3    Yoon, Y.4    Tieu, K.5
  • 137
    • 67650348459 scopus 로고    scopus 로고
    • Frequency and selectivity of mitochondrial fusion are key to its quality maintenance function
    • Mouli P.K., Twig G., Shirihai O.S. Frequency and selectivity of mitochondrial fusion are key to its quality maintenance function. Biophys. J. 2009, 96:3509-3518.
    • (2009) Biophys. J. , vol.96 , pp. 3509-3518
    • Mouli, P.K.1    Twig, G.2    Shirihai, O.S.3
  • 139
    • 84871749760 scopus 로고    scopus 로고
    • Mitochondrial morphology in mitophagy and macroautophagy
    • (Epub ahead of print)
    • Gomes L.C., Scorrano L. Mitochondrial morphology in mitophagy and macroautophagy. Biochim. Biophys. Acta 2012, (Epub ahead of print). 10.1016/j.bbamcr.2012.02.012.
    • (2012) Biochim. Biophys. Acta
    • Gomes, L.C.1    Scorrano, L.2
  • 140
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra D., Tanaka A., Suen D.F., Youle R.J. Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J. Cell Biol. 2008, 183:795-803.
    • (2008) J. Cell Biol. , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 141
    • 78649685455 scopus 로고    scopus 로고
    • Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL
    • Jin S.M., Lazarou M., Wang C., Kane L.A., Narendra D.P., Youle R.J. Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL. J. Cell Biol. 2010, 191:933-942.
    • (2010) J. Cell Biol. , vol.191 , pp. 933-942
    • Jin, S.M.1    Lazarou, M.2    Wang, C.3    Kane, L.A.4    Narendra, D.P.5    Youle, R.J.6
  • 143
    • 79960716413 scopus 로고    scopus 로고
    • Regulating mitochondrial outer membrane proteins by ubiquitination and proteasomal degradation
    • Karbowski M., Youle R.J. Regulating mitochondrial outer membrane proteins by ubiquitination and proteasomal degradation. Curr. Opin. Cell Biol. 2011, 23:476-482.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 476-482
    • Karbowski, M.1    Youle, R.J.2
  • 144
    • 79957472437 scopus 로고    scopus 로고
    • Parkin mediates proteasome-dependent protein degradation and rupture of the outer mitochondrial membrane
    • Yoshii S.R., Kishi C., Ishihara N., Mizushima N. Parkin mediates proteasome-dependent protein degradation and rupture of the outer mitochondrial membrane. J. Biol. Chem. 2011, 286:19630-19640.
    • (2011) J. Biol. Chem. , vol.286 , pp. 19630-19640
    • Yoshii, S.R.1    Kishi, C.2    Ishihara, N.3    Mizushima, N.4
  • 146
    • 80355127945 scopus 로고    scopus 로고
    • Mitochondrial autophagy by Bnip3 involves Drp1-mediated mitochondrial fission and recruitment of Parkin in cardiac myocytes
    • Lee Y., Lee H.Y., Hanna R.A., Gustafsson A.B. Mitochondrial autophagy by Bnip3 involves Drp1-mediated mitochondrial fission and recruitment of Parkin in cardiac myocytes. Am. J. Physiol. Heart Circ. Physiol. 2011, 301:H1924-H1931.
    • (2011) Am. J. Physiol. Heart Circ. Physiol. , vol.301
    • Lee, Y.1    Lee, H.Y.2    Hanna, R.A.3    Gustafsson, A.B.4
  • 147
    • 55749090654 scopus 로고    scopus 로고
    • The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila
    • Deng H., Dodson M.W., Huang H., Guo M. The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:14503-14508.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 14503-14508
    • Deng, H.1    Dodson, M.W.2    Huang, H.3    Guo, M.4
  • 148
    • 77950384477 scopus 로고    scopus 로고
    • Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin
    • Ziviani E., Tao R.N., Whitworth A.J. Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:5018-5023.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 5018-5023
    • Ziviani, E.1    Tao, R.N.2    Whitworth, A.J.3
  • 152
    • 66349121718 scopus 로고    scopus 로고
    • Hypoxia-induced autophagy is mediated through hypoxia-inducible factor induction of BNIP3 and BNIP3L via their BH3 domains
    • Bellot G., Garcia-Medina R., Gounon P., Chiche J., Roux D., Pouysségur J., Mazure N.M. Hypoxia-induced autophagy is mediated through hypoxia-inducible factor induction of BNIP3 and BNIP3L via their BH3 domains. Mol. Cell. Biol. 2009, 29:2570-2581.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 2570-2581
    • Bellot, G.1    Garcia-Medina, R.2    Gounon, P.3    Chiche, J.4    Roux, D.5    Pouysségur, J.6    Mazure, N.M.7
  • 153
    • 84865544952 scopus 로고    scopus 로고
    • Mitochondrial fission, fusion, and stress
    • Youle R.J., van der Bliek A.M. Mitochondrial fission, fusion, and stress. Science 2012, 337:1062-1065.
