메뉴 건너뛰기




Volumn 28, Issue 4, 2018, Pages R170-R185

Mitophagy and Quality Control Mechanisms in Mitochondrial Maintenance

Author keywords

[No Author keywords available]

Indexed keywords

PROTEASOME; UBIQUITIN;

EID: 85042076557     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2018.01.004     Document Type: Review
Times cited : (1373)

References (170)
  • 1
    • 0014070709 scopus 로고
    • On the origin of mitosing cells
    • Sagan, L., On the origin of mitosing cells. J. Theor. Biol. 14 (1967), 255–274.
    • (1967) J. Theor. Biol. , vol.14 , pp. 255-274
    • Sagan, L.1
  • 2
    • 85017230204 scopus 로고    scopus 로고
    • Prion-like polymerization in immunity and inflammation
    • a023580
    • Cai, X., Xu, H., Chen, Z.J., Prion-like polymerization in immunity and inflammation. Cold Spring Harb. Persp. Biol., 9, 2017 a023580.
    • (2017) Cold Spring Harb. Persp. Biol. , vol.9
    • Cai, X.1    Xu, H.2    Chen, Z.J.3
  • 3
    • 73349091842 scopus 로고    scopus 로고
    • The role of mitochondria in apoptosis
    • Wang, C., Youle, R.J., The role of mitochondria in apoptosis. Annu. Rev. Genet. 43 (2009), 95–118.
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 95-118
    • Wang, C.1    Youle, R.J.2
  • 4
    • 16844366524 scopus 로고    scopus 로고
    • Selective mitochondrial autophagy, or mitophagy, as a targeted defense against oxidative stress, mitochondrial dysfunction, and aging
    • Lemasters, J.J., Selective mitochondrial autophagy, or mitophagy, as a targeted defense against oxidative stress, mitochondrial dysfunction, and aging. Rejuven. Res. 8 (2005), 3–5.
    • (2005) Rejuven. Res. , vol.8 , pp. 3-5
    • Lemasters, J.J.1
  • 5
    • 85021656064 scopus 로고    scopus 로고
    • Proteasomal and autophagic degradation systems
    • Dikic, I., Proteasomal and autophagic degradation systems. Annu. Rev. Biochem 86 (2017), 193–224.
    • (2017) Annu. Rev. Biochem , vol.86 , pp. 193-224
    • Dikic, I.1
  • 7
    • 0017718492 scopus 로고
    • The effects of hibernation on cone visual cells in the ground squirrel. Invest. Ophthalmol
    • Reme, C.E., Young, R.W., The effects of hibernation on cone visual cells in the ground squirrel. Invest. Ophthalmol. Vis. Sci. 16 (1977), 815–840.
    • (1977) Vis. Sci. , vol.16 , pp. 815-840
    • Reme, C.E.1    Young, R.W.2
  • 9
    • 0038156122 scopus 로고    scopus 로고
    • The proapoptotic factor Nix is coexpressed with Bcl-xL during terminal erythroid differentiation
    • Aerbajinai, W., Giattina, M., Lee, Y.T., Raffeld, M., Miller, J.L., The proapoptotic factor Nix is coexpressed with Bcl-xL during terminal erythroid differentiation. Blood 102 (2003), 712–717.
    • (2003) Blood , vol.102 , pp. 712-717
    • Aerbajinai, W.1    Giattina, M.2    Lee, Y.T.3    Raffeld, M.4    Miller, J.L.5
  • 15
    • 84866543686 scopus 로고    scopus 로고
    • A short linear motif in BNIP3L (NIX) mediates mitochondrial clearance in reticulocytes
    • Zhang, J., Loyd, M.R., Randall, M.S., Waddell, M.B., Kriwacki, R.W., Ney, P.A., A short linear motif in BNIP3L (NIX) mediates mitochondrial clearance in reticulocytes. Autophagy 8 (2012), 1325–1332.
    • (2012) Autophagy , vol.8 , pp. 1325-1332
    • Zhang, J.1    Loyd, M.R.2    Randall, M.S.3    Waddell, M.B.4    Kriwacki, R.W.5    Ney, P.A.6
  • 16
    • 84902007678 scopus 로고    scopus 로고
    • Ulk1-mediated Atg5-independent macroautophagy mediates elimination of mitochondria from embryonic reticulocytes
    • Honda, S., Arakawa, S., Nishida, Y., Yamaguchi, H., Ishii, E., Shimizu, S., Ulk1-mediated Atg5-independent macroautophagy mediates elimination of mitochondria from embryonic reticulocytes. Nat. Commun, 5, 2014, 4004.
