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Volumn 212, Issue 4, 2016, Pages 379-387

Metabolic regulation of mitochondrial dynamics

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE;

EID: 84959516439     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201511036     Document Type: Article
Times cited : (819)

References (91)
  • 2
    • 0023718495 scopus 로고
    • Coupling membranes as energy-transmitting cables. I. Filamentous mitochondria in fibroblasts and mitochondrial clusters in cardiomyocytes
    • Amchenkova, A.A., L.E. Bakeeva, Y.S. Chentsov, V.P. Skulachev, and D.B. Zorov. 1988. Coupling membranes as energy-transmitting cables. I. Filamentous mitochondria in fibroblasts and mitochondrial clusters in cardiomyocytes. J. Cell Biol. 107:481-495. http://dx.doi.org/10.1083/jcb.107.2.481
    • (1988) J. Cell Biol. , vol.107 , pp. 481-495
    • Amchenkova, A.A.1    Bakeeva, L.E.2    Chentsov, Y.S.3    Skulachev, V.P.4    Zorov, D.B.5
  • 3
    • 84896264348 scopus 로고    scopus 로고
    • The i-AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fission
    • Anand, R., T. Wai, M.J. Baker, N. Kladt, A.C. Schauss, E. Rugarli, and T. Langer. 2014. The i-AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fission. J. Cell Biol. 204:919-929. http://dx.doi.org/10.1083/jcb.201308006
    • (2014) J. Cell Biol. , vol.204 , pp. 919-929
    • Anand, R.1    Wai, T.2    Baker, M.J.3    Kladt, N.4    Schauss, A.C.5    Rugarli, E.6    Langer, T.7
  • 4
    • 84898603457 scopus 로고    scopus 로고
    • Stress-induced OMA1 activation and autocatalytic turnover regulate OPA1-dependent mitochondrial dynamics
    • Baker, M.J., P.A. Lampe, D. Stojanovski, A. Korwitz, R. Anand, T. Tatsuta, and T. Langer. 2014. Stress-induced OMA1 activation and autocatalytic turnover regulate OPA1-dependent mitochondrial dynamics. EMBO J. 33:578-593. http://dx.doi.org/10.1002/embj.201386474
    • (2014) EMBO J. , vol.33 , pp. 578-593
    • Baker, M.J.1    Lampe, P.A.2    Stojanovski, D.3    Korwitz, A.4    Anand, R.5    Tatsuta, T.6    Langer, T.7
  • 5
    • 84903281183 scopus 로고    scopus 로고
    • Membrane trafficking. Nucleoside diphosphate kinases fuel dynamin superfamily proteins with GTP for membrane remodeling
    • Boissan, M., G. Montagnac, Q. Shen, L. Griparic, J. Guitton, M. Romao, N. Sauvonnet, T. Lagache, I. Lascu, G. Raposo, et al. 2014. Membrane trafficking. Nucleoside diphosphate kinases fuel dynamin superfamily proteins with GTP for membrane remodeling. Science. 344:1510-1515. http://dx.doi.org/10.1126/science.1253768
    • (2014) Science. , vol.344 , pp. 1510-1515
    • Boissan, M.1    Montagnac, G.2    Shen, Q.3    Griparic, L.4    Guitton, J.5    Romao, M.6    Sauvonnet, N.7    Lagache, T.8    Lascu, I.9    Raposo, G.10
  • 6
    • 33748643416 scopus 로고    scopus 로고
    • Mitochondrial DNA-deletion mutations accumulate intracellularly to detrimental levels in aged human skeletal muscle fibers
    • Bua, E., J. Johnson, A. Herbst, B. Delong, D. McKenzie, S. Salamat, and J.M. Aiken. 2006. Mitochondrial DNA-deletion mutations accumulate intracellularly to detrimental levels in aged human skeletal muscle fibers. Am. J. Hum. Genet. 79:469-480. http://dx.doi.org/10.1086/507132
    • (2006) Am. J. Hum. Genet. , vol.79 , pp. 469-480
    • Bua, E.1    Johnson, J.2    Herbst, A.3    Delong, B.4    McKenzie, D.5    Salamat, S.6    Aiken, J.M.7
  • 7
    • 84926289356 scopus 로고    scopus 로고
    • Mitochondrial DNA: Impacting central and peripheral nervous systems
    • Carelli, V., and D.C. Chan. 2014. Mitochondrial DNA: Impacting central and peripheral nervous systems. Neuron. 84:1126-1142. http://dx.doi.org/10.1016/j.neuron.2014.11.022
    • (2014) Neuron. , vol.84 , pp. 1126-1142
    • Carelli, V.1    Chan, D.C.2
  • 9
    • 84869030015 scopus 로고    scopus 로고
    • Fusion and fission: Interlinked processes critical for mitochondrial health
