메뉴 건너뛰기




Volumn 15, Issue 10, 2014, Pages 634-646

Mitochondrial dynamics and inheritance during cell division, development and disease

Author keywords

[No Author keywords available]

Indexed keywords

DNA; MITOCHONDRIAL DNA;

EID: 84910141948     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm3877     Document Type: Review
Times cited : (785)

References (138)
  • 2
    • 84897000909 scopus 로고    scopus 로고
    • Mitochondrial iron-sulfur protein biogenesis and human disease
    • Stehling, O., Wilbrecht, C., & Lill, R. Mitochondrial iron-sulfur protein biogenesis and human disease. Biochimie 100, 61-77 (2014
    • (2014) Biochimie , vol.100 , pp. 61-77
    • Stehling, O.1    Wilbrecht, C.2    Lill, R.3
  • 3
    • 77956095537 scopus 로고    scopus 로고
    • Mitochondria and cell death: Outer membrane permeabilization and beyond
    • Tait, S. W., & Green, D. R. Mitochondria and cell death: outer membrane permeabilization and beyond. Nature Rev. Mol. Cell Biol. 11, 621-632 (2010
    • (2010) Nature Rev. Mol. Cell Biol. , vol.11 , pp. 621-632
    • Tait, S.W.1    Green, D.2
  • 4
    • 84881548201 scopus 로고    scopus 로고
    • Mitochondria: Sensors and mediators of innate immune receptor signaling
    • Cloonan, S. M., & Choi, A. M. Mitochondria: sensors and mediators of innate immune receptor signaling. Curr. Opin. Microbiol. 16, 327-338 (2013
    • (2013) Curr. Opin. Microbiol. , vol.16 , pp. 327-338
    • Cloonan, S.M.1    Choi, A.2
  • 5
    • 0033525788 scopus 로고    scopus 로고
    • Mitochondrial evolution
    • Gray, M. W., Burger, G., & Lang, B. F. Mitochondrial evolution. Science 283, 1476-1481 (1999
    • (1999) Science , vol.283 , pp. 1476-1481
    • Gray, M.W.1    Burger, G.2    Lang, B.F.3
  • 6
    • 84869030015 scopus 로고    scopus 로고
    • Fusion and fission: Interlinked processes critical for mitochondrial health
    • Chan, D. C. Fusion and fission: interlinked processes critical for mitochondrial health. Annu. Rev. Genet. 46, 265-287 (2012
    • (2012) Annu. Rev. Genet. , vol.46 , pp. 265-287
    • Chan, D.1
  • 7
    • 0039064824 scopus 로고
    • Mitochondria are associated with microtubules and not with intermediate filaments in cultured fibroblasts
    • Ball, E. H., & Singer, S. J. Mitochondria are associated with microtubules and not with intermediate filaments in cultured fibroblasts. Proc. Natl Acad. Sci. USA 79, 123-126 (1982
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 123-126
    • Ball, E.H.1    Singer, S.J.2
  • 8
    • 0008688565 scopus 로고
    • Association of mitochondria with microtubules in cultured cells
    • Heggeness, M. H., Simon, M., & Singer, S. J. Association of mitochondria with microtubules in cultured cells. Proc. Natl Acad. Sci. USA 75, 3863-3866 (1978
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 3863-3866
    • Heggeness, M.H.1    Simon, M.2    Singer, S.J.3
  • 9
    • 84856056846 scopus 로고    scopus 로고
    • Mitochondrial transport in neurons: Impact on synaptic homeostasis and neurodegeneration
    • Sheng, Z. H., & Cai, Q. Mitochondrial transport in neurons: impact on synaptic homeostasis and neurodegeneration. Nature Rev. Neurosci. 13, 77-93 (2012
    • (2012) Nature Rev. Neurosci. , vol.13 , pp. 77-93
    • Sheng, Z.H.1    Cai, Q.2
  • 10
    • 0032568790 scopus 로고    scopus 로고
    • Targeted disruption of mouse conventional kinesin heavy chain, kif5b, results in abnormal perinuclear clustering of mitochondria
    • Tanaka, Y. et al. Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria. Cell 93, 1147-1158 (1998
    • (1998) Cell , vol.93 , pp. 1147-1158
    • Tanaka, Y.1
  • 11
    • 79960402471 scopus 로고    scopus 로고
    • Klp6: A newly identified kinesin that regulates the morphology and transport of mitochondria in neuronal cells
    • Tanaka, K., Sugiura, Y., Ichishita, R., Mihara, K., & Oka, T. KLP6: a newly identified kinesin that regulates the morphology and transport of mitochondria in neuronal cells. J. Cell Sci. 124, 2457-2465 (2011
    • (2011) J. Cell Sci. , vol.124 , pp. 2457-2465
    • Tanaka, K.1    Sugiura, Y.2    Ichishita, R.3    Mihara, K.4    Oka, T.5
  • 12
    • 50349090965 scopus 로고    scopus 로고
    • Intracellular transport and kinesin superfamily proteins, kifs: Structure, function, and dynamics
    • Hirokawa, N., & Noda, Y. Intracellular transport and kinesin superfamily proteins, KIFs: structure, function, and dynamics. Physiol. Rev. 88, 1089-1118 (2008
    • (2008) Physiol. Rev. , vol.88 , pp. 1089-1118
    • Hirokawa, N.1    Noda, Y.2
  • 13
    • 0028641560 scopus 로고
    • Kif1b, a novel microtubule plus end-directed monomeric motor protein for transport of mitochondria
    • Nangaku, M. et al. KIF1B, a novel microtubule plus end-directed monomeric motor protein for transport of mitochondria. Cell 79, 1209-1220 (1994
    • (1994) Cell , vol.79 , pp. 1209-1220
    • Nangaku, M.1
  • 14
    • 84862870271 scopus 로고    scopus 로고
    • The axonal transport of mitochondria
    • Saxton, W. M., & Hollenbeck, P. J. The axonal transport of mitochondria. J. Cell Sci. 125, 2095-2104 (2012
    • (2012) J. Cell Sci. , vol.125 , pp. 2095-2104
    • Saxton, W.M.1    Hollenbeck, P.J.2
  • 15
    • 0037137704 scopus 로고    scopus 로고
    • Axonal transport of mitochondria to synapses depends on milton, a novel drosophila protein
    • Stowers, R. S., Megeath, L. J., Gorska-Andrzejak, J., Meinertzhagen, I. A., & Schwarz, T. L. Axonal transport of mitochondria to synapses depends on milton, a novel Drosophila protein. Neuron 36, 1063-1077 (2002
    • (2002) Neuron , vol.36 , pp. 1063-1077
    • Stowers, R.S.1    Megeath, L.J.2    Gorska-Andrzejak, J.3    Meinertzhagen, I.A.4    Schwarz, T.L.5
  • 16
    • 23044432581 scopus 로고    scopus 로고
    • The gtpase dmiro is required for axonal transport of mitochondria to drosophila synapses
    • Guo, X. et al. The GTPase dMiro is required for axonal transport of mitochondria to Drosophila synapses. Neuron 47, 379-393 (2005
    • (2005) Neuron , vol.47 , pp. 379-393
    • Guo, X.1
  • 17
    • 58149091896 scopus 로고    scopus 로고
    • The mechanism of ca2+-dependent regulation of kinesin-mediated mitochondrial motility