    • (2014) Nat. Commun , vol.5 , pp. 4004
    • Honda, S.1    Arakawa, S.2    Nishida, Y.3    Yamaguchi, H.4    Ishii, E.5    Shimizu, S.6
  • 17
    • 70349634803 scopus 로고    scopus 로고
    • Autophagy-dependent and -independent mechanisms of mitochondrial clearance during reticulocyte maturation
    • Zhang, J., Ney, P.A., Autophagy-dependent and -independent mechanisms of mitochondrial clearance during reticulocyte maturation. Autophagy 5 (2009), 1064–1065.
    • (2009) Autophagy , vol.5 , pp. 1064-1065
    • Zhang, J.1    Ney, P.A.2
  • 18
    • 51649124519 scopus 로고    scopus 로고
    • Ulk1 plays a critical role in the autophagic clearance of mitochondria and ribosomes during reticulocyte maturation
    • Kundu, M., Lindsten, T., Yang, C.Y., Wu, J., Zhao, F., Zhang, J., Selak, M.A., Ney, P.A., Thompson, C.B., Ulk1 plays a critical role in the autophagic clearance of mitochondria and ribosomes during reticulocyte maturation. Blood 112 (2008), 1493–1502.
    • (2008) Blood , vol.112 , pp. 1493-1502
    • Kundu, M.1    Lindsten, T.2    Yang, C.Y.3    Wu, J.4    Zhao, F.5    Zhang, J.6    Selak, M.A.7    Ney, P.A.8    Thompson, C.B.9
  • 20
    • 0031929515 scopus 로고    scopus 로고
    • Isolation, mapping, and functional analysis of a novel human cDNA (BNIP3L) encoding a protein homologous to human NIP3. Genes Chrom
    • Matsushima, M., Fujiwara, T., Takahashi, E., Minaguchi, T., Eguchi, Y., Tsujimoto, Y., Suzumori, K., Nakamura, Y., Isolation, mapping, and functional analysis of a novel human cDNA (BNIP3L) encoding a protein homologous to human NIP3. Genes Chrom. Cancer 21 (1998), 230–235.
    • (1998) Cancer , vol.21 , pp. 230-235
    • Matsushima, M.1    Fujiwara, T.2    Takahashi, E.3    Minaguchi, T.4    Eguchi, Y.5    Tsujimoto, Y.6    Suzumori, K.7    Nakamura, Y.8
  • 23
    • 0035884701 scopus 로고    scopus 로고
    • HIF-1-dependent regulation of hypoxic induction of the cell death factors BNIP3 and NIX in human tumors
    • Sowter, H.M., Ratcliffe, P.J., Watson, P., Greenberg, A.H., Harris, A.L., HIF-1-dependent regulation of hypoxic induction of the cell death factors BNIP3 and NIX in human tumors. Cancer Res. 61 (2001), 6669–6673.
    • (2001) Cancer Res. , vol.61 , pp. 6669-6673
    • Sowter, H.M.1    Ratcliffe, P.J.2    Watson, P.3    Greenberg, A.H.4    Harris, A.L.5
  • 24
    • 0034255036 scopus 로고    scopus 로고
    • Expression of the gene encoding the proapoptotic Nip3 protein is induced by hypoxia
    • Bruick, R.K., Expression of the gene encoding the proapoptotic Nip3 protein is induced by hypoxia. Proc. Natl. Acad. Sci. USA 97 (2000), 9082–9087.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9082-9087
    • Bruick, R.K.1
  • 26
    • 84861733247 scopus 로고    scopus 로고
    • Microtubule-associated protein 1 light chain 3 (LC3) interacts with Bnip3 protein to selectively remove endoplasmic reticulum and mitochondria via autophagy
    • Hanna, R.A., Quinsay, M.N., Orogo, A.M., Giang, K., Rikka, S., Gustafsson, A.B., Microtubule-associated protein 1 light chain 3 (LC3) interacts with Bnip3 protein to selectively remove endoplasmic reticulum and mitochondria via autophagy. J. Biol. Chem. 287 (2012), 19094–19104.
    • (2012) J. Biol. Chem. , vol.287 , pp. 19094-19104
    • Hanna, R.A.1    Quinsay, M.N.2    Orogo, A.M.3    Giang, K.4    Rikka, S.5    Gustafsson, A.B.6
  • 27
    • 27944470616 scopus 로고    scopus 로고
    • Phylogenomics of life-or-death switches in multicellular animals: Bcl-2, BH3-Only, and BNip families of apoptotic regulators
    • Aouacheria, A., Brunet, F., Gouy, M., Phylogenomics of life-or-death switches in multicellular animals: Bcl-2, BH3-Only, and BNip families of apoptotic regulators. Mol. Biol. Evol. 22 (2005), 2395–2416.