    • (2012) Science , vol.337 , pp. 1062-1065
    • Youle, R.J.1    van der Bliek, A.M.2
  • 155
    • 34249689057 scopus 로고    scopus 로고
    • Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission
    • Taguchi N., Ishihara N., Jofuku A., Oka T., Mihara K. Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission. J. Biol. Chem. 2007, 282:11521-11529.
    • (2007) J. Biol. Chem. , vol.282 , pp. 11521-11529
    • Taguchi, N.1    Ishihara, N.2    Jofuku, A.3    Oka, T.4    Mihara, K.5
  • 157
    • 78751470559 scopus 로고    scopus 로고
    • Aberrant mitochondrial fission in neurons induced by protein kinase C{delta} under stress conditions in vivo
    • Qi X., Disatnik M.H., Shen N., Sobel R.A., Mochly-Rosen D. Aberrant mitochondrial fission in neurons induced by protein kinase C{delta} under stress conditions in vivo. Mol. Biol. Cell 2011, 22:256-265.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 256-265
    • Qi, X.1    Disatnik, M.H.2    Shen, N.3    Sobel, R.A.4    Mochly-Rosen, D.5
  • 158
    • 34547611925 scopus 로고    scopus 로고
    • Cyclic AMP-dependent protein kinase phosphorylation of Drp1 regulates its GTPase activity and mitochondrial morphology
    • Chang C.R., Blackstone C. Cyclic AMP-dependent protein kinase phosphorylation of Drp1 regulates its GTPase activity and mitochondrial morphology. J. Biol. Chem. 2007, 282:21583-21587.
    • (2007) J. Biol. Chem. , vol.282 , pp. 21583-21587
    • Chang, C.R.1    Blackstone, C.2
  • 159
    • 34848840991 scopus 로고    scopus 로고
    • Reversible phosphorylation of Drp1 by cyclic AMP-dependent protein kinase and calcineurin regulates mitochondrial fission and cell death
    • Cribbs J.T., Strack S. Reversible phosphorylation of Drp1 by cyclic AMP-dependent protein kinase and calcineurin regulates mitochondrial fission and cell death. EMBO Rep. 2007, 8:939-944.
    • (2007) EMBO Rep. , vol.8 , pp. 939-944
    • Cribbs, J.T.1    Strack, S.2
  • 160
    • 79955623510 scopus 로고    scopus 로고
    • During autophagy mitochondria elongate, are spared from degradation and sustain cell viability
    • Gomes L.C., Di Benedetto G., Scorrano L. During autophagy mitochondria elongate, are spared from degradation and sustain cell viability. Nat. Cell Biol. 2011, 5:589-598.
    • (2011) Nat. Cell Biol. , vol.5 , pp. 589-598
    • Gomes, L.C.1    Di Benedetto, G.2    Scorrano, L.3
  • 161
    • 79959987510 scopus 로고    scopus 로고
    • Tubular network formation protects mitochondria from autophagosomal degradation during nutrient starvation
    • Rambold A.S., Kostelecky B., Elia N., Lippincott-Schwartz J. Tubular network formation protects mitochondria from autophagosomal degradation during nutrient starvation. Proc. Natl. Acad. Sci. U. S. A. 2011, 25:10190-10195.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.25 , pp. 10190-10195
    • Rambold, A.S.1    Kostelecky, B.2    Elia, N.3    Lippincott-Schwartz, J.4
  • 164
    • 0037135975 scopus 로고    scopus 로고
    • Rab32 is an A-kinase anchoring protein and participates in mitochondrial dynamics
    • Alto N.M., Soderling J., Scott J.D. Rab32 is an A-kinase anchoring protein and participates in mitochondrial dynamics. J. Cell Biol. 2002, 158:659-668.
    • (2002) J. Cell Biol. , vol.158 , pp. 659-668
    • Alto, N.M.1    Soderling, J.2    Scott, J.D.3
  • 166
    • 84862909353 scopus 로고    scopus 로고
    • The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways
    • Wang Z., Jiang H., Chen S., Du F., Wang X. The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways. Cell 2012, 148:228-243.
    • (2012) Cell , vol.148 , pp. 228-243
    • Wang, Z.1    Jiang, H.2    Chen, S.3    Du, F.4    Wang, X.5
  • 170
    • 64249133725 scopus 로고    scopus 로고
    • S-Nitrosylation of Drp1 mediates β-amyloid-related mitochondrial fission and neuronal injury
    • Cho D.H., Nakamura T., Fang J., Cieplak P., Godzik A., Gu Z., Lipton S.A. S-Nitrosylation of Drp1 mediates β-amyloid-related mitochondrial fission and neuronal injury. Science 2009, 324:102-105.
    • (2009) Science , vol.324 , pp. 102-105
    • Cho, D.H.1    Nakamura, T.2    Fang, J.3    Cieplak, P.4    Godzik, A.5    Gu, Z.6    Lipton, S.A.7
  • 173
    • 67650076601 scopus 로고    scopus 로고
    • MAPL is a new mitochondrial SUMO E3 ligase that regulates mitochondrial fission
    • Braschi E., Zunino R., McBride H.M. MAPL is a new mitochondrial SUMO E3 ligase that regulates mitochondrial fission. EMBO Rep. 2009, 10:748-754.