    • Chan, D.C. 2012. Fusion and fission: Interlinked processes critical for mitochondrial health. Annu. Rev. Genet. 46:265-287. http://dx.doi.org/10.1146/annurev -genet -110410-132529
    • (2012) Annu. Rev. Genet. , vol.46 , pp. 265-287
    • Chan, D.C.1
  • 11
    • 34547611925 scopus 로고    scopus 로고
    • Cyclic AMP-dependent protein kinase phosphorylation of Drp1 regulates its GTPase activity and mitochondrial morphology
    • Chang, C.R., and C. Blackstone. 2007. Cyclic AMP-dependent protein kinase phosphorylation of Drp1 regulates its GTPase activity and mitochondrial morphology. J. Biol. Chem. 282:21583-21587. http://dx.doi.org/10.1074/jbc. C700083200
    • (2007) J. Biol. Chem. , vol.282 , pp. 21583-21587
    • Chang, C.R.1    Blackstone, C.2
  • 12
    • 84880806405 scopus 로고    scopus 로고
    • Kinesin-1-syntaphilin coupling mediates activity-dependent regulation of axonal mitochondrial transport
    • Chen, Y., and Z.H. Sheng. 2013. Kinesin-1-syntaphilin coupling mediates activity-dependent regulation of axonal mitochondrial transport. J. Cell Biol. 202:351-364. http://dx.doi.org/10.1083/jcb.201302040
    • (2013) J. Cell Biol. , vol.202 , pp. 351-364
    • Chen, Y.1    Sheng, Z.H.2
  • 13
    • 84899912073 scopus 로고    scopus 로고
    • A regulatory signaling loop comprising the PGAM5 phosphatase and CK2 controls receptor-mediated mitophagy
    • Chen, G., Z. Han, D. Feng, Y. Chen, L. Chen, H. Wu, L. Huang, C. Zhou, X. Cai, C. Fu, et al. 2014. A regulatory signaling loop comprising the PGAM5 phosphatase and CK2 controls receptor-mediated mitophagy. Mol. Cell. 54:362-377. http://dx.doi.org/10.1016/j.molcel.2014.02.034
    • (2014) Mol. Cell. , vol.54 , pp. 362-377
    • Chen, G.1    Han, Z.2    Feng, D.3    Chen, Y.4    Chen, L.5    Wu, H.6    Huang, L.7    Zhou, C.8    Cai, X.9    Fu, C.10
  • 14
    • 0037455575 scopus 로고    scopus 로고
    • Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development
    • Chen, H., S.A. Detmer, A.J. Ewald, E.E. Griffin, S.E. Fraser, and D.C. Chan. 2003. Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development. J. Cell Biol. 160:189-200. http://dx.doi.org/10.1083/jcb.200211046
    • (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
  • 15
    • 22544451586 scopus 로고    scopus 로고
    • Disruption of fusion results in mitochondrial heterogeneity and dysfunction
    • Chen, H., A. Chomyn, and D.C. Chan. 2005. Disruption of fusion results in mitochondrial heterogeneity and dysfunction. J. Biol. Chem. 280:26185-26192. http://dx.doi.org/10.1074/jbc. M503062200
    • (2005) J. Biol. Chem. , vol.280 , pp. 26185-26192
    • Chen, H.1    Chomyn, A.2    Chan, D.C.3
  • 16
    • 34547601410 scopus 로고    scopus 로고
    • Mitochondrial fusion protects against neurodegeneration in the cerebellum
    • Chen, H., J.M. McCaffery, and D.C. Chan. 2007. Mitochondrial fusion protects against neurodegeneration in the cerebellum. Cell. 130:548-562. http://dx.doi.org/10.1016/j.cell.2007.06.026
    • (2007) Cell. , vol.130 , pp. 548-562
    • Chen, H.1    McCaffery, J.M.2    Chan, D.C.3
  • 17
    • 77951737783 scopus 로고    scopus 로고
    • Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations
    • Chen, H., M. Vermulst, Y.E. Wang, A. Chomyn, T.A. Prolla, J.M. McCaffery, and D.C. Chan. 2010. Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations. Cell. 141:280-289. http://dx.doi.org/10.1016/j.cell.2010.02.026
    • (2010) Cell. , vol.141 , pp. 280-289
    • Chen, H.1    Vermulst, M.2    Wang, Y.E.3    Chomyn, A.4    Prolla, T.A.5    McCaffery, J.M.6    Chan, D.C.7
  • 19
    • 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., and S. Strack. 2007. Reversible phosphorylation of Drp1 by cyclic AMP-dependent protein kinase and calcineurin regulates mitochondrial fission and cell death. EMBO Rep. 8:939-944. http://dx.doi.org/10.1038/sj.embor.7401062
    • (2007) EMBO Rep. , vol.8 , pp. 939-944
    • Cribbs, J.T.1    Strack, S.2
  • 21
    • 0036369531 scopus 로고    scopus 로고
    • OPA1 (Kjer type) dominant optic atrophy: A novel mitochondrial disease