    • (2005) Mol. Biol. Evol. , vol.22 , pp. 2395-2416
    • Aouacheria, A.1    Brunet, F.2    Gouy, M.3
  • 28
    • 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 (2008), 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
  • 29
    • 84940956493 scopus 로고    scopus 로고
    • Parkinson's disease
    • Kalia, L.V., Lang, A.E., Parkinson's disease. Lancet 386 (2015), 896–912.
    • (2015) Lancet , vol.386 , pp. 896-912
    • Kalia, L.V.1    Lang, A.E.2
  • 32
    • 33646351299 scopus 로고    scopus 로고
    • Mitochondrial DNA deletions are abundant and cause functional impairment in aged human substantia nigra neurons
    • Kraytsberg, Y., Kudryavtseva, E., McKee, A.C., Geula, C., Kowall, N.W., Khrapko, K., Mitochondrial DNA deletions are abundant and cause functional impairment in aged human substantia nigra neurons. Nature Genet. 38 (2006), 518–520.
    • (2006) Nature Genet. , vol.38 , pp. 518-520
    • Kraytsberg, Y.1    Kudryavtseva, E.2    McKee, A.C.3    Geula, C.4    Kowall, N.W.5    Khrapko, K.6
  • 33
    • 33745589773 scopus 로고    scopus 로고
    • Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
    • Clark, I.E., Dodson, M.W., Jiang, C., Cao, J.H., Huh, J.R., Seol, J.H., Yoo, S.J., Hay, B.A., Guo, M., Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin. Nature 441 (2006), 1162–1166.
    • (2006) Nature , vol.441 , pp. 1162-1166
    • Clark, I.E.1    Dodson, M.W.2    Jiang, C.3    Cao, J.H.4    Huh, J.R.5    Seol, J.H.6    Yoo, S.J.7    Hay, B.A.8    Guo, M.9
  • 35
    • 33745602748 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
    • Park, J., Lee, S.B., Lee, S., Kim, Y., Song, S., Kim, S., Bae, E., Kim, J., Shong, M., Kim, J.M., et al. Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin. Nature 441 (2006), 1157–1161.
    • (2006) Nature , vol.441 , pp. 1157-1161
    • Park, J.1    Lee, S.B.2    Lee, S.3    Kim, Y.4    Song, S.5    Kim, S.6    Bae, E.7    Kim, J.8    Shong, M.9    Kim, J.M.10
  • 36
    • 78649685455 scopus 로고    scopus 로고
    • Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL. J
    • Jin, S.M., Lazarou, M., Wang, C., Kane, L.A., Narendra, D.P., Youle, R.J., Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL. J. Cell Biol. 191 (2010), 933–942.
    • (2010) Cell Biol. , vol.191 , pp. 933-942
    • Jin, S.M.1    Lazarou, M.2    Wang, C.3    Kane, L.A.4    Narendra, D.P.5    Youle, R.J.6
  • 38
    • 79955667485 scopus 로고    scopus 로고
    • The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking
    • Meissner, C., Lorenz, H., Weihofen, A., Selkoe, D.J., Lemberg, M.K., The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking. J. Neurochem 117 (2011), 856–867.
    • (2011) J. Neurochem , vol.117 , pp. 856-867
    • Meissner, C.1    Lorenz, H.2    Weihofen, A.3    Selkoe, D.J.4    Lemberg, M.K.5
  • 39
    • 84887453820 scopus 로고    scopus 로고
    • PINK1 is degraded through the N-end rule pathway
    • Yamano, K., Youle, R.J., PINK1 is degraded through the N-end rule pathway. Autophagy 9 (2013), 1758–1769.
    • (2013) Autophagy , vol.9 , pp. 1758-1769
    • Yamano, K.1    Youle, R.J.2
  • 40
    • 84857032953 scopus 로고    scopus 로고
    • Role of PINK1 binding to the TOM complex and alternate intracellular membranes in recruitment and activation of the E3 ligase Parkin
    • Lazarou, M., Jin, S.M., Kane, L.A., Youle, R.J., Role of PINK1 binding to the TOM complex and alternate intracellular membranes in recruitment and activation of the E3 ligase Parkin. Dev. Cell 22 (2012), 320–333.
    • (2012) Dev. Cell , vol.22 , pp. 320-333
    • Lazarou, M.1    Jin, S.M.2    Kane, L.A.3    Youle, R.J.4
  • 41
    • 84890957474 scopus 로고    scopus 로고
    • A dimeric PINK1-containing complex on depolarized mitochondria stimulates Parkin recruitment
    • Okatsu, K., Uno, M., Koyano, F., Go, E., Kimura, M., Oka, T., Tanaka, K., Matsuda, N., A dimeric PINK1-containing complex on depolarized mitochondria stimulates Parkin recruitment. J. Biol. Chem. 288 (2013), 36372–36384.
