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Volumn 21, Issue 6, 2010, Pages 575-581

Organellar vs cellular control of mitochondrial dynamics

Author keywords

Autophagy; Bioenergetics; Cell cycle; Fission; Fusion; Mitochondrial dynamics; Mitochondrial movement; Mitophagy; MtDNA

Indexed keywords

ADENOSINE TRIPHOSPHATE;

EID: 77955276502     PISSN: 10849521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.semcdb.2010.01.003     Document Type: Review
Times cited : (65)

References (89)
  • 1
    • 33745748154 scopus 로고    scopus 로고
    • Organization, dynamics and transmission of mitochondrial DNA: focus on vertebrate nucleoids
    • Malka F., Lombes A., Rojo M. Organization, dynamics and transmission of mitochondrial DNA: focus on vertebrate nucleoids. Biochim Biophys Acta 2006, 1763:463-472.
    • (2006) Biochim Biophys Acta , vol.1763 , pp. 463-472
    • Malka, F.1    Lombes, A.2    Rojo, M.3
  • 3
    • 3242884720 scopus 로고    scopus 로고
    • Organization and dynamics of human mitochondrial DNA
    • Legros F., Malka F., Frachon P., Lombes A., Rojo M. Organization and dynamics of human mitochondrial DNA. J Cell Sci 2004, 117:2653-2662.
    • (2004) J Cell Sci , vol.117 , pp. 2653-2662
    • Legros, F.1    Malka, F.2    Frachon, P.3    Lombes, A.4    Rojo, M.5
  • 4
    • 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, 13:4343-4354.
    • (2002) Mol Biol Cell , vol.13 , pp. 4343-4354
    • Legros, F.1    Lombes, A.2    Frachon, P.3    Rojo, M.4
  • 5
    • 46249106487 scopus 로고    scopus 로고
    • Mitochondrial nucleoids maintain genetic autonomy but allow for functional complementation
    • Gilkerson R.W., Schon E.A., Hernandez E., Davidson M.M. Mitochondrial nucleoids maintain genetic autonomy but allow for functional complementation. J Cell Biol 2008, 181:1117-1128.
    • (2008) J Cell Biol , vol.181 , pp. 1117-1128
    • Gilkerson, R.W.1    Schon, E.A.2    Hernandez, E.3    Davidson, M.M.4
  • 6
    • 38549110110 scopus 로고    scopus 로고
    • Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
    • Twig G., Elorza A., Molina A.J., Mohamed H., Wikstrom J.D., Walzer G., et al. Fission and selective fusion govern mitochondrial segregation and elimination by autophagy. EMBO J 2008, 27:433-446.
    • (2008) EMBO J , vol.27 , pp. 433-446
    • Twig, G.1    Elorza, A.2    Molina, A.J.3    Mohamed, H.4    Wikstrom, J.D.5    Walzer, G.6
  • 7
    • 0034881326 scopus 로고    scopus 로고
    • Inter-mitochondrial complementation: mitochondria-specific system preventing mice from expression of disease phenotypes by mutant mtDNA
    • Nakada K., Inoue K., Ono T., Isobe K., Ogura A., Goto Y.I., et al. Inter-mitochondrial complementation: mitochondria-specific system preventing mice from expression of disease phenotypes by mutant mtDNA. Nat Med 2001, 7:934-940.
    • (2001) Nat Med , vol.7 , pp. 934-940
    • Nakada, K.1    Inoue, K.2    Ono, T.3    Isobe, K.4    Ogura, A.5    Goto, Y.I.6
  • 8
    • 2442687998 scopus 로고    scopus 로고
    • Frequent fusion and fission of plant mitochondria with unequal nucleoid distribution
    • Arimura S., Yamamoto J., Aida G.P., Nakazono M., Tsutsumi N. Frequent fusion and fission of plant mitochondria with unequal nucleoid distribution. Proc Natl Acad Sci USA 2004, 101:7805-7808.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7805-7808
    • Arimura, S.1    Yamamoto, J.2    Aida, G.P.3    Nakazono, M.4    Tsutsumi, N.5
  • 9
    • 0035146891 scopus 로고    scopus 로고
    • Mitochondrial filaments and clusters as intracellular power-transmitting cables
    • Skulachev V.P. Mitochondrial filaments and clusters as intracellular power-transmitting cables. Trends Biochem Sci 2001, 26:23-29.