    • Delettre, C., G. Lenaers, L. Pelloquin, P. Belenguer, and C.P. Hamel. 2002. OPA1 (Kjer type) dominant optic atrophy: A novel mitochondrial disease. Mol. Genet. Metab. 75:97-107. http://dx.doi.org/10.1006/mgme.2001.3278
    • (2002) Mol. Genet. Metab. , vol.75 , pp. 97-107
    • Delettre, C.1    Lenaers, G.2    Pelloquin, L.3    Belenguer, P.4    Hamel, C.P.5
  • 22
    • 80155137546 scopus 로고    scopus 로고
    • PKA/AKAP1 and PP2A/Bβ2 regulate neuronal morphogenesis via Drp1 phosphorylation and mitochondrial bioenergetics
    • Dickey, A.S., and S. Strack. 2011. PKA/AKAP1 and PP2A/Bβ2 regulate neuronal morphogenesis via Drp1 phosphorylation and mitochondrial bioenergetics. J. Neurosci. 31:15716-15726. http://dx.doi.org/10.1523/JNEUROSCI.3159-11.2011
    • (2011) J. Neurosci. , vol.31 , pp. 15716-15726
    • Dickey, A.S.1    Strack, S.2
  • 23
    • 84925494009 scopus 로고    scopus 로고
    • Motif affinity and mass spectrometry proteomic approach for the discovery of cellular AMPK targets: Identification of mitochondrial fission factor as a new AMPK substrate
    • Ducommun, S., M. Deak, D. Sumpton, R.J. Ford, A. Núñez Galindo, M. Kussmann, B. Viollet, G.R. Steinberg, M. Foretz, L. Dayon, et al. 2015. Motif affinity and mass spectrometry proteomic approach for the discovery of cellular AMPK targets: Identification of mitochondrial fission factor as a new AMPK substrate. Cell. Signal. 27:978-988. http://dx.doi.org/10.1016/j.cellsig.2015.02.008
    • (2015) Cell. Signal. , vol.27 , pp. 978-988
    • Ducommun, S.1    Deak, M.2    Sumpton, D.3    Ford, R.J.4    Núñez Galindo, A.5    Kussmann, M.6    Viollet, B.7    Steinberg, G.R.8    Foretz, M.9    Dayon, L.10
  • 26
    • 0037133634 scopus 로고    scopus 로고
    • Fast 100-nm resolution threedimensional microscope reveals structural plasticity of mitochondria in live yeast
    • Egner, A., S. Jakobs, and S.W. Hell. 2002. Fast 100-nm resolution threedimensional microscope reveals structural plasticity of mitochondria in live yeast. Proc. Natl. Acad. Sci. USA. 99:3370-3375. http://dx.doi.org/10.1073/pnas.052545099
    • (2002) Proc. Natl. Acad. Sci. USA. , vol.99 , pp. 3370-3375
    • Egner, A.1    Jakobs, S.2    Hell, S.W.3
  • 28
    • 84899525169 scopus 로고    scopus 로고
    • Mitochondrial fusion is frequent in skeletal muscle and supports excitation-contraction coupling
    • Eisner, V., G. Lenaers, and G. Hajnóczky. 2014. Mitochondrial fusion is frequent in skeletal muscle and supports excitation-contraction coupling. J. Cell Biol. 205:179-195. http://dx.doi.org/10.1083/jcb.201312066
    • (2014) J. Cell Biol. , vol.205 , pp. 179-195
    • Eisner, V.1    Lenaers, G.2    Hajnóczky, G.3
  • 29
    • 0036837606 scopus 로고    scopus 로고
    • The length of cytochrome c oxidase-negative segments in muscle fibres in patients with mtDNA myopathy
    • Elson, J.L., D.C. Samuels, M.A. Johnson, D.M. Turnbull, and P.F. Chinnery. 2002. The length of cytochrome c oxidase-negative segments in muscle fibres in patients with mtDNA myopathy. Neuromuscul. Disord. 12:858-864. http://dx.doi.org/10.1016/S0960-8966(02)00047-0
    • (2002) Neuromuscul. Disord. , vol.12 , pp. 858-864
    • Elson, J.L.1    Samuels, D.C.2    Johnson, M.A.3    Turnbull, D.M.4    Chinnery, P.F.5
  • 30
    • 44649129342 scopus 로고    scopus 로고
    • The novel tail-anchored membrane protein Mffcontrols mitochondrial and peroxisomal fission in mammalian cells
    • Gandre-Babbe, S., and A.M. van der Bliek. 2008. The novel tail-anchored membrane protein Mffcontrols mitochondrial and peroxisomal fission in mammalian cells. Mol. Biol. Cell. 19:2402-2412. http://dx.doi.org/10.1091/mbc. E07-12-1287
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 2402-2412
    • Gandre-Babbe, S.1    van der Bliek, A.M.2
  • 31
    • 79955623510 scopus 로고    scopus 로고
    • During autophagy mitochondria elongate, are spared from degradation and sustain cell viability