    • (2013) J. Biol. Chem. , vol.288 , pp. 36372-36384
    • Okatsu, K.1    Uno, M.2    Koyano, F.3    Go, E.4    Kimura, M.5    Oka, T.6    Tanaka, K.7    Matsuda, N.8
  • 44
    • 84871891737 scopus 로고    scopus 로고
    • PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of Parkin and regulates mitophagy
    • Shiba-Fukushima, K., Imai, Y., Yoshida, S., Ishihama, Y., Kanao, T., Sato, S., Hattori, N., PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of Parkin and regulates mitophagy. Sci. Rep, 2, 2012, 1002.
    • (2012) Sci. Rep , vol.2 , pp. 1002
    • Shiba-Fukushima, K.1    Imai, Y.2    Yoshida, S.3    Ishihama, Y.4    Kanao, T.5    Sato, S.6    Hattori, N.7
  • 48
    • 84881477223 scopus 로고    scopus 로고
    • Structure of the human Parkin ligase domain in an autoinhibited state
    • Wauer, T., Komander, D., Structure of the human Parkin ligase domain in an autoinhibited state. EMBO J 32 (2013), 2099–2112.
    • (2013) EMBO J , vol.32 , pp. 2099-2112
    • Wauer, T.1    Komander, D.2
  • 57
    • 84939795423 scopus 로고    scopus 로고
    • Mechanism of phospho-ubiquitin-induced PARKIN activation
    • Wauer, T., Simicek, M., Schubert, A., Komander, D., Mechanism of phospho-ubiquitin-induced PARKIN activation. Nature 524 (2015), 370–374.
    • (2015) Nature , vol.524 , pp. 370-374
    • Wauer, T.1    Simicek, M.2    Schubert, A.3    Komander, D.4
  • 58
    • 84901815187 scopus 로고    scopus 로고
    • Cargo recognition and trafficking in selective autophagy
    • Stolz, A., Ernst, A., Dikic, I., Cargo recognition and trafficking in selective autophagy. Nat. Cell Biol. 16 (2014), 495–501.
    • (2014) Nat. Cell Biol. , vol.16 , pp. 495-501
    • Stolz, A.1    Ernst, A.2    Dikic, I.3
  • 60
    • 78649300971 scopus 로고    scopus 로고
    • p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both
    • Narendra, D., Kane, L.A., Hauser, D.N., Fearnley, I.M., Youle, R.J., p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both. Autophagy 6 (2010), 1090–1106.
    • (2010) Autophagy , vol.6 , pp. 1090-1106
    • Narendra, D.1    Kane, L.A.2    Hauser, D.N.3    Fearnley, I.M.4    Youle, R.J.5
  • 62
    • 84951930787 scopus 로고    scopus 로고
    • The PINK1-PARKIN mitochondrial ubiquitylation pathway drives a program of OPTN/NDP52 recruitment and TBK1 activation to promote mitophagy
    • Heo, J.M., Ordureau, A., Paulo, J.A., Rinehart, J., Harper, J.W., The PINK1-PARKIN mitochondrial ubiquitylation pathway drives a program of OPTN/NDP52 recruitment and TBK1 activation to promote mitophagy. Mol. Cell 60 (2015), 7–20.
    • (2015) Mol. Cell , vol.60 , pp. 7-20
    • Heo, J.M.1    Ordureau, A.2    Paulo, J.A.3    Rinehart, J.4    Harper, J.W.5
  • 63
    • 84908065760 scopus 로고    scopus 로고
    • Optineurin is an autophagy receptor for damaged mitochondria in parkin-mediated mitophagy that is disrupted by an ALS-linked mutation
    • Wong, Y.C., Holzbaur, E.L., Optineurin is an autophagy receptor for damaged mitochondria in parkin-mediated mitophagy that is disrupted by an ALS-linked mutation. Proc. Natl. Acad. Sci. USA 111 (2014), E4439–4448.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. E4439-4448
    • Wong, Y.C.1    Holzbaur, E.L.2
  • 64
    • 84974815636 scopus 로고    scopus 로고
    • Dynamic recruitment and activation of ALS-associated TBK1 with its target optineurin are required for efficient mitophagy
    • Moore, A.S., Holzbaur, E.L., Dynamic recruitment and activation of ALS-associated TBK1 with its target optineurin are required for efficient mitophagy. Proc. Natl. Acad. Sci. USA 113 (2016), E3349–3358.