    • (2009) EMBO Rep. , vol.10 , pp. 748-754
    • Braschi, E.1    Zunino, R.2    McBride, H.M.3
  • 174
    • 34248225298 scopus 로고    scopus 로고
    • The SUMO protease SENP5 is required to maintain mitochondrial morphology and function
    • Zunino R., Schauss A., Rippstein P., Andrade-Navarro M., McBride H.M. The SUMO protease SENP5 is required to maintain mitochondrial morphology and function. J. Cell Sci. 2007, 120:1178-1188.
    • (2007) J. Cell Sci. , vol.120 , pp. 1178-1188
    • Zunino, R.1    Schauss, A.2    Rippstein, P.3    Andrade-Navarro, M.4    McBride, H.M.5
  • 176
    • 67650534951 scopus 로고    scopus 로고
    • Translocation of SenP5 from the nucleoli to the mitochondria modulates DRP1-dependent fission during mitosis
    • Zunino R., Braschi E., Xu L., McBride H.M. Translocation of SenP5 from the nucleoli to the mitochondria modulates DRP1-dependent fission during mitosis. J. Biol. Chem. 2009, 284:17783-17795.
    • (2009) J. Biol. Chem. , vol.284 , pp. 17783-17795
    • Zunino, R.1    Braschi, E.2    Xu, L.3    McBride, H.M.4
  • 178
    • 78049529676 scopus 로고    scopus 로고
    • Vps35 mediates vesicle transport between the mitochondria and peroxisomes
    • Braschi E., Goyon V., Zunino R., Mohanty A., Xu L., McBride H.M. Vps35 mediates vesicle transport between the mitochondria and peroxisomes. Curr. Biol. 2010, 20:1310-1315.
    • (2010) Curr. Biol. , vol.20 , pp. 1310-1315
    • Braschi, E.1    Goyon, V.2    Zunino, R.3    Mohanty, A.4    Xu, L.5    McBride, H.M.6
  • 179
    • 33749253910 scopus 로고    scopus 로고
    • MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change mitochondrial morphology
    • Nakamura N., Kimura Y., Tokuda M., Honda S., Hirose S. MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change mitochondrial morphology. EMBO Rep. 2006, 7:1019-1022.
    • (2006) EMBO Rep. , vol.7 , pp. 1019-1022
    • Nakamura, N.1    Kimura, Y.2    Tokuda, M.3    Honda, S.4    Hirose, S.5
  • 181
    • 34347398050 scopus 로고    scopus 로고
    • The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division
    • Karbowski M., Neutzner A., Youle R.J. The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division. J. Cell Biol. 2007, 178:71-84.
    • (2007) J. Cell Biol. , vol.178 , pp. 71-84
    • Karbowski, M.1    Neutzner, A.2    Youle, R.J.3
  • 184
    • 84857132601 scopus 로고    scopus 로고
    • Mitochondrial ubiquitin ligase MITOL blocks S-nitrosylated MAP1B-light chain 1-mediated mitochondrial dysfunction and neuronal cell death
    • Yonashiro R., Kimijima Y., Shimura T., Kawaguchi K., Fukuda T., Inatome R., Yanagi S. Mitochondrial ubiquitin ligase MITOL blocks S-nitrosylated MAP1B-light chain 1-mediated mitochondrial dysfunction and neuronal cell death. Proc. Natl. Acad. Sci. U. S. A. 2012, 109:2382-2387.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 2382-2387
    • Yonashiro, R.1    Kimijima, Y.2    Shimura, T.3    Kawaguchi, K.4    Fukuda, T.5    Inatome, R.6    Yanagi, S.7
  • 186
    • 3843125367 scopus 로고    scopus 로고
    • Knockdown of MTP18, a novel phosphatidylinositol 3-kinase-dependent protein, affects mitochondrial morphology and induces apoptosis
    • Tondera D., Santel A., Schwarzer R., Dames S., Giese K., Klippel A., Kaufmann J. Knockdown of MTP18, a novel phosphatidylinositol 3-kinase-dependent protein, affects mitochondrial morphology and induces apoptosis. J. Biol. Chem. 2004, 279:31544-31555.
    • (2004) J. Biol. Chem. , vol.279 , pp. 31544-31555
    • Tondera, D.1    Santel, A.2    Schwarzer, R.3    Dames, S.4    Giese, K.5    Klippel, A.6    Kaufmann, J.7
  • 187
    • 23844539004 scopus 로고    scopus 로고
    • The mitochondrial protein MTP18 contributes to mitochondrial fission in mammalian cells
    • Tondera D., Czauderna F., Paulick K., Schwarzer R., Kaufmann J., Santel A. The mitochondrial protein MTP18 contributes to mitochondrial fission in mammalian cells. J. Cell Sci. 2005, 118:3049-3059.
    • (2005) J. Cell Sci. , vol.118 , pp. 3049-3059
    • Tondera, D.1    Czauderna, F.2    Paulick, K.3    Schwarzer, R.4    Kaufmann, J.5    Santel, A.6
  • 188
    • 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


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