    • Wang, X., & Schwarz, T. L. The mechanism of Ca2+-dependent regulation of kinesin-mediated mitochondrial motility. Cell 136, 163-174 (2009
    • (2009) Cell , vol.136 , pp. 163-174
    • Wang, X.1    Schwarz, T.L.2
  • 18
    • 37749053855 scopus 로고    scopus 로고
    • Docking of axonal mitochondria by syntaphilin controls their mobility and affects short-term facilitation
    • Kang, J. S. et al. Docking of axonal mitochondria by syntaphilin controls their mobility and affects short-term facilitation. Cell 132, 137-148 (2008
    • (2008) Cell , vol.132 , pp. 137-148
    • Kang, J.S.1
  • 19
    • 84880806405 scopus 로고    scopus 로고
    • Kinesin-1-syntaphilin coupling mediates activity-dependent regulation of axonal mitochondrial transport
    • Chen, Y., & Sheng, Z. H. Kinesin-1-syntaphilin coupling mediates activity-dependent regulation of axonal mitochondrial transport. J. Cell Biol. 202, 351-364 (2013
    • (2013) J. Cell Biol. , vol.202 , pp. 351-364
    • Chen, Y.1    Sheng, Z.H.2
  • 20
    • 33646768127 scopus 로고    scopus 로고
    • Axonal transport of mitochondria requires milton to recruit kinesin heavy chain and is light chain independent
    • Glater, E. E., Megeath, L. J., Stowers, R. S., & Schwarz, T. L. Axonal transport of mitochondria requires milton to recruit kinesin heavy chain and is light chain independent. J. Cell Biol. 173, 545-557 (2006
    • (2006) J. Cell Biol. , vol.173 , pp. 545-557
    • Glater, E.E.1    Megeath, L.J.2    Stowers, R.S.3    Schwarz, T.L.4
  • 21
    • 84873279659 scopus 로고    scopus 로고
    • Trak/milton motor-Adaptor proteins steer mitochondrial trafficking to axons and dendrites
    • van Spronsen, M. et al. TRAK/Milton motor-Adaptor proteins steer mitochondrial trafficking to axons and dendrites. Neuron 77, 485-502 (2013
    • (2013) Neuron , vol.77 , pp. 485-502
    • Van Spronsen, M.1
  • 22
    • 84865544952 scopus 로고    scopus 로고
    • Mitochondrial fission, fusion, and stress
    • Youle, R. J., & van der Bliek, A. M. Mitochondrial fission, fusion, and stress. Science 337, 1062-1065 (2012
    • (2012) Science , vol.337 , pp. 1062-1065
    • Youle, R.J.1    Van Der Bliek, A.M.2
  • 23
    • 77951737783 scopus 로고    scopus 로고
    • Mitochondrial fusion is required for mtdna stability in skeletal muscle and tolerance of mtdna mutations
    • Chen, H. et al. Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations. Cell 141, 280-289 (2010
    • (2010) Cell , vol.141 , pp. 280-289
    • Chen, H.1
  • 24
    • 0037455575 scopus 로고    scopus 로고
    • Mitofusins mfn1 and mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development
    • Chen, H. et al. Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development. J. Cell Biol. 160, 189-200 (2003
    • (2003) J. Cell Biol. , vol.160 , pp. 189-200
    • Chen, H.1
  • 25
    • 68249087424 scopus 로고    scopus 로고
    • Mitochondrial fission factor drp1 is essential for embryonic development and synapse formation in mice
    • Ishihara, N. et al. Mitochondrial fission factor Drp1 is essential for embryonic development and synapse formation in mice. Nature Cell Biol. 11, 958-966 (2009
    • (2009) Nature Cell Biol. , vol.11 , pp. 958-966
    • Ishihara, N.1
  • 26
    • 70349944660 scopus 로고    scopus 로고
    • The dynamin-related gtpase drp1 is required for embryonic and brain development in mice
    • Wakabayashi, J. et al. The dynamin-related GTPase Drp1 is required for embryonic and brain development in mice. J. Cell Biol. 186, 805-816 (2009
    • (2009) J. Cell Biol. , vol.186 , pp. 805-816
    • Wakabayashi, J.1
  • 27
    • 34547601410 scopus 로고    scopus 로고
    • Mitochondrial fusion protects against neurodegeneration in the cerebellum
    • Chen, H., McCaffery, J. M., & Chan, D. C. Mitochondrial fusion protects against neurodegeneration in the cerebellum. Cell 130, 548-562 (2007
    • (2007) Cell , vol.130 , pp. 548-562
    • Chen, H.1    McCaffery, J.M.2    Chan, D.C.3
  • 28
    • 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. 280, 26185-26192 (2005
    • (2005) J. Biol. Chem. , vol.280 , pp. 26185-26192
    • Chen, H.1    Chomyn, A.2    Chan, D.C.3
  • 29
    • 84901914053 scopus 로고    scopus 로고
    • Distribution and apoptotic function of outer membrane proteins depend on mitochondrial fusion
    • Weaver, D. et al. Distribution and apoptotic function of outer membrane proteins depend on mitochondrial fusion. Mol. Cell 54, 870-878 (2014
    • (2014) Mol. Cell , vol.54 , pp. 870-878
    • Weaver, D.1
  • 30
    • 38549110110 scopus 로고    scopus 로고
    • Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
    • Twig, G. et al. Fission and selective fusion govern mitochondrial segregation and elimination by autophagy. EMBO J. 27, 433-446 (2008
    • (2008) EMBO J. , vol.27 , pp. 433-446
    • Twig, G.1
  • 31
    • 33746299692 scopus 로고    scopus 로고
    • Regulation of mitochondrial morphology through proteolytic cleavage of opa1
    • Ishihara, N., Fujita, Y., Oka, T., & Mihara, K. Regulation of mitochondrial morphology through proteolytic cleavage of OPA1. EMBO J. 25, 2966-2977 (2006
    • (2006) EMBO J. , vol.25 , pp. 2966-2977
    • Ishihara, N.1    Fujita, Y.2    Oka, T.3    Mihara, K.4
  • 32
    • 0035487808 scopus 로고    scopus 로고
    • The role of dynamin-related protein 1, a mediator of mitochondrial fission, in apoptosis
    • Frank, S. et al. The role of dynamin-related protein 1, a mediator of mitochondrial fission, in apoptosis. Dev. Cell 1, 515-525 (2001
    • (2001) Dev. Cell , vol.1 , pp. 515-525
    • Frank, S.1
  • 33
    • 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. Nature Cell Biol. 13, 589-598 (2011
    • (2011) Nature Cell Biol. , vol.13 , pp. 589-598
    • Gomes, L.C.1    Di Benedetto, G.2    Scorrano, L.3
  • 34
    • 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. USA 108, 10190-10195 (2011
    • (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
  • 35
    • 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 106, 11960-11965 (2009
    • (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
  • 36
    • 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. 282, 11521-11529 (2007
    • (2007) J. Biol. Chem. , vol.282 , pp. 11521-11529