    • (2016) Proc. Natl. Acad. Sci. USA , vol.113 , pp. E3349-3358
    • Moore, A.S.1    Holzbaur, E.L.2
  • 67
    • 84940753095 scopus 로고    scopus 로고
    • TBK1 controls autophagosomal engulfment of polyubiquitinated mitochondria through p62/SQSTM1 phosphorylation
    • Matsumoto, G., Shimogori, T., Hattori, N., Nukina, N., TBK1 controls autophagosomal engulfment of polyubiquitinated mitochondria through p62/SQSTM1 phosphorylation. Hum. Mol. Genet. 24 (2015), 4429–4442.
    • (2015) Hum. Mol. Genet. , vol.24 , pp. 4429-4442
    • Matsumoto, G.1    Shimogori, T.2    Hattori, N.3    Nukina, N.4
  • 68
    • 85009198548 scopus 로고    scopus 로고
    • Atg8 family LC3/GABARAP proteins are crucial for autophagosome-lysosome fusion but not autophagosome formation during PINK1/Parkin mitophagy and starvation
    • Nguyen, T.N., Padman, B.S., Usher, J., Oorschot, V., Ramm, G., Lazarou, M., Atg8 family LC3/GABARAP proteins are crucial for autophagosome-lysosome fusion but not autophagosome formation during PINK1/Parkin mitophagy and starvation. J. Cell Biol. 215 (2016), 857–874.
    • (2016) J. Cell Biol. , vol.215 , pp. 857-874
    • Nguyen, T.N.1    Padman, B.S.2    Usher, J.3    Oorschot, V.4    Ramm, G.5    Lazarou, M.6
  • 69
  • 70
    • 85009178435 scopus 로고    scopus 로고
    • Prohibitin 2 is an inner mitochondrial membrane mitophagy receptor
    • Wei, Y., Chiang, W.C., Sumpter, R. Jr., Mishra, P., Levine, B., Prohibitin 2 is an inner mitochondrial membrane mitophagy receptor. Cell 168 (2017), 224–238.e210.
    • (2017) Cell , vol.168 , pp. 224-238.e210
    • Wei, Y.1    Chiang, W.C.2    Sumpter, R.3    Mishra, P.4    Levine, B.5
  • 71
    • 84946556916 scopus 로고    scopus 로고
    • Atypical mitochondrial inheritance patterns in eukaryotes
    • Breton, S., Stewart, D.T., Atypical mitochondrial inheritance patterns in eukaryotes. Genome 58 (2015), 423–431.
    • (2015) Genome , vol.58 , pp. 423-431
    • Breton, S.1    Stewart, D.T.2
  • 74
    • 84892619949 scopus 로고    scopus 로고
    • Dynamics of mitochondrial inheritance in the evolution of binary mating types and two sexes
    • Hadjivasiliou, Z., Lane, N., Seymour, R.M., Pomiankowski, A., Dynamics of mitochondrial inheritance in the evolution of binary mating types and two sexes. Proc. Biol. Sci., 280, 2013, 20131920.
    • (2013) Proc. Biol. Sci. , vol.280 , pp. 20131920
    • Hadjivasiliou, Z.1    Lane, N.2    Seymour, R.M.3    Pomiankowski, A.4
  • 75
    • 0033883489 scopus 로고    scopus 로고
    • Ubiquitinated sperm mitochondria, selective proteolysis, and the regulation of mitochondrial inheritance in mammalian embryos
    • Sutovsky, P., Moreno, R.D., Ramalho-Santos, J., Dominko, T., Simerly, C., Schatten, G., Ubiquitinated sperm mitochondria, selective proteolysis, and the regulation of mitochondrial inheritance in mammalian embryos. Biol. Reprod 63 (2000), 582–590.
    • (2000) Biol. Reprod , vol.63 , pp. 582-590
    • Sutovsky, P.1    Moreno, R.D.2    Ramalho-Santos, J.3    Dominko, T.4    Simerly, C.5    Schatten, G.6
  • 77
    • 84985916502 scopus 로고    scopus 로고
    • Autophagy and ubiquitin-proteasome system contribute to sperm mitophagy after mammalian fertilization
    • Song, W.H., Yi, Y.J., Sutovsky, M., Meyers, S., Sutovsky, P., Autophagy and ubiquitin-proteasome system contribute to sperm mitophagy after mammalian fertilization. Proc. Natl. Acad. Sci. USA 113 (2016), E5261–E5270.