    • (2001) Trends Biochem Sci , vol.26 , pp. 23-29
    • Skulachev, V.P.1
  • 12
    • 0015106989 scopus 로고
    • Symbiosis and evolution
    • Margulis L. Symbiosis and evolution. Sci Am 1971, 225:48-57.
    • (1971) Sci Am , vol.225 , pp. 48-57
    • Margulis, L.1
  • 13
    • 0034913239 scopus 로고    scopus 로고
    • The origin and early evolution of mitochondria
    • REVIEWS1018
    • Gray M.W., Burger G., Lang B.F. The origin and early evolution of mitochondria. Genome Biol 2001, 2. REVIEWS1018.
    • (2001) Genome Biol , vol.2
    • Gray, M.W.1    Burger, G.2    Lang, B.F.3
  • 14
    • 0033525788 scopus 로고    scopus 로고
    • Mitochondrial evolution
    • Gray M.W., Burger G., Lang B.F. Mitochondrial evolution. Science 1999, 283:1476-1481.
    • (1999) Science , vol.283 , pp. 1476-1481
    • Gray, M.W.1    Burger, G.2    Lang, B.F.3
  • 15
    • 34948890528 scopus 로고    scopus 로고
    • Beta-cell mitochondria exhibit membrane potential heterogeneity that can be altered by stimulatory or toxic fuel levels
    • Wikstrom J.D., Katzman S.M., Mohamed H., Twig G., Graf S.A., Heart E., et al. Beta-cell mitochondria exhibit membrane potential heterogeneity that can be altered by stimulatory or toxic fuel levels. Diabetes 2007, 56:2569-2578.
    • (2007) Diabetes , vol.56 , pp. 2569-2578
    • Wikstrom, J.D.1    Katzman, S.M.2    Mohamed, H.3    Twig, G.4    Graf, S.A.5    Heart, E.6
  • 16
    • 67749089562 scopus 로고    scopus 로고
    • A hyperfused mitochondrial state achieved at G1-S regulates cyclin E buildup and entry into S phase
    • Mitra K., Wunder C., Roysam B., Lin G., Lippincott-Schwartz J. A hyperfused mitochondrial state achieved at G1-S regulates cyclin E buildup and entry into S phase. Proc Natl Acad Sci USA 2009, 106:11960-11965.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 11960-11965
    • Mitra, K.1    Wunder, C.2    Roysam, B.3    Lin, G.4    Lippincott-Schwartz, J.5
  • 17
    • 0037029049 scopus 로고    scopus 로고
    • Transcriptional activators and coactivators in the nuclear control of mitochondrial function in mammalian cells
    • Scarpulla R.C. Transcriptional activators and coactivators in the nuclear control of mitochondrial function in mammalian cells. Gene 2002, 286:81-89.
    • (2002) Gene , vol.286 , pp. 81-89
    • Scarpulla, R.C.1
  • 18
    • 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
  • 20
    • 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
  • 21
    • 26444463430 scopus 로고    scopus 로고
    • Proteins that fuse and fragment mitochondria in apoptosis: con-fissing a deadly con-fusion?
    • Scorrano L. Proteins that fuse and fragment mitochondria in apoptosis: con-fissing a deadly con-fusion?. J Bioenerg Biomembr 2005, 37:165-170.
    • (2005) J Bioenerg Biomembr , vol.37 , pp. 165-170
    • Scorrano, L.1
  • 22
    • 68949163080 scopus 로고    scopus 로고
    • Ca2+-dependent regulation of mitochondrial dynamics by the Miro-Milton complex
    • Liu X., Hajnoczky G. Ca2+-dependent regulation of mitochondrial dynamics by the Miro-Milton complex. Int J Biochem Cell Biol 2009, 41:1972-1976.