    • Gomes, L.C., G. Di Benedetto, and L. Scorrano. 2011. During autophagy mitochondria elongate, are spared from degradation and sustain cell viability. Nat. Cell Biol. 13:589-598. http://dx.doi.org/10.1038/ncb2220
    • (2011) Nat. Cell Biol. , vol.13 , pp. 589-598
    • Gomes, L.C.1    Di Benedetto, G.2    Scorrano, L.3
  • 33
    • 76149093590 scopus 로고    scopus 로고
    • Inducible proteolytic inactivation of OPA1 mediated by the OMA1 protease in mammalian cells
    • Head, B., L. Griparic, M. Amiri, S. Gandre-Babbe, and A.M. van der Bliek. 2009. Inducible proteolytic inactivation of OPA1 mediated by the OMA1 protease in mammalian cells. J. Cell Biol. 187:959-966. http://dx.doi.org/10.1083/jcb.200906083
    • (2009) J. Cell Biol. , vol.187 , pp. 959-966
    • Head, B.1    Griparic, L.2    Amiri, M.3    Gandre-Babbe, S.4    van der Bliek, A.M.5
  • 35
    • 78651468702 scopus 로고    scopus 로고
    • The soluble form of Bax regulates mitochondrial fusion via MFN2 homotypic complexes
    • Hoppins, S., F. Edlich, M.M. Cleland, S. Banerjee, J.M. McCaffery, R.J. Youle, and J. Nunnari. 2011. The soluble form of Bax regulates mitochondrial fusion via MFN2 homotypic complexes. Mol. Cell. 41:150-160. http://dx.doi.org/10.1016/j.molcel.2010.11.030
    • (2011) Mol. Cell. , vol.41 , pp. 150-160
    • Hoppins, S.1    Edlich, F.2    Cleland, M.M.3    Banerjee, S.4    McCaffery, J.M.5    Youle, R.J.6    Nunnari, J.7
  • 36
    • 33746299692 scopus 로고    scopus 로고
    • Regulation of mitochondrial morphology through proteolytic cleavage of OPA1
    • Ishihara, N., Y. Fujita, T. Oka, and K. Mihara. 2006. Regulation of mitochondrial morphology through proteolytic cleavage of OPA1. EMBO J. 25:2966-2977. http://dx.doi.org/10.1038/sj.emboj.7601184
    • (2006) EMBO J. , vol.25 , pp. 2966-2977
    • Ishihara, N.1    Fujita, Y.2    Oka, T.3    Mihara, K.4
  • 37
    • 0037768628 scopus 로고    scopus 로고
    • Spatial and temporal dynamics of budding yeast mitochondria lacking the division component Fis1p
    • Jakobs, S., N. Martini, A.C. Schauss, A. Egner, B. Westermann, and S.W. Hell. 2003. Spatial and temporal dynamics of budding yeast mitochondria lacking the division component Fis1p. J. Cell Sci. 116:2005-2014. http://dx.doi.org/10.1242/jcs.00423
    • (2003) J. Cell Sci. , vol.116 , pp. 2005-2014
    • Jakobs, S.1    Martini, N.2    Schauss, A.C.3    Egner, A.4    Westermann, B.5    Hell, S.W.6
  • 38
    • 37749053855 scopus 로고    scopus 로고
    • Docking of axonal mitochondria by syntaphilin controls their mobility and affects short-term facilitation
    • Kang, J.S., J.H. Tian, P.Y. Pan, P. Zald, C. Li, C. Deng, and Z.H. Sheng. 2008. Docking of axonal mitochondria by syntaphilin controls their mobility and affects short-term facilitation. Cell. 132:137-148. http://dx.doi.org/10.1016/j.cell.2007.11.024
    • (2008) Cell. , vol.132 , pp. 137-148
    • Kang, J.S.1    Tian, J.H.2    Pan, P.Y.3    Zald, P.4    Li, C.5    Deng, C.6    Sheng, Z.H.7
  • 40
    • 84908250304 scopus 로고    scopus 로고
    • Determinants and functions of mitochondrial behavior
    • Labbé, K., A. Murley, and J. Nunnari. 2014. Determinants and functions of mitochondrial behavior. Annu. Rev. Cell Dev. Biol. 30:357-391. http://dx.doi.org/10.1146/annurev -cellbio -101011-155756
    • (2014) Annu. Rev. Cell Dev. Biol. , vol.30 , pp. 357-391
    • Labbé, K.1    Murley, A.2    Nunnari, J.3
  • 41
    • 67449124361 scopus 로고    scopus 로고
    • HUMMR, a hypoxia- and HIF-1alpha-inducible protein, alters mitochondrial distribution and transport
    • Li, Y., S. Lim, D. Hoffman, P. Aspenstrom, H.J. Federoff, and D.A. Rempe. 2009. HUMMR, a hypoxia- and HIF-1alpha-inducible protein, alters mitochondrial distribution and transport. J. Cell Biol. 185:1065-1081. http://dx.doi.org/10.1083/jcb.200811033
    • (2009) J. Cell Biol. , vol.185 , pp. 1065-1081
    • Li, Y.1    Lim, S.2    Hoffman, D.3    Aspenstrom, P.4    Federoff, H.J.5    Rempe, D.A.6
  • 42
    • 84942287874 scopus 로고    scopus 로고
    • Mutations causing mitochondrial disease: What is new and what challenges remain?