    • (2016) Proc. Natl. Acad. Sci. USA , vol.113 , pp. E5261-E5270
    • Song, W.H.1    Yi, Y.J.2    Sutovsky, M.3    Meyers, S.4    Sutovsky, P.5
  • 79
    • 78650729600 scopus 로고    scopus 로고
    • Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin. J
    • Tanaka, A., Cleland, M.M., Xu, S., Narendra, D.P., Suen, D.F., Karbowski, M., Youle, R.J., Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin. J. Cell Biol. 191 (2010), 1367–1380.
    • (2010) Cell Biol. , vol.191 , pp. 1367-1380
    • Tanaka, A.1    Cleland, M.M.2    Xu, S.3    Narendra, D.P.4    Suen, D.F.5    Karbowski, M.6    Youle, R.J.7
  • 80
    • 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 (2011), 291–300.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 291-300
    • Xu, S.1    Peng, G.2    Wang, Y.3    Fang, S.4    Karbowski, M.5
  • 81
    • 85000919223 scopus 로고    scopus 로고
    • Elimination of paternal mitochondria in mouse embryos occurs through autophagic degradation dependent on PARKIN and MUL1
    • Rojansky, R., Cha, M.Y., Chan, D.C., Elimination of paternal mitochondria in mouse embryos occurs through autophagic degradation dependent on PARKIN and MUL1. eLife, 5, 2016, e17896.
    • (2016) eLife , vol.5 , pp. e17896
    • Rojansky, R.1    Cha, M.Y.2    Chan, D.C.3
  • 82
    • 84875581921 scopus 로고    scopus 로고
    • Fis1 acts as a mitochondrial recruitment factor for TBC1D15 that is involved in regulation of mitochondrial morphology
    • Onoue, K., Jofuku, A., Ban-Ishihara, R., Ishihara, T., Maeda, M., Koshiba, T., Itoh, T., Fukuda, M., Otera, H., Oka, T., et al. Fis1 acts as a mitochondrial recruitment factor for TBC1D15 that is involved in regulation of mitochondrial morphology. J. Cell Sci. 126 (2013), 176–185.
    • (2013) J. Cell Sci. , vol.126 , pp. 176-185
    • Onoue, K.1    Jofuku, A.2    Ban-Ishihara, R.3    Ishihara, T.4    Maeda, M.5    Koshiba, T.6    Itoh, T.7    Fukuda, M.8    Otera, H.9    Oka, T.10
  • 83
    • 84898652320 scopus 로고    scopus 로고
    • Mitochondrial Rab GAPs govern autophagosome biogenesis during mitophagy
    • Yamano, K., Fogel, A.I., Wang, C., van der Bliek, A.M., Youle, R.J., Mitochondrial Rab GAPs govern autophagosome biogenesis during mitophagy. eLife, 3, 2014, e01612.
    • (2014) eLife , vol.3 , pp. e01612
    • Yamano, K.1    Fogel, A.I.2    Wang, C.3    van der Bliek, A.M.4    Youle, R.J.5
  • 84
    • 84900315972 scopus 로고    scopus 로고
    • Paternal mitochondrial destruction after fertilization is mediated by a common endocytic and autophagic pathway in Drosophila. Dev
    • Politi, Y., Gal, L., Kalifa, Y., Ravid, L., Elazar, Z., Arama, E., Paternal mitochondrial destruction after fertilization is mediated by a common endocytic and autophagic pathway in Drosophila. Dev. Cell 29 (2014), 305–320.
    • (2014) Cell , vol.29 , pp. 305-320
    • Politi, Y.1    Gal, L.2    Kalifa, Y.3    Ravid, L.4    Elazar, Z.5    Arama, E.6
  • 86
    • 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 (2012), 660–668.
    • (2012) Dev. Cell , vol.22 , pp. 660-668
    • DeLuca, S.Z.1    O'Farrell, P.H.2
  • 88
    • 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 (2011), 1141–1144.
    • (2011) Science , vol.334 , pp. 1141-1144
    • Sato, M.1    Sato, K.2
  • 89
    • 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 (2009), 98–109.
    • (2009) Dev. Cell , vol.17 , pp. 98-109
    • Kanki, T.1    Wang, K.2    Cao, Y.3    Baba, M.4    Klionsky, D.J.5
  • 90
    • 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 (2009), 87–97.
    • (2009) Dev. Cell , vol.17 , pp. 87-97
    • Okamoto, K.1    Kondo-Okamoto, N.2    Ohsumi, Y.3
  • 92
    • 0036901104 scopus 로고    scopus 로고
    • Mechanism of cargo selection in the cytoplasm to vacuole targeting pathway
    • Shintani, T., Huang, W.P., Stromhaug, P.E., Klionsky, D.J., Mechanism of cargo selection in the cytoplasm to vacuole targeting pathway. Dev. Cell 3 (2002), 825–837.