    • Taguchi, N.1    Ishihara, N.2    Jofuku, A.3    Oka, T.4    Mihara, K.5
  • 38
    • 4344583901 scopus 로고    scopus 로고
    • Role of mitochondrial permeability transition pores in mitochondrial autophagy
    • Rodriguez-Enriquez, S., He, L., & Lemasters, J. J. Role of mitochondrial permeability transition pores in mitochondrial autophagy. Int. J. Biochem. Cell Biol. 36, 2463-2472 (2004
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 2463-2472
    • Rodriguez-Enriquez, S.1    He, L.2    Lemasters, J.J.3
  • 39
    • 57749121573 scopus 로고    scopus 로고
    • Mitophagy in yeast occurs through a selective mechanism
    • Kanki, T., & Klionsky, D. J. Mitophagy in yeast occurs through a selective mechanism. J. Biol. Chem. 283, 32386-32393 (2008
    • (2008) J. Biol. Chem. , vol.283 , pp. 32386-32393
    • Kanki, T.1    Klionsky, D.J.2
  • 40
    • 84869397441 scopus 로고    scopus 로고
    • Human mitochondrial dna: Roles of inherited and somatic mutations
    • Schon, E. A., DiMauro, S., & Hirano, M. Human mitochondrial DNA: roles of inherited and somatic mutations. Nature Rev. Genet. 13, 878-890 (2012
    • (2012) Nature Rev. Genet. , vol.13 , pp. 878-890
    • Schon, E.A.1    Dimauro, S.2    Hirano, M.3
  • 41
    • 84865864065 scopus 로고    scopus 로고
    • The genetics and neuropathology of parkinson's disease
    • Houlden, H., & Singleton, A. B. The genetics and neuropathology of Parkinson's disease. Acta Neuropathol. 124, 325-338 (2012
    • (2012) Acta Neuropathol. , vol.124 , pp. 325-338
    • Houlden, H.1    Singleton, A.B.2
  • 42
    • 33745589773 scopus 로고    scopus 로고
    • Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
    • Clark, I. E. et al. Drosophila Pink1 is required for mitochondrial function and interacts genetically with parkin. Nature 441, 1162-1166 (2006
    • (2006) Nature , vol.441 , pp. 1162-1166
    • Clark, I.E.1
  • 43
    • 33745602748 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in drosophila pink1 mutants is complemented by parkin
    • Park, J. et al. Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by Parkin. Nature 441, 1157-1161 (2006
    • (2006) Nature , vol.441 , pp. 1157-1161
    • Park, J.1
  • 44
    • 33746080412 scopus 로고    scopus 로고
    • Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of drosophila pink1 is rescued by parkin
    • Yang, Y. et al. Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of Drosophila Pink1 is rescued by Parkin. Proc. Natl Acad. Sci. USA 103, 10793-10798 (2006
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 10793-10798
    • Yang, Y.1
  • 45
    • 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. 183, 795-803 (2008
    • (2008) J. Cell Biol. , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 46
    • 75749156257 scopus 로고    scopus 로고
    • Pink1 is selectively stabilized on impaired mitochondria to activate parkin
    • Narendra, D. P. et al. PINK1 is selectively stabilized on impaired mitochondria to activate parkin. PLoS Biol. 8, e1000298 (2010
    • (2010) PLoS Biol. , vol.8 , pp. e1000298
    • Narendra, D.P.1
  • 47
    • 79954520907 scopus 로고    scopus 로고
    • Broad activation of the ubiquitin-proteasome system by parkin is critical for mitophagy
    • Chan, N. C. et al. Broad activation of the ubiquitin-proteasome system by parkin is critical for mitophagy. Hum. Mol. Genet. 20, 1726-1737 (2011
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 1726-1737
    • Chan, N.C.1
  • 48
    • 84876296881 scopus 로고    scopus 로고
    • Landscape of the parkin-dependent ubiquitylome in response to mitochondrial depolarization
    • Sarraf, S. A. et al. Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization. Nature 496, 372-376 (2013
    • (2013) Nature , vol.496 , pp. 372-376
    • Sarraf, S.A.1
  • 49
    • 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. 286, 19630-19640 (2011
    • (2011) J. Biol. Chem. , vol.286 , pp. 19630-19640
    • Yoshii, S.R.1    Kishi, C.2    Ishihara, N.3    Mizushima, N.4
  • 50
    • 78650729600 scopus 로고    scopus 로고
    • Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by parkin
    • Tanaka, A. et al. Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by parkin. J. Cell Biol. 191, 1367-1380 (2010
    • (2010) J. Cell Biol. , vol.191 , pp. 1367-1380
    • Tanaka, A.1
  • 51
    • 79551663809 scopus 로고    scopus 로고
    • The aaa-Atpase p97 is essential for outer mitochondrial membrane protein turnover
    • Xu, S., Peng, G., Wang, Y., Fang, S., & Karbowski, M. The AAA-ATPase p97 is essential for outer mitochondrial membrane protein turnover. Mol. Biol. Cell 22, 291-300 (2011
    • (2011) Mol. Biol. Cell , vol.22 , pp. 291-300
    • Xu, S.1    Peng, G.2    Wang, Y.3    Fang, S.4    Karbowski, M.5
  • 52
    • 77955398958 scopus 로고    scopus 로고
    • Parkin overexpression selects against a deleterious mtdna mutation in heteroplasmic cybrid cells
    • Suen, D. F., Narendra, D. P., Tanaka, A., Manfredi, G., & Youle, R. J. Parkin overexpression selects against a deleterious mtDNA mutation in heteroplasmic cybrid cells. Proc. Natl Acad. Sci. USA 107, 11835-11840 (2010
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 11835-11840
    • Suen, D.F.1    Narendra, D.P.2    Tanaka, A.3    Manfredi, G.4    Youle, R.J.5
  • 53
    • 84876213313 scopus 로고    scopus 로고
    • The pink1-parkin pathway promotes both mitophagy and selective respiratory chain turnover in vivo
    • Vincow, E. S. et al. The PINK1-parkin pathway promotes both mitophagy and selective respiratory chain turnover in vivo. Proc. Natl Acad. Sci. USA 110, 6400-6405 (2013
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 6400-6405
    • Vincow, E.S.1
  • 54
    • 76249127368 scopus 로고    scopus 로고
    • Loss of autophagy in erythroid cells leads to defective removal of mitochondria and severe anemia in vivo
    • Mortensen, M. et al. Loss of autophagy in erythroid cells leads to defective removal of mitochondria and severe anemia in vivo. Proc. Natl Acad. Sci. USA 107, 832-837 (2010
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 832-837
    • Mortensen, M.1
  • 55
    • 28444455308 scopus 로고    scopus 로고