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 1972-1976
    • Liu, X.1    Hajnoczky, G.2
  • 24
    • 70350324917 scopus 로고    scopus 로고
    • Mitochondrial 'kiss-and-run': interplay between mitochondrial motility and fusion-fission dynamics
    • Liu X, Weaver D, Shirihai OS, Hajnoczky G, Ref Type: Generic
    • Liu X. Mitochondrial 'kiss-and-run': interplay between mitochondrial motility and fusion-fission dynamics. EMBO J 2009, Liu X, Weaver D, Shirihai OS, Hajnoczky G, Ref Type: Generic.
    • (2009) EMBO J
    • Liu, X.1
  • 26
    • 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
  • 27
    • 33745714433 scopus 로고    scopus 로고
    • Tagging and tracking individual networks within a complex mitochondrial web with photoactivatable GFP
    • Twig G., Graf S.A., Wikstrom J.D., Mohamed H., Haigh S.E., Elorza A., et al. Tagging and tracking individual networks within a complex mitochondrial web with photoactivatable GFP. Am J Physiol Cell Physiol 2006, 291:C176-C184.
    • (2006) Am J Physiol Cell Physiol , vol.291
    • Twig, G.1    Graf, S.A.2    Wikstrom, J.D.3    Mohamed, H.4    Haigh, S.E.5    Elorza, A.6
  • 28
    • 0142246587 scopus 로고    scopus 로고
    • Photoconversion of matrix targeted GFP enables analysis of continuity and intermixing of the mitochondrial lumen
    • Jakobs S., Schauss A.C., Hell S.W. Photoconversion of matrix targeted GFP enables analysis of continuity and intermixing of the mitochondrial lumen. FEBS Lett 2003, 554:194-200.
    • (2003) FEBS Lett , vol.554 , pp. 194-200
    • Jakobs, S.1    Schauss, A.C.2    Hell, S.W.3
  • 29
    • 65449184157 scopus 로고    scopus 로고
    • Monitoring mitochondrial dynamics with photoactivatable [corrected] green fluorescent protein
    • Molina A.J., Shirihai O.S. Monitoring mitochondrial dynamics with photoactivatable [corrected] green fluorescent protein. Methods Enzymol 2009, 457:289-304.
    • (2009) Methods Enzymol , vol.457 , pp. 289-304
    • Molina, A.J.1    Shirihai, O.S.2
  • 30
    • 55549134335 scopus 로고    scopus 로고
    • Measurement of instantaneous velocity vectors of organelle transport: mitochondrial transport and bioenergetics in hippocampal neurons
    • Gerencser A.A., Nicholls D.G. Measurement of instantaneous velocity vectors of organelle transport: mitochondrial transport and bioenergetics in hippocampal neurons. Biophys J 2008, 95:3079-3099.
    • (2008) Biophys J , vol.95 , pp. 3079-3099
    • Gerencser, A.A.1    Nicholls, D.G.2
  • 31
    • 27744491193 scopus 로고    scopus 로고
    • Emerging functions of mammalian mitochondrial fusion and fission
    • Spec No. 2
    • Chen H., Chan D.C. Emerging functions of mammalian mitochondrial fusion and fission. Hum Mol Genet 2005, 14(Spec No. 2):R283-R289.
    • (2005) Hum Mol Genet , vol.14
    • Chen, H.1    Chan, D.C.2
  • 32
    • 22544451586 scopus 로고    scopus 로고
    • Disruption of fusion results in mitochondrial heterogeneity and dysfunction
    • Chen H., Chomyn A., Chan D.C. Disruption of fusion results in mitochondrial heterogeneity and dysfunction. J Biol Chem 2005, 280:26185-26192.