    • (2002) Dev. Cell , vol.3 , pp. 825-837
    • Shintani, T.1    Huang, W.P.2    Stromhaug, P.E.3    Klionsky, D.J.4
  • 93
    • 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 (2008), 32386–32393.
    • (2008) J. Biol. Chem. , vol.283 , pp. 32386-32393
    • Kanki, T.1    Klionsky, D.J.2
  • 94
    • 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 (2013), 9–18.
    • (2013) Dev. Cell , vol.26 , pp. 9-18
    • Mao, K.1    Wang, K.2    Liu, X.3    Klionsky, D.J.4
  • 95
    • 84878780410 scopus 로고    scopus 로고
    • Mitochondrial degradation during starvation is selective and temporally distinct from bulk autophagy in yeast
    • Eiyama, A., Kondo-Okamoto, N., Okamoto, K., Mitochondrial degradation during starvation is selective and temporally distinct from bulk autophagy in yeast. FEBS Lett. 587 (2013), 1787–1792.
    • (2013) FEBS Lett. , vol.587 , pp. 1787-1792
    • Eiyama, A.1    Kondo-Okamoto, N.2    Okamoto, K.3
  • 97
    • 4644273585 scopus 로고    scopus 로고
    • Uth1p is involved in the autophagic degradation of mitochondria
    • Kissova, I., Deffieu, M., Manon, S., Camougrand, N., Uth1p is involved in the autophagic degradation of mitochondria. J. Biol. Chem. 279 (2004), 39068–39074.
    • (2004) J. Biol. Chem. , vol.279 , pp. 39068-39074
    • Kissova, I.1    Deffieu, M.2    Manon, S.3    Camougrand, N.4
  • 98
    • 27944482199 scopus 로고    scopus 로고
    • Impairing the bioenergetic status and the biogenesis of mitochondria triggers mitophagy in yeast
    • Priault, M., Salin, B., Schaeffer, J., Vallette, F.M., di Rago, J.P., Martinou, J.C., Impairing the bioenergetic status and the biogenesis of mitochondria triggers mitophagy in yeast. Cell Death Diff. 12 (2005), 1613–1621.
    • (2005) Cell Death Diff. , vol.12 , pp. 1613-1621
    • Priault, M.1    Salin, B.2    Schaeffer, J.3    Vallette, F.M.4    di Rago, J.P.5    Martinou, J.C.6
  • 99
    • 84864293013 scopus 로고    scopus 로고
    • Mitochondrial transcription factor A regulates mitochondrial transcription initiation, DNA packaging, and genome copy number
    • Campbell, C.T., Kolesar, J.E., Kaufman, B.A., Mitochondrial transcription factor A regulates mitochondrial transcription initiation, DNA packaging, and genome copy number. Biochim. Biophys. Acta 1819 (2012), 921–929.
    • (2012) Biochim. Biophys. Acta , vol.1819 , pp. 921-929
    • Campbell, C.T.1    Kolesar, J.E.2    Kaufman, B.A.3
  • 100
    • 41249086496 scopus 로고    scopus 로고
    • Nuclear respiratory factor 1 regulates all ten nuclear-encoded subunits of cytochrome c oxidase in neurons
    • Dhar, S.S., Ongwijitwat, S., Wong-Riley, M.T., Nuclear respiratory factor 1 regulates all ten nuclear-encoded subunits of cytochrome c oxidase in neurons. J. Biol. Chem. 283 (2008), 3120–3129.
    • (2008) J. Biol. Chem. , vol.283 , pp. 3120-3129
    • Dhar, S.S.1    Ongwijitwat, S.2    Wong-Riley, M.T.3
  • 101
    • 33646690296 scopus 로고    scopus 로고
    • Nuclear respiratory factor 2 senses changing cellular energy demands and its silencing down-regulates cytochrome oxidase and other target gene mRNAs
    • Ongwijitwat, S., Liang, H.L., Graboyes, E.M., Wong-Riley, M.T., Nuclear respiratory factor 2 senses changing cellular energy demands and its silencing down-regulates cytochrome oxidase and other target gene mRNAs. Gene 374 (2006), 39–49.
    • (2006) Gene , vol.374 , pp. 39-49
    • Ongwijitwat, S.1    Liang, H.L.2    Graboyes, E.M.3    Wong-Riley, M.T.4
  • 103
    • 0033803048 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor gamma coactivator-1 promotes cardiac mitochondrial biogenesis
    • Lehman, J.J., Barger, P.M., Kovacs, A., Saffitz, J.E., Medeiros, D.M., Kelly, D.P., Peroxisome proliferator-activated receptor gamma coactivator-1 promotes cardiac mitochondrial biogenesis. J. Clin. Invest. 106 (2000), 847–856.