    • Organelle degradation during the lens and erythroid differentiation is independent of autophagy
    • Matsui, M., Yamamoto, A., Kuma, A., Ohsumi, Y., & Mizushima, N. Organelle degradation during the lens and erythroid differentiation is independent of autophagy. Biochem. Biophys. Res. Commun. 339, 485-489 (2006
    • (2006) Biochem. Biophys. Res. Commun. , vol.339 , pp. 485-489
    • Matsui, M.1    Yamamoto, A.2    Kuma, A.3    Ohsumi, Y.4    Mizushima, N.5
  • 56
    • 67650230871 scopus 로고    scopus 로고
    • Mitochondrial clearance is regulated by atg7-dependent and-independent mechanisms during reticulocyte maturation
    • Zhang, J. et al. Mitochondrial clearance is regulated by Atg7-dependent and-independent mechanisms during reticulocyte maturation. Blood 114, 157-164 (2009
    • (2009) Blood , vol.114 , pp. 157-164
    • Zhang, J.1
  • 57
    • 37649017266 scopus 로고    scopus 로고
    • Nix is required for programmed mitochondrial clearance during reticulocyte maturation
    • Schweers, R. L. et al. NIX is required for programmed mitochondrial clearance during reticulocyte maturation. Proc. Natl Acad. Sci. USA 104, 19500-19505 (2007
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 19500-19505
    • Schweers, R.L.1
  • 58
    • 47049100413 scopus 로고    scopus 로고
    • Essential role for nix in autophagic maturation of erythroid cells
    • Sandoval, H. et al. Essential role for Nix in autophagic maturation of erythroid cells. Nature 454, 232-235 (2008
    • (2008) Nature , vol.454 , pp. 232-235
    • Sandoval, H.1
  • 59
    • 74049153002 scopus 로고    scopus 로고
    • Nix is a selective autophagy receptor for mitochondrial clearance
    • Novak, I. et al. Nix is a selective autophagy receptor for mitochondrial clearance. EMBO Rep. 11, 45-51 (2010
    • (2010) EMBO Rep. , vol.11 , pp. 45-51
    • Novak, I.1
  • 60
    • 84862789618 scopus 로고    scopus 로고
    • Mitochondrial outer-membrane protein fundc1 mediates hypoxia-induced mitophagy in mammalian cells
    • Liu, L. et al. Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells. Nature Cell Biol. 14, 177-185 (2012
    • (2012) Nature Cell Biol. , vol.14 , pp. 177-185
    • Liu, L.1
  • 61
    • 84899912073 scopus 로고    scopus 로고
    • A regulatory signaling loop comprising the pgam5 phosphatase and ck2 controls receptor-mediated mitophagy
    • Chen, G. et al. A regulatory signaling loop comprising the PGAM5 phosphatase and CK2 controls receptor-mediated mitophagy. Mol. Cell 54, 362-377 (2014
    • (2014) Mol. Cell , vol.54 , pp. 362-377
    • Chen, G.1
  • 62
    • 67650246357 scopus 로고    scopus 로고
    • Mitochondria-Anchored receptor atg32 mediates degradation of mitochondria via selective autophagy
    • Okamoto, K., Kondo-Okamoto, N., & Ohsumi, Y. Mitochondria-Anchored receptor Atg32 mediates degradation of mitochondria via selective autophagy. Dev. Cell 17, 87-97 (2009
    • (2009) Dev. Cell , vol.17 , pp. 87-97
    • Okamoto, K.1    Kondo-Okamoto, N.2    Ohsumi, Y.3
  • 63
    • 67650264633 scopus 로고    scopus 로고
    • Atg32 is a mitochondrial protein that confers selectivity during mitophagy
    • Kanki, T., Wang, K., Cao, Y., Baba, M., & Klionsky, D. J. Atg32 is a mitochondrial protein that confers selectivity during mitophagy. Dev. Cell 17, 98-109 (2009
    • (2009) Dev. Cell , vol.17 , pp. 98-109
    • Kanki, T.1    Wang, K.2    Cao, Y.3    Baba, M.4    Klionsky, D.J.5
  • 64
    • 84880506979 scopus 로고    scopus 로고
    • The scaffold protein atg11 recruits fission machinery to drive selective mitochondria degradation by autophagy
    • Mao, K., Wang, K., Liu, X., & Klionsky, D. J. The scaffold protein Atg11 recruits fission machinery to drive selective mitochondria degradation by autophagy. Dev. Cell 26, 9-18 (2013
    • (2013) Dev. Cell , vol.26 , pp. 9-18
    • Mao, K.1    Wang, K.2    Liu, X.3    Klionsky, D.J.4
  • 65
    • 79953158981 scopus 로고    scopus 로고
    • Mitophagy in yeast is independent of mitochondrial fission and requires the stress response gene whi2
    • Mendl, N. et al. Mitophagy in yeast is independent of mitochondrial fission and requires the stress response gene WHI2. J. Cell Sci. 124, 1339-1350 (2011
    • (2011) J. Cell Sci. , vol.124 , pp. 1339-1350
    • Mendl, N.1
  • 66
    • 77950083955 scopus 로고    scopus 로고
    • Heteroplasmic mitochondrial dna mutations in normal and tumour cells
    • He, Y. et al. Heteroplasmic mitochondrial DNA mutations in normal and tumour cells. Nature 464, 610-614 (2010
    • (2010) Nature , vol.464 , pp. 610-614
    • He, Y.1
  • 67
    • 84871565767 scopus 로고    scopus 로고
    • Universal heteroplasmy of human mitochondrial dna
    • Payne, B. A. et al. Universal heteroplasmy of human mitochondrial DNA. Hum. Mol. Genet. 22, 384-390 (2013
    • (2013) Hum. Mol. Genet. , vol.22 , pp. 384-390
    • Payne, B.A.1
  • 68
    • 79551638162 scopus 로고    scopus 로고
    • Mitochondrial optic neuropathies-disease mechanisms and therapeutic strategies
    • Yu-Wai-Man, P., Griffiths, P. G., & Chinnery, P. F. Mitochondrial optic neuropathies-disease mechanisms and therapeutic strategies. Prog. Retin Eye Res. 30, 81-114 (2011
    • (2011) Prog. Retin Eye Res. , vol.30 , pp. 81-114
    • Yu-Wai-Man, P.1    Griffiths, P.G.2    Chinnery, P.F.3
  • 69
    • 65449154775 scopus 로고    scopus 로고
    • Retinal ganglion cell neurodegeneration in mitochondrial inherited disorders
    • Carelli, V. et al. Retinal ganglion cell neurodegeneration in mitochondrial inherited disorders. Biochim. Biophys. Acta 1787, 518-528 (2009
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 518-528
    • Carelli, V.1
  • 70
    • 0026608057 scopus 로고
    • Melas mutation in mtdna binding site for transcription termination factor causes defects in protein synthesis and in respiration but no change in levels of upstream and downstream mature transcripts
    • Chomyn, A. et al. MELAS mutation in mtDNA binding site for transcription termination factor causes defects in protein synthesis and in respiration but no change in levels of upstream and downstream mature transcripts. Proc. Natl Acad. Sci. USA 89, 4221-4225 (1992
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 4221-4225
    • Chomyn, A.1
  • 71
    • 0025836655 scopus 로고