    • Lightowlers, R.N., R.W. Taylor, and D.M. Turnbull. 2015. Mutations causing mitochondrial disease: What is new and what challenges remain? Science. 349:1494-1499. http://dx.doi.org/10.1126/science.aac7516
    • (2015) Science. , vol.349 , pp. 1494-1499
    • Lightowlers, R.N.1    Taylor, R.W.2    Turnbull, D.M.3
  • 43
    • 84862789618 scopus 로고    scopus 로고
    • Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells
    • Liu, L., D. Feng, G. Chen, M. Chen, Q. Zheng, P. Song, Q. Ma, C. Zhu, R. Wang, W. Qi, et al. 2012. Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells. Nat. Cell Biol. 14:177-185. http://dx.doi.org/10.1038/ncb2422
    • (2012) Nat. Cell Biol. , vol.14 , pp. 177-185
    • Liu, L.1    Feng, D.2    Chen, G.3    Chen, M.4    Zheng, Q.5    Song, P.6    Ma, Q.7    Zhu, C.8    Wang, R.9    Qi, W.10
  • 44
    • 84874639591 scopus 로고    scopus 로고
    • Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission
    • Losón, O.C., Z. Song, H. Chen, and D.C. Chan. 2013. Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission. Mol. Biol. Cell. 24:659-667. http://dx.doi.org/10.1091/mbc. E12-10-0721
    • (2013) Mol. Biol. Cell. , vol.24 , pp. 659-667
    • Losón, O.C.1    Song, Z.2    Chen, H.3    Chan, D.C.4
  • 45
    • 84896739005 scopus 로고    scopus 로고
    • The mitochondrial fission receptor MiD51 requires ADP as a cofactor
    • Losón, O.C., R. Liu, M.E. Rome, S. Meng, J.T. Kaiser, S.O. Shan, and D.C. Chan. 2014. The mitochondrial fission receptor MiD51 requires ADP as a cofactor. Structure. 22:367-377. http://dx.doi.org/10.1016/j.str.2014.01.001
    • (2014) Structure. , vol.22 , pp. 367-377
    • Losón, O.C.1    Liu, R.2    Rome, M.E.3    Meng, S.4    Kaiser, J.T.5    Shan, S.O.6    Chan, D.C.7
  • 46
    • 84941425977 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of MiD49, a receptor for the mitochondrial fission protein Drp1
    • Losón, O.C., S. Meng, H. Ngo, R. Liu, J.T. Kaiser, and D.C. Chan. 2015. Crystal structure and functional analysis of MiD49, a receptor for the mitochondrial fission protein Drp1. Protein Sci. 24:386-394. http://dx.doi.org/10.1002/pro.2629
    • (2015) Protein Sci. , vol.24 , pp. 386-394
    • Losón, O.C.1    Meng, S.2    Ngo, H.3    Liu, R.4    Kaiser, J.T.5    Chan, D.C.6
  • 48
    • 77951181836 scopus 로고    scopus 로고
    • PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy
    • Matsuda, N., S. Sato, K. Shiba, K. Okatsu, K. Saisho, C.A. Gautier, Y.S. Sou, S. Saiki, S. Kawajiri, F. Sato, et al. 2010. PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy. J. Cell Biol. 189:211-221. http://dx.doi.org/10.1083/jcb.200910140
    • (2010) J. Cell Biol. , vol.189 , pp. 211-221
    • Matsuda, N.1    Sato, S.2    Shiba, K.3    Okatsu, K.4    Saisho, K.5    Gautier, C.A.6    Sou, Y.S.7    Saiki, S.8    Kawajiri, S.9    Sato, F.10
  • 49
    • 84897863239 scopus 로고    scopus 로고
    • Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control
    • McLelland, G.L., V. Soubannier, C.X. Chen, H.M. McBride, and E.A. Fon. 2014. Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control. EMBO J. 33:282-295.