    • (2005) J Biol Chem , vol.280 , pp. 26185-26192
    • Chen, H.1    Chomyn, A.2    Chan, D.C.3
  • 33
    • 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
  • 34
    • 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
  • 35
    • 33745274726 scopus 로고    scopus 로고
    • Mitochondria: dynamic organelles in disease, aging, and development
    • Chan D.C. Mitochondria: dynamic organelles in disease, aging, and development. Cell 2006, 125:1241-1252.
    • (2006) Cell , vol.125 , pp. 1241-1252
    • Chan, D.C.1
  • 36
    • 20944447173 scopus 로고    scopus 로고
    • Regulation of Ca2+-induced permeability transition by Bcl-2 is antagonized by Drpl and hFis1
    • Kong D., Xu L., Yu Y., Zhu W., Andrews D.W., Yoon Y., et al. Regulation of Ca2+-induced permeability transition by Bcl-2 is antagonized by Drpl and hFis1. Mol Cell Biochem 2005, 272:187-199.
    • (2005) Mol Cell Biochem , vol.272 , pp. 187-199
    • Kong, D.1    Xu, L.2    Yu, Y.3    Zhu, W.4    Andrews, D.W.5    Yoon, Y.6
  • 37
    • 0037164813 scopus 로고    scopus 로고
    • Spatial and temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2 during apoptosis
    • Karbowski M., Lee Y.J., Gaume B., Jeong S.Y., Frank S., Nechushtan A., et al. Spatial and temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2 during apoptosis. J Cell Biol 2002, 159:931-938.
    • (2002) J Cell Biol , vol.159 , pp. 931-938
    • Karbowski, M.1    Lee, Y.J.2    Gaume, B.3    Jeong, S.Y.4    Frank, S.5    Nechushtan, A.6
  • 38
    • 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., 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 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
  • 39
    • 0141592470 scopus 로고    scopus 로고
    • HFis1, a novel component of the mammalian mitochondrial fission machinery
    • James D.I., Parone P.A., Mattenberger Y., Martinou J.C. hFis1, a novel component of the 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
  • 40
    • 1542380494 scopus 로고    scopus 로고
    • Sumo1 conjugates mitochondrial substrates and participates in mitochondrial fission
    • Harder Z., Zunino R., McBride H. Sumo1 conjugates mitochondrial substrates and participates in mitochondrial fission. Curr Biol 2004, 14:340-345.
    • (2004) Curr Biol , vol.14 , pp. 340-345
    • Harder, Z.1    Zunino, R.2    McBride, H.3
  • 41
    • 33746620461 scopus 로고    scopus 로고
    • (De)constructing mitochondria: what for?
    • Dimmer K.S., Scorrano L. (De)constructing mitochondria: what for?. Physiology (Bethesda) 2006, 21:233-241.
    • (2006) Physiology (Bethesda) , vol.21 , pp. 233-241
    • Dimmer, K.S.1    Scorrano, L.2
  • 42
    • 33745685054 scopus 로고    scopus 로고
    • Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling
    • Cipolat S., Rudka T., Hartmann D., Costa V., Serneels L., Craessaerts K., et al. Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling. Cell 2006, 126:163-175.
    • (2006) Cell , vol.126 , pp. 163-175
    • Cipolat, S.1    Rudka, T.2    Hartmann, D.3    Costa, V.4    Serneels, L.5    Craessaerts, K.6
  • 44
    • 34648839914 scopus 로고    scopus 로고
    • OPA1 cleavage depends on decreased mitochondrial ATP level and bivalent metals
    • Baricault L., Segui B., Guegand L., Olichon A., Valette A., Larminat F., et al. OPA1 cleavage depends on decreased mitochondrial ATP level and bivalent metals. Exp Cell Res 2007, 313:3800-3808.