    • Introduction of disease-related mitochondrial dna deletions into hela cells lacking mitochondrial dna results in mitochondrial dysfunction
    • Hayashi, J. et al. Introduction of disease-related mitochondrial DNA deletions into HeLa cells lacking mitochondrial DNA results in mitochondrial dysfunction. Proc. Natl Acad. Sci. USA 88, 10614-10618 (1991
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 10614-10618
    • Hayashi, J.1
  • 72
    • 0037444769 scopus 로고    scopus 로고
    • Mitochondrial threshold effects
    • Rossignol, R. et al. Mitochondrial threshold effects. Biochem. J. 370, 751-762 (2003
    • (2003) Biochem. J. , vol.370 , pp. 751-762
    • Rossignol, R.1
  • 73
    • 0034881326 scopus 로고    scopus 로고
    • Inter-mitochondrial complementation: Mitochondria-specific system preventing mice from expression of disease phenotypes by mutant mtdna
    • Nakada, K. et al. Inter-mitochondrial complementation: mitochondria-specific system preventing mice from expression of disease phenotypes by mutant mtDNA. Nature Med. 7, 934-940 (2001
    • (2001) Nature Med , vol.7 , pp. 934-940
    • Nakada, K.1
  • 74
    • 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. Nature Genet. 28, 272-275 (2001
    • (2001) Nature Genet. , vol.28 , pp. 272-275
    • Ono, T.1    Isobe, K.2    Nakada, K.3    Hayashi, J.I.4
  • 75
    • 0025944643 scopus 로고
    • Replacement of bovine mitochondrial dna by a sequence variant within one generation
    • Koehler, C. M. et al. Replacement of bovine mitochondrial DNA by a sequence variant within one generation. Genetics 129, 247-255 (1991
    • (1991) Genetics , vol.129 , pp. 247-255
    • Koehler, C.M.1
  • 76
    • 0029816795 scopus 로고    scopus 로고
    • Random genetic drift in the female germline explains the rapid segregation of mammalian mitochondrial dna
    • Jenuth, J. P., Peterson, A. C., Fu, K., & Shoubridge, E. A. Random genetic drift in the female germline explains the rapid segregation of mammalian mitochondrial DNA. Nature Genet. 14, 146-151 (1996
    • (1996) Nature Genet. , vol.14 , pp. 146-151
    • Jenuth, J.P.1    Peterson, A.C.2    Fu, K.3    Shoubridge, E.A.4
  • 77
    • 0030052504 scopus 로고    scopus 로고
    • Longitudinal study of a heteroplasmic 3460 leber hereditary optic neuropathy family by multiplexed primer-extension analysis and nucleotide sequencing
    • Ghosh, S. S., Fahy, E., Bodis-Wollner, I., Sherman, J., & Howell, N. Longitudinal study of a heteroplasmic 3460 Leber hereditary optic neuropathy family by multiplexed primer-extension analysis and nucleotide sequencing. Am. J. Hum. Genet. 58, 325-334 (1996
    • (1996) Am. J. Hum. Genet. , vol.58 , pp. 325-334
    • Ghosh, S.S.1    Fahy, E.2    Bodis-Wollner, I.3    Sherman, J.4    Howell, N.5
  • 78
    • 0026620865 scopus 로고
    • Segregation and manifestations of the mtdna trna(lys)a→g(8344) mutation of myoclonus epilepsy and ragged-red fibers (merrf) syndrome
    • Larsson, N. G. et al. Segregation and manifestations of the mtDNA tRNA(Lys) A→G(8344) mutation of myoclonus epilepsy and ragged-red fibers (MERRF) syndrome. Am. J. Hum. Genet. 51, 1201-1212 (1992
    • (1992) Am. J. Hum. Genet. , vol.51 , pp. 1201-1212
    • Larsson, N.G.1
  • 79
    • 38649091334 scopus 로고    scopus 로고
    • A reduction of mitochondrial dna molecules during embryogenesis explains the rapid segregation of genotypes
    • Cree, L. M. et al. A reduction of mitochondrial DNA molecules during embryogenesis explains the rapid segregation of genotypes. Nature Genet. 40, 249-254 (2008
    • (2008) Nature Genet. , vol.40 , pp. 249-254
    • Cree, L.M.1
  • 80
    • 74249105479 scopus 로고    scopus 로고
    • New evidence confirms that the mitochondrial bottleneck is generated without reduction of mitochondrial dna content in early primordial germ cells of mice
    • Cao, L. et al. New evidence confirms that the mitochondrial bottleneck is generated without reduction of mitochondrial DNA content in early primordial germ cells of mice. PLoS Genet. 5, e1000756 (2009
    • (2009) PLoS Genet. , vol.5 , pp. e1000756
    • Cao, L.1
  • 81
    • 56749180593 scopus 로고    scopus 로고
    • The mitochondrial dna genetic bottleneck results from replication of a subpopulation of genomes
    • Wai, T., Teoli, D., & Shoubridge, E. A. The mitochondrial DNA genetic bottleneck results from replication of a subpopulation of genomes. Nature Genet. 40, 1484-1488 (2008
    • (2008) Nature Genet. , vol.40 , pp. 1484-1488
    • Wai, T.1    Teoli, D.2    Shoubridge, E.A.3
  • 82
    • 0017758576 scopus 로고
    • Mouse l cell mitochondrial dna molecules are selected randomly for replication throughout the cell cycle
    • Bogenhagen, D., & Clayton, D. A. Mouse L cell mitochondrial DNA molecules are selected randomly for replication throughout the cell cycle. Cell 11, 719-727 (1977
    • (1977) Cell , vol.11 , pp. 719-727
    • Bogenhagen, D.1    Clayton, D.A.2
  • 83
    • 37249055914 scopus 로고    scopus 로고
    • Deletion-mutant mtdna increases in somatic tissues but decreases in female germ cells with age
    • Sato, A. et al. Deletion-mutant mtDNA increases in somatic tissues but decreases in female germ cells with age. Genetics 177, 2031-2037 (2007
    • (2007) Genetics , vol.177 , pp. 2031-2037
    • Sato, A.1
  • 84
    • 39349105943 scopus 로고    scopus 로고
    • A mouse model of mitochondrial disease reveals germline selection against severe mtdna mutations
    • Fan, W. et al. A mouse model of mitochondrial disease reveals germline selection against severe mtDNA mutations. Science 319, 958-962 (2008
    • (2008) Science , vol.319 , pp. 958-962
    • Fan, W.1
  • 85
    • 38949091096 scopus 로고    scopus 로고
    • Strong purifying selection in transmission of mammalian mitochondrial dna
    • References 84 and 85 provide evidence for the existence of a mechanism of purifying selection for mtDNA mutations in the mouse female germ line
    • Stewart, J. B. et al. Strong purifying selection in transmission of mammalian mitochondrial DNA. PLoS Biol. 6, e10 (2008). References 84 and 85 provide evidence for the existence of a mechanism of purifying selection for mtDNA mutations in the mouse female germ line.