    • (2014) EMBO J. , vol.33 , pp. 282-295
    • McLelland, G.L.1    Soubannier, V.2    Chen, C.X.3    McBride, H.M.4    Fon, E.A.5
  • 50
    • 0038700756 scopus 로고    scopus 로고
    • Mitochondrial membrane remodelling regulated by a conserved rhomboid protease
    • McQuibban, G.A., S. Saurya, and M. Freeman. 2003. Mitochondrial membrane remodelling regulated by a conserved rhomboid protease. Nature. 423:537-541. http://dx.doi.org/10.1038/nature01633
    • (2003) Nature. , vol.423 , pp. 537-541
    • McQuibban, G.A.1    Saurya, S.2    Freeman, M.3
  • 51
    • 4544378532 scopus 로고    scopus 로고
    • Mitochondrial fusion intermediates revealed in vitro
    • Meeusen, S., J.M. McCaffery, and J. Nunnari. 2004. Mitochondrial fusion intermediates revealed in vitro. Science. 305:1747-1752. http://dx.doi.org/10.1126/science.1100612
    • (2004) Science. , vol.305 , pp. 1747-1752
    • Meeusen, S.1    McCaffery, J.M.2    Nunnari, J.3
  • 53
    • 34147149003 scopus 로고    scopus 로고
    • ADP regulates movements of mitochondria in neurons
    • Mironov, S.L. 2007. ADP regulates movements of mitochondria in neurons. Biophys. J. 92:2944-2952. http://dx.doi.org/10.1529/biophysj.106.092981
    • (2007) Biophys. J. , vol.92 , pp. 2944-2952
    • Mironov, S.L.1
  • 54
    • 84910141948 scopus 로고    scopus 로고
    • Mitochondrial dynamics and inheritance during cell division, development and disease
    • Mishra, P., and D.C. Chan. 2014. Mitochondrial dynamics and inheritance during cell division, development and disease. Nat. Rev. Mol. Cell Biol. 15:634-646. http://dx.doi.org/10.1038/nrm3877
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 634-646
    • Mishra, P.1    Chan, D.C.2
  • 55
    • 84897538678 scopus 로고    scopus 로고
    • Proteolytic cleavage of Opa1 stimulates mitochondrial inner membrane fusion and couples fusion to oxidative phosphorylation
    • Mishra, P., V. Carelli, G. Manfredi, and D.C. Chan. 2014. Proteolytic cleavage of Opa1 stimulates mitochondrial inner membrane fusion and couples fusion to oxidative phosphorylation. Cell Metab. 19:630-641. http://dx.doi.org/10.1016/j.cmet.2014.03.011
    • (2014) Cell Metab. , vol.19 , pp. 630-641
    • Mishra, P.1    Carelli, V.2    Manfredi, G.3    Chan, D.C.4
  • 56
    • 84951335747 scopus 로고    scopus 로고
    • Mitochondrial dynamics is a distinguishing feature of skeletal muscle fiber types and regulates organellar compartmentalization
    • Mishra, P., G. Varuzhanyan, A.H. Pham, and D.C. Chan. 2015. Mitochondrial dynamics is a distinguishing feature of skeletal muscle fiber types and regulates organellar compartmentalization. Cell Metab. 22:1033-1044. http://dx.doi.org/10.1016/j.cmet.2015.09.027
    • (2015) Cell Metab. , vol.22 , pp. 1033-1044
    • Mishra, P.1    Varuzhanyan, G.2    Pham, A.H.3    Chan, D.C.4
  • 57
    • 67749089562 scopus 로고    scopus 로고
    • A hyperfused mitochondrial state achieved at G1-S regulates cyclin E buildup and entry into S phase
    • Mitra, K., C. Wunder, B. Roysam, G. Lin, and J. Lippincott-Schwartz. 2009. A hyperfused mitochondrial state achieved at G1-S regulates cyclin E buildup and entry into S phase. Proc. Natl. Acad. Sci. USA. 106:11960-11965. http://dx.doi.org/10.1073/pnas.0904875106
    • (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
  • 58
    • 0026907560 scopus 로고
    • Molecular analysis of the muscle pathology associated with mitochondrial DNA deletions
    • Moraes, C.T., E. Ricci, V. Petruzzella, S. Shanske, S. DiMauro, E.A. Schon, and E. Bonilla. 1992. Molecular analysis of the muscle pathology associated with mitochondrial DNA deletions. Nat. Genet. 1:359-367. http://dx.doi.org/10.1038/ng0892-359
    • (1992) Nat. Genet. , vol.1 , pp. 359-367
    • Moraes, C.T.1    Ricci, E.2    Petruzzella, V.3    Shanske, S.4    DiMauro, S.5    Schon, E.A.6    Bonilla, E.7
  • 61
  • 62
    • 78650167618 scopus 로고    scopus 로고
    • Mffis an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells
    • Otera, H., C. Wang, M.M. Cleland, K. Setoguchi, S. Yokota, R.J. Youle, and K. Mihara. 2010. Mffis an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells. J. Cell Biol. 191:1141-1158. http://dx.doi.org/10.1083/jcb.201007152