    • (2007) Exp Cell Res , vol.313 , pp. 3800-3808
    • Baricault, L.1    Segui, B.2    Guegand, L.3    Olichon, A.4    Valette, A.5    Larminat, F.6
  • 45
    • 33845976357 scopus 로고    scopus 로고
    • Proteolytic processing of OPA1 links mitochondrial dysfunction to alterations in mitochondrial morphology
    • Duvezin-Caubet S., Jagasia R., Wagener J., Hofmann S., Trifunovic A., Hansson A., et al. Proteolytic processing of OPA1 links mitochondrial dysfunction to alterations in mitochondrial morphology. J Biol Chem 2006, 281:37972-37979.
    • (2006) J Biol Chem , vol.281 , pp. 37972-37979
    • Duvezin-Caubet, S.1    Jagasia, R.2    Wagener, J.3    Hofmann, S.4    Trifunovic, A.5    Hansson, A.6
  • 46
    • 43049115673 scopus 로고    scopus 로고
    • Modulation of mitochondrial morphology by bioenergetics defects in primary human fibroblasts
    • Guillery O., Malka F., Frachon P., Milea D., Rojo M., Lombes A. Modulation of mitochondrial morphology by bioenergetics defects in primary human fibroblasts. Neuromuscul Disord 2008, 18:319-330.
    • (2008) Neuromuscul Disord , vol.18 , pp. 319-330
    • Guillery, O.1    Malka, F.2    Frachon, P.3    Milea, D.4    Rojo, M.5    Lombes, A.6
  • 47
    • 13444287961 scopus 로고    scopus 로고
    • Mitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity
    • Ishihara N., Eura Y., Mihara K. 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    Eura, Y.2    Mihara, K.3
  • 48
    • 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., 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 2003, 301:891-898.
    • (2003) Biochem Biophys Res Commun , vol.301 , pp. 891-898
    • Ishihara, N.1    Jofuku, A.2    Eura, Y.3    Mihara, K.4
  • 49
    • 68149103297 scopus 로고    scopus 로고
    • Mitofusins and OPA1 mediate sequential steps in mitochondrial membrane fusion
    • Song Z., Ghochani M., McCaffery J.M., Frey T.G., Chan D.C. Mitofusins and OPA1 mediate sequential steps in mitochondrial membrane fusion. Mol Biol Cell 2009, 20:3525-3532.
    • (2009) Mol Biol Cell , vol.20 , pp. 3525-3532
    • Song, Z.1    Ghochani, M.2    McCaffery, J.M.3    Frey, T.G.4    Chan, D.C.5
  • 50
    • 34548313688 scopus 로고    scopus 로고
    • OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L
    • Song Z., Chen H., Fiket M., Alexander C., Chan D.C. OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L. J Cell Biol 2007, 178:749-755.
    • (2007) J Cell Biol , vol.178 , pp. 749-755
    • Song, Z.1    Chen, H.2    Fiket, M.3    Alexander, C.4    Chan, D.C.5
  • 51
    • 34548313686 scopus 로고    scopus 로고
    • Regulation of the mitochondrial dynamin-like protein Opa1 by proteolytic cleavage
    • Griparic L., Kanazawa T., van der Bliek A.M. Regulation of the mitochondrial dynamin-like protein Opa1 by proteolytic cleavage. J Cell Biol 2007, 178:757-764.
    • (2007) J Cell Biol , vol.178 , pp. 757-764
    • Griparic, L.1    Kanazawa, T.2    van der Bliek, A.M.3
  • 52
    • 20544468415 scopus 로고    scopus 로고
    • Analysis of functional domains of rat mitochondrial Fis1, the mitochondrial fission-stimulating protein
    • Jofuku A., Ishihara N., Mihara K. Analysis of functional domains of rat mitochondrial Fis1, the mitochondrial fission-stimulating protein. Biochem Biophys Res Commun 2005, 333:650-659.
    • (2005) Biochem Biophys Res Commun , vol.333 , pp. 650-659
    • Jofuku, A.1    Ishihara, N.2    Mihara, K.3
  • 53
    • 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, 15:678-683.