    • (2008) Plos Biol , vol.6 , pp. e10
    • Stewart, J.B.1
  • 86
    • 49949119847 scopus 로고    scopus 로고
    • Purifying selection of mtdna and its implications for understanding evolution and mitochondrial disease
    • Stewart, J. B., Freyer, C., Elson, J. L., & Larsson, N. G. Purifying selection of mtDNA and its implications for understanding evolution and mitochondrial disease. Nature Rev. Genet. 9, 657-662 (2008
    • (2008) Nature Rev. Genet. , vol.9 , pp. 657-662
    • Stewart, J.B.1    Freyer, C.2    Elson, J.L.3    Larsson, N.G.4
  • 88
    • 0023518420 scopus 로고
    • Amounts of mitochondrial dna and abundance of some mitochondrial gene transcripts in early mouse embryos
    • Piko, L., & Taylor, K. D. Amounts of mitochondrial DNA and abundance of some mitochondrial gene transcripts in early mouse embryos. Dev. Biol. 123, 364-374 (1987
    • (1987) Dev. Biol. , vol.123 , pp. 364-374
    • Piko, L.1    Taylor, K.D.2
  • 89
    • 84861699019 scopus 로고    scopus 로고
    • Rapid mitochondrial dna segregation in primate preimplantation embryos precedes somatic and germline bottleneck
    • Lee, H. S. et al. Rapid mitochondrial DNA segregation in primate preimplantation embryos precedes somatic and germline bottleneck. Cell Rep. 1, 506-515 (2012
    • (2012) Cell Rep. , vol.1 , pp. 506-515
    • Lee, H.S.1
  • 90
    • 0030951244 scopus 로고    scopus 로고
    • Tissue-specific selection for different mtdna genotypes in heteroplasmic mice
    • Jenuth, J. P., Peterson, A. C., & Shoubridge, E. A. Tissue-specific selection for different mtDNA genotypes in heteroplasmic mice. Nature Genet. 16, 93-95 (1997
    • (1997) Nature Genet. , vol.16 , pp. 93-95
    • Jenuth, J.P.1    Peterson, A.C.2    Shoubridge, E.A.3
  • 91
    • 0035888637 scopus 로고    scopus 로고
    • Selection of a mtdna sequence variant in hepatocytes of heteroplasmic mice is not due to differences in respiratory chain function or efficiency of replication
    • Battersby, B. J., & Shoubridge, E. A. Selection of a mtDNA sequence variant in hepatocytes of heteroplasmic mice is not due to differences in respiratory chain function or efficiency of replication. Hum. Mol. Genet. 10, 2469-2479 (2001
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 2469-2479
    • Battersby, B.J.1    Shoubridge, E.A.2
  • 92
    • 84867522393 scopus 로고    scopus 로고
    • Heteroplasmy of mouse mtdna is genetically unstable and results in altered behavior and cognition
    • Sharpley, M. S. et al. Heteroplasmy of mouse mtDNA is genetically unstable and results in altered behavior and cognition. Cell 151, 333-343 (2012
    • (2012) Cell , vol.151 , pp. 333-343
    • Sharpley, M.S.1
  • 94
    • 0037158599 scopus 로고    scopus 로고
    • Paternal inheritance of mitochondrial dna
    • Schwartz, M., & Vissing, J. Paternal inheritance of mitochondrial DNA. N. Engl. J. Med. 347, 576-580 (2002
    • (2002) N. Engl. J. Med. , vol.347 , pp. 576-580
    • Schwartz, M.1    Vissing, J.2
  • 95
    • 84858200622 scopus 로고    scopus 로고
    • Barriers to male transmission of mitochondrial dna in sperm development
    • DeLuca, S. Z., & O'Farrell, P. H. Barriers to male transmission of mitochondrial DNA in sperm development. Dev. Cell 22, 660-668 (2012
    • (2012) Dev. Cell , vol.22 , pp. 660-668
    • Deluca, S.Z.1    O'Farrell, P.H.2
  • 96
    • 0021416818 scopus 로고
    • Maternal inheritance of the mouse mitochondrial genome is not mediated by a loss or gross alteration of the paternal mitochondrial dna or by methylation of the oocyte mitochondrial dna
    • Hecht, N. B., Liem, H., Kleene, K. C., Distel, R. J., & Ho, S. M. Maternal inheritance of the mouse mitochondrial genome is not mediated by a loss or gross alteration of the paternal mitochondrial DNA or by methylation of the oocyte mitochondrial DNA. Dev. Biol. 102, 452-461 (1984
    • (1984) Dev. Biol. , vol.102 , pp. 452-461
    • Hecht, N.B.1    Liem, H.2    Kleene, K.C.3    Distel, R.J.4    Ho, S.M.5
  • 97
    • 0033604547 scopus 로고    scopus 로고
    • Ubiquitin tag for sperm mitochondria
    • Sutovsky, P. et al. Ubiquitin tag for sperm mitochondria. Nature 402, 371-372 (1999
    • (1999) Nature , vol.402 , pp. 371-372
    • Sutovsky, P.1
  • 98
    • 82255183165 scopus 로고    scopus 로고
    • Postfertilization autophagy of sperm organelles prevents paternal mitochondrial dna transmission
    • Al Rawi, S. et al. Postfertilization autophagy of sperm organelles prevents paternal mitochondrial DNA transmission. Science 334, 1144-1147 (2011
    • (2011) Science , vol.334 , pp. 1144-1147
    • Al Rawi, S.1
  • 99
    • 82255192465 scopus 로고    scopus 로고
    • Degradation of paternal mitochondria by fertilization-triggered autophagy in c. Elegans embryos
    • Sato, M., & Sato, K. Degradation of paternal mitochondria by fertilization-triggered autophagy in C. elegans embryos. Science 334, 1141-1144 (2011
    • (2011) Science , vol.334 , pp. 1141-1144
    • Sato, M.1    Sato, K.2
  • 100
    • 82655187112 scopus 로고    scopus 로고
    • Elimination of paternal mitochondria through the lysosomal degradation pathway in c. Elegans
    • Zhou, Q., Li, H., & Xue, D. Elimination of paternal mitochondria through the lysosomal degradation pathway in C. elegans. Cell Res. 21, 1662-1669 (2011
    • (2011) Cell Res. , vol.21 , pp. 1662-1669
    • Zhou, Q.1    Li, H.2    Xue, D.3
  • 101
    • 84881410399 scopus 로고    scopus 로고
    • Unique insights into maternal mitochondrial inheritance in mice
    • Luo, S. M. et al. Unique insights into maternal mitochondrial inheritance in mice. Proc. Natl Acad. Sci. USA 110, 13038-13043 (2013
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 13038-13043
    • Luo, S.M.1
  • 102
    • 33749991592 scopus 로고    scopus 로고
    • Mitochondrial inner-membrane fusion and crista maintenance requires the dynamin-related gtpase mgm1
    • Meeusen, S. et al. Mitochondrial inner-membrane fusion and crista maintenance requires the dynamin-related GTPase Mgm1. Cell 127, 383-395 (2006
    • (2006) Cell , vol.127 , pp. 383-395
    • Meeusen, S.1
  • 103
    • 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 20, 3525-3532 (2009
    • (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.5
  • 104
    • 84874639591 scopus 로고    scopus 로고
    • Fis1 mff mid49, and mid51 mediate drp1 recruitment in mitochondrial fission
    • Loson, O. C., Song, Z., Chen, H., & Chan, D. C. Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission. Mol. Biol. Cell 24, 659-667 (2013
    • (2013) Mol. Biol. Cell , vol.24 , pp. 659-667
    • Loson, O.C.1    Song, Z.2    Chen, H.3    Chan, D.C.4
  • 105
    • 78650167618 scopus 로고    scopus 로고
    • Mff is an essential factor for mitochondrial recruitment of drp1 during mitochondrial fission in mammalian cells
    • Otera, H. et al. Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells. J. Cell Biol. 191, 1141-1158 (2010