    • (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
  • 63
    • 84903975888 scopus 로고    scopus 로고
    • Glucose regulates mitochondrial motility via Milton modification by O-GlcNAc transferase
    • Pekkurnaz, G., J.C. Trinidad, X. Wang, D. Kong, and T.L. Schwarz. 2014. Glucose regulates mitochondrial motility via Milton modification by O-GlcNAc transferase. Cell. 158:54-68. http://dx.doi.org/10.1016/j.cell.2014.06.007
    • (2014) Cell. , vol.158 , pp. 54-68
    • Pekkurnaz, G.1    Trinidad, J.C.2    Wang, X.3    Kong, D.4    Schwarz, T.L.5
  • 65
    • 84870060160 scopus 로고    scopus 로고
    • Mouse lines with photoactivatable mitochondria to study mitochondrial dynamics
    • Pham, A.H., J.M. McCaffery, and D.C. Chan. 2012. Mouse lines with photoactivatable mitochondria to study mitochondrial dynamics. Genesis. 50:833-843. http://dx.doi.org/10.1002/dvg.22050
    • (2012) Genesis. , vol.50 , pp. 833-843
    • Pham, A.H.1    McCaffery, J.M.2    Chan, D.C.3
  • 66
    • 33646759268 scopus 로고    scopus 로고
    • Kinesin-1 and dynein are the primary motors for fast transport of mitochondria in Drosophila motor axons
    • Pilling, A.D., D. Horiuchi, C.M. Lively, and W.M. Saxton. 2006. Kinesin-1 and dynein are the primary motors for fast transport of mitochondria in Drosophila motor axons. Mol. Biol. Cell. 17:2057-2068. http://dx.doi.org/10.1091/mbc. E05-06-0526
    • (2006) Mol. Biol. Cell. , vol.17 , pp. 2057-2068
    • Pilling, A.D.1    Horiuchi, D.2    Lively, C.M.3    Saxton, W.M.4
  • 67
    • 84928212582 scopus 로고    scopus 로고
    • Extracellular regulated kinase phosphorylates mitofusin 1 to control mitochondrial morphology and apoptosis
    • Pyakurel, A., C. Savoia, D. Hess, and L. Scorrano. 2015. Extracellular regulated kinase phosphorylates mitofusin 1 to control mitochondrial morphology and apoptosis. Mol. Cell. 58:244-254. http://dx.doi.org/10.1016/j.molcel.2015.02.021
    • (2015) Mol. Cell. , vol.58 , pp. 244-254
    • Pyakurel, A.1    Savoia, C.2    Hess, D.3    Scorrano, L.4
  • 68
    • 79959987510 scopus 로고    scopus 로고
    • Tubular network formation protects mitochondria from autophagosomal degradation during nutrient starvation
    • Rambold, A.S., B. Kostelecky, N. Elia, and J. Lippincott-Schwartz. 2011. Tubular network formation protects mitochondria from autophagosomal degradation during nutrient starvation. Proc. Natl. Acad. Sci. USA. 108:10190-10195. http://dx.doi.org/10.1073/pnas.1107402108
    • (2011) Proc. Natl. Acad. Sci. USA. , vol.108 , pp. 10190-10195
    • Rambold, A.S.1    Kostelecky, B.2    Elia, N.3    Lippincott-Schwartz, J.4
  • 70
    • 0842325793 scopus 로고    scopus 로고
    • Energy substrate modulates mitochondrial structure and oxidative capacity in cancer cells
    • Rossignol, R., R. Gilkerson, R. Aggeler, K. Yamagata, S.J. Remington, and R.A. Capaldi. 2004. Energy substrate modulates mitochondrial structure and oxidative capacity in cancer cells. Cancer Res. 64:985-993. http://dx.doi.org/10.1158/0008-5472.CAN -03-1101
    • (2004) Cancer Res. , vol.64 , pp. 985-993
    • Rossignol, R.1    Gilkerson, R.2    Aggeler, R.3    Yamagata, K.4    Remington, S.J.5    Capaldi, R.A.6
  • 71
    • 84880213863 scopus 로고    scopus 로고
    • OPA1 promotes pH flashes that spread between contiguous mitochondria without matrix protein exchange
    • Santo-Domingo, J., M. Giacomello, D. Poburko, L. Scorrano, and N. Demaurex. 2013. OPA1 promotes pH flashes that spread between contiguous mitochondria without matrix protein exchange. EMBO J. 32:1927-1940. http://dx.doi.org/10.1038/emboj.2013.124
    • (2013) EMBO J. , vol.32 , pp. 1927-1940
    • Santo-Domingo, J.1    Giacomello, M.2    Poburko, D.3    Scorrano, L.4    Demaurex, N.5
  • 72
    • 84876296881 scopus 로고    scopus 로고
    • Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization
    • Sarraf, S.A., M. Raman, V. Guarani-Pereira, M.E. Sowa, E.L. Huttlin, S.P. Gygi, and J.W. Harper. 2013. Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization. Nature. 496:372-376. http://dx.doi.org/10.1038/nature12043