    • (2005) Curr Biol , vol.15 , pp. 678-683
    • De Vos, K.J.1    Allan, V.J.2    Grierson, A.J.3    Sheetz, M.P.4
  • 54
    • 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
  • 55
    • 0035487007 scopus 로고    scopus 로고
    • The mitochondrial permeability transition initiates autophagy in rat hepatocytes
    • Elmore S.P., Qian T., Grissom S.F., Lemasters J.J. The mitochondrial permeability transition initiates autophagy in rat hepatocytes. FASEB J 2001, 15:2286-2287.
    • (2001) FASEB J , vol.15 , pp. 2286-2287
    • Elmore, S.P.1    Qian, T.2    Grissom, S.F.3    Lemasters, J.J.4
  • 56
  • 57
    • 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
  • 58
    • 34548077177 scopus 로고    scopus 로고
    • Autophagy and vacuole homeostasis: a case for self-degradation?
    • Mijaljica D., Prescott M., Klionsky D.J., Devenish R.J. Autophagy and vacuole homeostasis: a case for self-degradation?. Autophagy 2007, 3:417-421.
    • (2007) Autophagy , vol.3 , pp. 417-421
    • Mijaljica, D.1    Prescott, M.2    Klionsky, D.J.3    Devenish, R.J.4
  • 59
    • 38549101188 scopus 로고    scopus 로고
    • Quality control of mitochondria: protection against neurodegeneration and ageing
    • Tatsuta T., Langer T. Quality control of mitochondria: protection against neurodegeneration and ageing. EMBO J 2008, 27:306-314.
    • (2008) EMBO J , vol.27 , pp. 306-314
    • Tatsuta, T.1    Langer, T.2
  • 60
    • 0000037251 scopus 로고    scopus 로고
    • Rapid diffusion of green fluorescent protein in the mitochondrial matrix
    • Partikian A., Olveczky B., Swaminathan R., Li Y., Verkman A.S. Rapid diffusion of green fluorescent protein in the mitochondrial matrix. J Cell Biol 1998, 140:821-829.
    • (1998) J Cell Biol , vol.140 , pp. 821-829
    • Partikian, A.1    Olveczky, B.2    Swaminathan, R.3    Li, Y.4    Verkman, A.S.5
  • 61
    • 0036536714 scopus 로고    scopus 로고
    • Mitochondrial dynamics and division in budding yeast
    • Shaw J.M., Nunnari J. Mitochondrial dynamics and division in budding yeast. Trends Cell Biol 2002, 12:178-184.
    • (2002) Trends Cell Biol , vol.12 , pp. 178-184
    • Shaw, J.M.1    Nunnari, J.2
  • 62
    • 33745758647 scopus 로고    scopus 로고
    • Molecular mechanism of mitochondrial membrane fusion
    • Griffin E.E., Detmer S.A., Chan D.C. Molecular mechanism of mitochondrial membrane fusion. Biochim Biophys Acta 2006, 1763:482-489.
    • (2006) Biochim Biophys Acta , vol.1763 , pp. 482-489
    • Griffin, E.E.1    Detmer, S.A.2    Chan, D.C.3
  • 63
    • 68949150785 scopus 로고    scopus 로고
    • What can mitochondrial heterogeneity tell us about mitochondrial dynamics and autophagy?
    • Wikstrom J.D., Twig G., Shirihai O.S. What can mitochondrial heterogeneity tell us about mitochondrial dynamics and autophagy?. Int J Biochem Cell Biol 2009, 41:1914-1927.
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 1914-1927
    • Wikstrom, J.D.1    Twig, G.2    Shirihai, O.S.3
  • 64
    • 0038783254 scopus 로고    scopus 로고
    • Mitofusin-1 protein 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 protein 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
  • 65
    • 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
  • 66
    • 33845877961 scopus 로고    scopus 로고
    • Identification of a novel protein that regulates mitochondrial fusion by modulating mitofusin (Mfn) protein function
    • Eura Y., Ishihara N., Oka T., Mihara K. Identification of a novel protein that regulates mitochondrial fusion by modulating mitofusin (Mfn) protein function. J Cell Sci 2006, 119:4913-4925.