    • (2010) J. Cell Biol. , vol.191 , pp. 1141-1158
    • Otera, H.1
  • 106
    • 84868556435 scopus 로고    scopus 로고
    • Mitochondrial network size scaling in budding yeast
    • Rafelski, S. M. et al. Mitochondrial network size scaling in budding yeast. Science 338, 822-824 (2012
    • (2012) Science , vol.338 , pp. 822-824
    • Rafelski, S.M.1
  • 107
    • 0025076787 scopus 로고
    • Temperature-sensitive yeast mutants defective in mitochondrial inheritance
    • McConnell, S. J., Stewart, L. C., Talin, A., & Yaffe, M. P. Temperature-sensitive yeast mutants defective in mitochondrial inheritance. J. Cell Biol. 111, 967-976 (1990
    • (1990) J. Cell Biol. , vol.111 , pp. 967-976
    • McConnell, S.J.1    Stewart, L.C.2    Talin, A.3    Yaffe, M.P.4
  • 108
    • 0036514271 scopus 로고    scopus 로고
    • Formins direct arp2/3-independent actin filament assembly to polarize cell growth in yeast
    • Evangelista, M., Pruyne, D., Amberg, D. C., Boone, C., & Bretscher, A. Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast. Nature Cell Biol. 4, 260-269 (2002
    • (2002) Nature Cell Biol. , vol.4 , pp. 260-269
    • Evangelista, M.1    Pruyne, D.2    Amberg, D.C.3    Boone, C.4    Bretscher, A.5
  • 109
  • 110
    • 0028048692 scopus 로고
    • Yeast mitochondria contain atp-sensitive, reversible actin-binding activity
    • Lazzarino, D. A., Boldogh, I., Smith, M. G., Rosand, J., & Pon, L. A. Yeast mitochondria contain ATP-sensitive, reversible actin-binding activity. Mol. Biol. Cell 5, 807-818 (1994
    • (1994) Mol. Biol. Cell , vol.5 , pp. 807-818
    • Lazzarino, D.A.1    Boldogh, I.2    Smith, M.G.3    Rosand, J.4    Pon, L.A.5
  • 111
    • 0027765526 scopus 로고
    • Actin structure and function: Roles in mitochondrial organization and morphogenesis in budding yeast and identification of the phalloidin-binding site
    • Drubin, D. G., Jones, H. D., & Wertman, K. F. Actin structure and function: roles in mitochondrial organization and morphogenesis in budding yeast and identification of the phalloidin-binding site. Mol. Biol. Cell 4, 1277-1294 (1993
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1277-1294
    • Drubin, D.G.1    Jones, H.D.2    Wertman, K.F.3
  • 112
    • 0035853076 scopus 로고    scopus 로고
    • Arp2/3 complex and actin dynamics are required for actin-based mitochondrial motility in yeast
    • Boldogh, I. R. et al. Arp2/3 complex and actin dynamics are required for actin-based mitochondrial motility in yeast. Proc. Natl Acad. Sci. USA 98, 3162-3167 (2001
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 3162-3167
    • Boldogh, I.R.1
  • 113
    • 4344703533 scopus 로고    scopus 로고
    • A type v myosin (myo2p) and a rab-like g-protein (ypt11p) are required for retention of newly inherited mitochondria in yeast cells during cell division
    • Boldogh, I. R., Ramcharan, S. L., Yang, H. C., & Pon, L. A. A type V myosin (Myo2p) and a Rab-like G-protein (Ypt11p) are required for retention of newly inherited mitochondria in yeast cells during cell division. Mol. Biol. Cell 15, 3994-4002 (2004
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3994-4002
    • Boldogh, I.R.1    Ramcharan, S.L.2    Yang, H.C.3    Pon, L.A.4
  • 115
    • 42049089309 scopus 로고    scopus 로고
    • The class v myosin motor protein, myo2, plays a major role in mitochondrial motility in saccharomyces cerevisiae
    • Altmann, K., Frank, M., Neumann, D., Jakobs, S., & Westermann, B. The class V myosin motor protein, Myo2, plays a major role in mitochondrial motility in Saccharomyces cerevisiae. J. Cell Biol. 181, 119-130 (2008
    • (2008) J. Cell Biol. , vol.181 , pp. 119-130
    • Altmann, K.1    Frank, M.2    Neumann, D.3    Jakobs, S.4    Westermann, B.5
  • 116
    • 84884590196 scopus 로고    scopus 로고
    • Active segregation of yeast mitochondria by myo2 is essential and mediated by mmr1 and ypt11
    • Chernyakov, I., Santiago-Tirado, F., & Bretscher, A. Active segregation of yeast mitochondria by Myo2 is essential and mediated by Mmr1 and Ypt11. Curr. Biol. 23, 1818-1824 (2013
    • (2013) Curr. Biol. , vol.23 , pp. 1818-1824
    • Chernyakov, I.1    Santiago-Tirado, F.2    Bretscher, A.3
  • 117
    • 80052577157 scopus 로고    scopus 로고
    • The myosin-related motor protein myo2 is an essential mediator of bud-directed mitochondrial movement in yeast
    • Fortsch, J., Hummel, E., Krist, M., & Westermann, B. The myosin-related motor protein Myo2 is an essential mediator of bud-directed mitochondrial movement in yeast. J. Cell Biol. 194, 473-488 (2011
    • (2011) J. Cell Biol. , vol.194 , pp. 473-488
    • Fortsch, J.1    Hummel, E.2    Krist, M.3    Westermann, B.4
  • 118
    • 0037451122 scopus 로고    scopus 로고
    • Identification of an organelle-specific myosin v receptor
    • Ishikawa, K. et al. Identification of an organelle-specific myosin V receptor. J. Cell Biol. 160, 887-897 (2003
    • (2003) J. Cell Biol. , vol.160 , pp. 887-897
    • Ishikawa, K.1
  • 119
    • 0037422115 scopus 로고    scopus 로고
    • Regulated degradation of a class v myosin receptor directs movement of the yeast vacuole
    • Tang, F. et al. Regulated degradation of a class V myosin receptor directs movement of the yeast vacuole. Nature 422, 87-92 (2003
    • (2003) Nature , vol.422 , pp. 87-92
    • Tang, F.1
  • 120
    • 0028902506 scopus 로고
    • The role of myo2, a yeast class v myosin, in vesicular transport
    • Govindan, B., Bowser, R., & Novick, P. The role of Myo2, a yeast class V myosin, in vesicular transport. J. Cell Biol. 128, 1055-1068 (1995
    • (1995) J. Cell Biol. , vol.128 , pp. 1055-1068
    • Govindan, B.1    Bowser, R.2    Novick, P.3
  • 121
    • 0032576569 scopus 로고    scopus 로고
    • Tropomyosin-containing actin cables direct the myo2p-dependent polarized delivery of secretory vesicles in budding yeast
    • Pruyne, D. W., Schott, D. H., & Bretscher, A. Tropomyosin-containing actin cables direct the Myo2p-dependent polarized delivery of secretory vesicles in budding yeast. J. Cell Biol. 143, 1931-1945 (1998
    • (1998) J. Cell Biol. , vol.143 , pp. 1931-1945
    • Pruyne, D.W.1    Schott, D.H.2    Bretscher, A.3
  • 122
    • 0035795423 scopus 로고    scopus 로고
    • A role for actin cdc1p and myo2p in the inheritance of late golgi elements in saccharomyces cerevisiae
    • Rossanese, O. W. et al. A role for actin, Cdc1p, and Myo2p in the inheritance of late Golgi elements in Saccharomyces cerevisiae. J. Cell Biol. 153, 47-62 (2001
    • (2001) J. Cell Biol. , vol.153 , pp. 47-62
    • Rossanese, O.W.1
  • 123
    • 0035842904 scopus 로고    scopus 로고
    • A role for vps1p, actin, and the myo2p motor in peroxisome abundance and inheritance in saccharomyces cerevisiae
    • Hoepfner, D., van den Berg, M., Philippsen, P., Tabak, H. F., & Hettema, E. H. A role for Vps1p, actin, and the Myo2p motor in peroxisome abundance and inheritance in Saccharomyces cerevisiae. J. Cell Biol. 155, 979-990 (2001