    • (2013) Nature. , vol.496 , pp. 372-376
    • Sarraf, S.A.1    Raman, M.2    Guarani-Pereira, V.3    Sowa, M.E.4    Huttlin, E.L.5    Gygi, S.P.6    Harper, J.W.7
  • 73
    • 84862870271 scopus 로고    scopus 로고
    • The axonal transport of mitochondria
    • Saxton, W.M., and P.J. Hollenbeck. 2012. The axonal transport of mitochondria. J. Cell Sci. 125:2095-2104. http://dx.doi.org/10.1242/jcs.053850
    • (2012) J. Cell Sci. , vol.125 , pp. 2095-2104
    • Saxton, W.M.1    Hollenbeck, P.J.2
  • 76
    • 84867032955 scopus 로고    scopus 로고
    • The intracellular redox state is a core determinant of mitochondrial fusion
    • Shutt, T., M. Geoffrion, R. Milne, and H.M. McBride. 2012. The intracellular redox state is a core determinant of mitochondrial fusion. EMBO Rep. 13:909-915. http://dx.doi.org/10.1038/embor.2012.128
    • (2012) EMBO Rep. , vol.13 , pp. 909-915
    • Shutt, T.1    Geoffrion, M.2    Milne, R.3    McBride, H.M.4
  • 77
    • 0035146891 scopus 로고    scopus 로고
    • Mitochondrial filaments and clusters as intracellular power-transmitting cables
    • Skulachev, V.P. 2001. Mitochondrial filaments and clusters as intracellular power-transmitting cables. Trends Biochem. Sci. 26:23-29. http://dx.doi.org/10.1016/S0968-0004(00)01735-7
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 23-29
    • Skulachev, V.P.1
  • 78
    • 34548313688 scopus 로고    scopus 로고
    • OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L
    • Song, Z., H. Chen, M. Fiket, C. Alexander, and D.C. Chan. 2007. OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L. J. Cell Biol. 178:749-755. http://dx.doi.org/10.1083/jcb.200704110
    • (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
  • 79
    • 0037137704 scopus 로고    scopus 로고
    • Axonal transport of mitochondria to synapses depends on milton, a novel Drosophila protein
    • Stowers, R.S., L.J. Megeath, J. Górska-Andrzejak, I.A. Meinertzhagen, and T.L. Schwarz. 2002. Axonal transport of mitochondria to synapses depends on milton, a novel Drosophila protein. Neuron. 36:1063-1077. http://dx.doi.org/10.1016/S0896-6273(02)01094-2
    • (2002) Neuron. , vol.36 , pp. 1063-1077
    • Stowers, R.S.1    Megeath, L.J.2    Górska-Andrzejak, J.3    Meinertzhagen, I.A.4    Schwarz, T.L.5
  • 80
    • 84908085343 scopus 로고    scopus 로고
    • A new pathway for mitochondrial quality control: Mitochondrial-derived vesicles
    • Sugiura, A., G.L. McLelland, E.A. Fon, and H.M. McBride. 2014. A new pathway for mitochondrial quality control: Mitochondrial-derived vesicles. EMBO J. 33:2142-2156. http://dx.doi.org/10.15252/embj.201488104
    • (2014) EMBO J. , vol.33 , pp. 2142-2156
    • Sugiura, A.1    McLelland, G.L.2    Fon, E.A.3    McBride, H.M.4
  • 82
    • 84899907498 scopus 로고    scopus 로고
    • AMP-activated protein kinase mediates activity-dependent axon branching by recruiting mitochondria to axon
    • Tao, K., N. Matsuki, and R. Koyama. 2014. AMP-activated protein kinase mediates activity-dependent axon branching by recruiting mitochondria to axon. Dev. Neurobiol. 74:557-573. http://dx.doi.org/10.1002/dneu.22149
    • (2014) Dev. Neurobiol. , vol.74 , pp. 557-573
    • Tao, K.1    Matsuki, N.2    Koyama, R.3
  • 87
    • 58149091896 scopus 로고    scopus 로고
    • The mechanism of Ca2+-dependent regulation of kinesin-mediated mitochondrial motility
    • Wang, X., and T.L. Schwarz. 2009. The mechanism of Ca2+-dependent regulation of kinesin-mediated mitochondrial motility. Cell. 136:163-174. http://dx.doi.org/10.1016/j.cell.2008.11.046
    • (2009) Cell. , vol.136 , pp. 163-174
    • Wang, X.1    Schwarz, T.L.2
  • 90
    • 0014784078 scopus 로고
    • The midpiece of the mouse spermatozoon: Its form and development as seen by surface replication
    • Woolley, D.M. 1970. The midpiece of the mouse spermatozoon: Its form and development as seen by surface replication. J. Cell Sci. 6:865-879.
    • (1970) J. Cell Sci. , vol.6 , pp. 865-879
    • Woolley, D.M.1


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