    • (2006) J Cell Sci , vol.119 , pp. 4913-4925
    • Eura, Y.1    Ishihara, N.2    Oka, T.3    Mihara, K.4
  • 67
    • 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
  • 68
    • 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., Lombes A. Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo. J Cell Sci 2002, 115:1663-1674.
    • (2002) J Cell Sci , vol.115 , pp. 1663-1674
    • Rojo, M.1    Legros, F.2    Chateau, D.3    Lombes, A.4
  • 69
    • 40949156234 scopus 로고    scopus 로고
    • Measuring mitochondrial shape changes and their consequences on mitochondrial involvement during apoptosis
    • Frezza C., Cipolat S., Scorrano L. Measuring mitochondrial shape changes and their consequences on mitochondrial involvement during apoptosis. Methods Mol Biol 2007, 372:405-420.
    • (2007) Methods Mol Biol , vol.372 , pp. 405-420
    • Frezza, C.1    Cipolat, S.2    Scorrano, L.3
  • 70
    • 33749991592 scopus 로고    scopus 로고
    • Mitochondrial inner-membrane fusion and crista maintenance requires the dynamin-related GTPase Mgm1
    • Meeusen S., Devay R., Block J., Cassidy-Stone A., Wayson S., McCaffery J.M., 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    Devay, R.2    Block, J.3    Cassidy-Stone, A.4    Wayson, S.5    McCaffery, J.M.6
  • 71
    • 38849099158 scopus 로고    scopus 로고
    • Chemical inhibition of the mitochondrial division dynamin reveals its role in Bax/Bak-dependent mitochondrial outer membrane permeabilization
    • Cassidy-Stone A., Chipuk J.E., Ingerman E., Song C., Yoo C., Kuwana T., et al. Chemical inhibition of the mitochondrial division dynamin reveals its role in Bax/Bak-dependent mitochondrial outer membrane permeabilization. Dev Cell 2008, 14:193-204.
    • (2008) Dev Cell , vol.14 , pp. 193-204
    • Cassidy-Stone, A.1    Chipuk, J.E.2    Ingerman, E.3    Song, C.4    Yoo, C.5    Kuwana, T.6
  • 72
    • 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
  • 74
    • 9444226972 scopus 로고    scopus 로고
    • Control of mitochondrial motility and distribution by the calcium signal: a homeostatic circuit
    • Yi M., Weaver D., Hajnoczky G. Control of mitochondrial motility and distribution by the calcium signal: a homeostatic circuit. J Cell Biol 2004, 167:661-672.
    • (2004) J Cell Biol , vol.167 , pp. 661-672
    • Yi, M.1    Weaver, D.2    Hajnoczky, G.3
  • 76
    • 9244263050 scopus 로고    scopus 로고
    • Live cell imaging of mitochondrial movement along actin cables in budding yeast
    • Fehrenbacher K.L., Yang H.C., Gay A.C., Huckaba T.M., Pon L.A. Live cell imaging of mitochondrial movement along actin cables in budding yeast. Curr Biol 2004, 14:1996-2004.
    • (2004) Curr Biol , vol.14 , pp. 1996-2004
    • Fehrenbacher, K.L.1    Yang, H.C.2    Gay, A.C.3    Huckaba, T.M.4    Pon, L.A.5
  • 77
    • 3242875557 scopus 로고    scopus 로고
    • Axonal mitochondrial transport and potential are correlated
    • Miller K.E., Sheetz M.P. Axonal mitochondrial transport and potential are correlated. J Cell Sci 2004, 117:2791-2804.
    • (2004) J Cell Sci , vol.117 , pp. 2791-2804
    • Miller, K.E.1    Sheetz, M.P.2
  • 78
    • 23044432581 scopus 로고    scopus 로고
    • The GTPase dMiro is required for axonal transport of mitochondria to Drosophila synapses
    • Guo X., Macleod G.T., Wellington A., Hu F., Panchumarthi S., Schoenfield M., et al. The GTPase dMiro is required for axonal transport of mitochondria to Drosophila synapses. Neuron 2005, 47:379-393.