    • (2001) J. Cell Biol. , vol.155 , pp. 979-990
    • Hoepfner, D.1    Van Den Berg, M.2    Philippsen, P.3    Tabak, H.F.4    Hettema, E.H.5
  • 124
    • 3342969453 scopus 로고    scopus 로고
    • Mmr1p is a mitochondrial factor for myo2p-dependent inheritance of mitochondria in the budding yeast
    • Itoh, T., Toh, E. A., & Matsui, Y. Mmr1p is a mitochondrial factor for Myo2p-dependent inheritance of mitochondria in the budding yeast. EMBO J. 23, 2520-2530 (2004
    • (2004) EMBO J. , vol.23 , pp. 2520-2530
    • Itoh, T.1    Toh, E.A.2    Matsui, Y.3
  • 125
    • 0036839610 scopus 로고    scopus 로고
    • Complex formation with ypt11p, a rab-type small gtpase, is essential to facilitate the function of myo2p, a class v myosin, in mitochondrial distribution in saccharomyces cerevisiae
    • Itoh, T., Watabe, A., Toh, E. A., & Matsui, Y. Complex formation with Ypt11p, a rab-type small GTPase, is essential to facilitate the function of Myo2p, a class V myosin, in mitochondrial distribution in Saccharomyces cerevisiae. Mol. Cell. Biol. 22, 7744-7757 (2002
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7744-7757
    • Itoh, T.1    Watabe, A.2    Toh, E.A.3    Matsui, Y.4
  • 126
    • 0034735917 scopus 로고    scopus 로고
    • Myosin vi is required for asymmetric segregation of cellular components during c. Elegans spermatogenesis
    • Kelleher, J. F. et al. Myosin VI is required for asymmetric segregation of cellular components during C. elegans spermatogenesis. Curr. Biol. 10, 1489-1496 (2000
    • (2000) Curr. Biol. , vol.10 , pp. 1489-1496
    • Kelleher, J.F.1
  • 127
    • 84880657411 scopus 로고    scopus 로고
    • The yeast cell cortical protein num1 integrates mitochondrial dynamics into cellular architecture
    • Klecker, T., Scholz, D., Fortsch, J., & Westermann, B. The yeast cell cortical protein Num1 integrates mitochondrial dynamics into cellular architecture. J. Cell Sci. 126, 2924-2930 (2013
    • (2013) J. Cell Sci. , vol.126 , pp. 2924-2930
    • Klecker, T.1    Scholz, D.2    Fortsch, J.3    Westermann, B.4
  • 128
    • 84873460115 scopus 로고    scopus 로고
    • Endoplasmic reticulum-Associated mitochondria-cortex tether functions in the distribution and inheritance of mitochondria
    • Lackner, L. L., Ping, H., Graef, M., Murley, A., & Nunnari, J. Endoplasmic reticulum-Associated mitochondria-cortex tether functions in the distribution and inheritance of mitochondria. Proc. Natl Acad. Sci. USA 110, E458-E467 (2013
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. E458-E467
    • Lackner, L.L.1    Ping, H.2    Graef, M.3    Murley, A.4    Nunnari, J.5
  • 129
    • 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 456, 605-610 (2008
    • (2008) Nature , vol.456 , pp. 605-610
    • De Brito, O.M.1    Scorrano, L.2
  • 130
    • 0027340729 scopus 로고
    • Microdomains with high ca2+ close to ip3-sensitive channels that are sensed by neighboring mitochondria
    • Rizzuto, R., Brini, M., Murgia, M., & Pozzan, T. Microdomains with high Ca2+ close to IP3-sensitive channels that are sensed by neighboring mitochondria. Science 262, 744-747 (1993
    • (1993) Science , vol.262 , pp. 744-747
    • Rizzuto, R.1    Brini, M.2    Murgia, M.3    Pozzan, T.4
  • 131
    • 0033199506 scopus 로고    scopus 로고
    • Association between the endoplasmic reticulum and mitochondria of yeast facilitates interorganelle transport of phospholipids through membrane contact
    • Achleitner, G. et al. Association between the endoplasmic reticulum and mitochondria of yeast facilitates interorganelle transport of phospholipids through membrane contact. Eur. J. Biochem. 264, 545-553 (1999
    • (1999) Eur. J. Biochem. , vol.264 , pp. 545-553
    • Achleitner, G.1
  • 132
    • 0027973135 scopus 로고
    • A unique mitochondria-Associated membrane fraction from rat liver has a high capacity for lipid synthesis and contains pre-golgi secretory proteins including nascent lipoproteins
    • Rusinol, A. E., Cui, Z., Chen, M. H., & Vance, J. E. A unique mitochondria-Associated membrane fraction from rat liver has a high capacity for lipid synthesis and contains pre-Golgi secretory proteins including nascent lipoproteins. J. Biol. Chem. 269, 27494-27502 (1994
    • (1994) J. Biol. Chem. , vol.269 , pp. 27494-27502
    • Rusinol, A.E.1    Cui, Z.2    Chen, M.H.3    Vance, J.E.4
  • 133
    • 80054844842 scopus 로고    scopus 로고
    • Er tubules mark sites of mitochondrial division
    • Shows that ER tubules are involved in the constriction of mitochondria at fission sites
    • Friedman, J. R. et al. ER tubules mark sites of mitochondrial division. Science 334, 358-362 (2011). Shows that ER tubules are involved in the constriction of mitochondria at fission sites.
    • (2011) Science , vol.334 , pp. 358-362
    • Friedman, J.R.1
  • 134
    • 84872769447 scopus 로고    scopus 로고
    • An actin-dependent step in mitochondrial fission mediated by the er-Associated formin inf2
    • Korobova, F., Ramabhadran, V., & Higgs, H. N. An actin-dependent step in mitochondrial fission mediated by the ER-Associated formin INF2. Science 339, 464-467 (2013
    • (2013) Science , vol.339 , pp. 464-467
    • Korobova, F.1    Ramabhadran, V.2    Higgs, H.N.3
  • 135
    • 67749122635 scopus 로고    scopus 로고
    • An er-mitochondria tethering complex revealed by a synthetic biology screen
    • Kornmann, B. et al. An ER-mitochondria tethering complex revealed by a synthetic biology screen. Science 325, 477-481 (2009
    • (2009) Science , vol.325 , pp. 477-481
    • Kornmann, B.1
  • 136
    • 84879059164 scopus 로고    scopus 로고
    • Er-Associated mitochondrial division links the distribution of mitochondria and mitochondrial dna in yeast
    • Murley, A. et al. ER-Associated mitochondrial division links the distribution of mitochondria and mitochondrial DNA in yeast. Elife 2, e00422 (2013
    • (2013) Elife , vol.2 , pp. e00422
    • Murley, A.1
  • 137
    • 0031059722 scopus 로고    scopus 로고
    • Mdm12p a component required for mitochondrial inheritance that is conserved between budding and fission yeast
    • Berger, K. H., Sogo, L. F., & Yaffe, M. P. Mdm12p, a component required for mitochondrial inheritance that is conserved between budding and fission yeast. J. Cell Biol. 136, 545-553 (1997
    • (1997) J. Cell Biol. , vol.136 , pp. 545-553
    • Berger, K.H.1    Sogo, L.F.2    Yaffe, M.P.3
  • 138
    • 0028024592 scopus 로고
    • Regulation of mitochondrial morphology and inheritance by mdm10p, a protein of the mitochondrial outer membrane
    • Sogo, L. F., & Yaffe, M. P. Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane. J. Cell Biol. 126, 1361-1373 (1994).
    • (1994) J. Cell Biol. , vol.126 , pp. 1361-1373
    • Sogo, L.F.1    Yaffe, M.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.