    • (2005) Neuron , vol.47 , pp. 379-393
    • Guo, X.1    Macleod, G.T.2    Wellington, A.3    Hu, F.4    Panchumarthi, S.5    Schoenfield, M.6
  • 79
    • 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
  • 80
    • 68949114217 scopus 로고    scopus 로고
    • Complexity of mitochondrial dynamics in neurons and its control by ADP produced during synaptic activity
    • Mironov S.L. Complexity of mitochondrial dynamics in neurons and its control by ADP produced during synaptic activity. Int J Biochem Cell Biol 2009, 41:2005-2014.
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 2005-2014
    • Mironov, S.L.1
  • 82
    • 0034938453 scopus 로고    scopus 로고
    • Human cells are protected from mitochondrial dysfunction by complementation of DNA products in fused mitochondria
    • Ono T., Isobe K., Nakada K., Hayashi J.I. Human cells are protected from mitochondrial dysfunction by complementation of DNA products in fused mitochondria. Nat Genet 2001, 28:272-275.
    • (2001) Nat Genet , vol.28 , pp. 272-275
    • Ono, T.1    Isobe, K.2    Nakada, K.3    Hayashi, J.I.4
  • 83
    • 47049105096 scopus 로고    scopus 로고
    • Human mismatch repair gene, MLH1, is transcriptionally repressed by the hypoxia-inducible transcription factors, DEC1 and DEC2
    • Nakamura H., Tanimoto K., Hiyama K., Yunokawa M., Kawamoto T., Kato Y., et al. Human mismatch repair gene, MLH1, is transcriptionally repressed by the hypoxia-inducible transcription factors, DEC1 and DEC2. Oncogene 2008, 27:4200-4209.
    • (2008) Oncogene , vol.27 , pp. 4200-4209
    • Nakamura, H.1    Tanimoto, K.2    Hiyama, K.3    Yunokawa, M.4    Kawamoto, T.5    Kato, Y.6
  • 84
    • 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
  • 86
    • 33748314528 scopus 로고    scopus 로고
    • Evidence for a mitochondrial regulatory pathway defined by peroxisome proliferator-activated receptor-gamma coactivator-1 alpha, estrogen-related receptor-alpha, and mitofusin 2
    • Soriano F.X., Liesa M., Bach D., Chan D.C., Palacin M., Zorzano A. Evidence for a mitochondrial regulatory pathway defined by peroxisome proliferator-activated receptor-gamma coactivator-1 alpha, estrogen-related receptor-alpha, and mitofusin 2. Diabetes 2006, 55:1783-1791.
    • (2006) Diabetes , vol.55 , pp. 1783-1791
    • Soriano, F.X.1    Liesa, M.2    Bach, D.3    Chan, D.C.4    Palacin, M.5    Zorzano, A.6
  • 87
    • 33745699393 scopus 로고    scopus 로고
    • OPA1 controls apoptotic cristae remodeling independently from mitochondrial fusion
    • Frezza C., Cipolat S., Martins de B.O., Micaroni M., Beznoussenko G.V., Rudka T., 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    Cipolat, S.2    Martins de, B.O.3    Micaroni, M.4    Beznoussenko, G.V.5    Rudka, T.6
  • 88
    • 43049117153 scopus 로고    scopus 로고
    • Metalloprotease-mediated OPA1 processing is modulated by the mitochondrial membrane potential
    • Guillery O., Malka F., Landes T., Guillou E., Blackstone C., Lombes A., et al. Metalloprotease-mediated OPA1 processing is modulated by the mitochondrial membrane potential. Biol Cell 2008, 100:315-325.
    • (2008) Biol Cell , vol.100 , pp. 315-325
    • Guillery, O.1    Malka, F.2    Landes, T.3    Guillou, E.4    Blackstone, C.5    Lombes, A.6


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