    • (2000) J. Clin. Invest. , vol.106 , pp. 847-856
    • Lehman, J.J.1    Barger, P.M.2    Kovacs, A.3    Saffitz, J.E.4    Medeiros, D.M.5    Kelly, D.P.6
  • 104
    • 0036903174 scopus 로고    scopus 로고
    • Adaptations of skeletal muscle to exercise: rapid increase in the transcriptional coactivator PGC-1
    • Baar, K., Wende, A.R., Jones, T.E., Marison, M., Nolte, L.A., Chen, M., Kelly, D.P., Holloszy, J.O., Adaptations of skeletal muscle to exercise: rapid increase in the transcriptional coactivator PGC-1. FASEB J. 16 (2002), 1879–1886.
    • (2002) FASEB J. , vol.16 , pp. 1879-1886
    • Baar, K.1    Wende, A.R.2    Jones, T.E.3    Marison, M.4    Nolte, L.A.5    Chen, M.6    Kelly, D.P.7    Holloszy, J.O.8
  • 106
    • 0037322888 scopus 로고    scopus 로고
    • Exercise induces transient transcriptional activation of the PGC-1alpha gene in human skeletal muscle
    • Pilegaard, H., Saltin, B., Neufer, P.D., Exercise induces transient transcriptional activation of the PGC-1alpha gene in human skeletal muscle. J. Physiol. 546 (2003), 851–858.
    • (2003) J. Physiol. , vol.546 , pp. 851-858
    • Pilegaard, H.1    Saltin, B.2    Neufer, P.D.3
  • 107
    • 22144434964 scopus 로고    scopus 로고
    • Transcriptional coactivator PGC-1 alpha controls the energy state and contractile function of cardiac muscle
    • Arany, Z., He, H., Lin, J., Hoyer, K., Handschin, C., Toka, O., Ahmad, F., Matsui, T., Chin, S., Wu, P.H., et al. Transcriptional coactivator PGC-1 alpha controls the energy state and contractile function of cardiac muscle. Cell Metab. 1 (2005), 259–271.
    • (2005) Cell Metab. , vol.1 , pp. 259-271
    • Arany, Z.1    He, H.2    Lin, J.3    Hoyer, K.4    Handschin, C.5    Toka, O.6    Ahmad, F.7    Matsui, T.8    Chin, S.9    Wu, P.H.10
  • 108
    • 85020822242 scopus 로고    scopus 로고
    • AMPK: mechanisms of cellular energy sensing and restoration of metabolic balance
    • Garcia, D., Shaw, R.J., AMPK: mechanisms of cellular energy sensing and restoration of metabolic balance. Mol. Cell 66 (2017), 789–800.
    • (2017) Mol. Cell , vol.66 , pp. 789-800
    • Garcia, D.1    Shaw, R.J.2
  • 109
    • 34547545892 scopus 로고    scopus 로고
    • AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1alpha
    • Jager, S., Handschin, C., St-Pierre, J., Spiegelman, B.M., AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1alpha. Proc. Natl. Acad. Sci. USA 104 (2007), 12017–12022.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 12017-12022
    • Jager, S.1    Handschin, C.2    St-Pierre, J.3    Spiegelman, B.M.4
  • 111
    • 77951221542 scopus 로고    scopus 로고
    • The role of the Atg1/ULK1 complex in autophagy regulation. Curr. Opin
    • Mizushima, N., The role of the Atg1/ULK1 complex in autophagy regulation. Curr. Opin. Cell Biol. 22 (2010), 132–139.
    • (2010) Cell Biol. , vol.22 , pp. 132-139
    • Mizushima, N.1
  • 114
    • 84977630118 scopus 로고    scopus 로고
    • TFEB at a glance. J
    • Napolitano, G., Ballabio, A., TFEB at a glance. J. Cell Sci. 129 (2016), 2475–2481.
    • (2016) Cell Sci. , vol.129 , pp. 2475-2481
    • Napolitano, G.1    Ballabio, A.2
  • 117
    • 84893500088 scopus 로고    scopus 로고
    • GCN5-like protein 1 (GCN5L1) controls mitochondrial content through coordinated regulation of mitochondrial biogenesis and mitophagy
    • Scott, I., Webster, B.R., Chan, C.K., Okonkwo, J.U., Han, K., Sack, M.N., GCN5-like protein 1 (GCN5L1) controls mitochondrial content through coordinated regulation of mitochondrial biogenesis and mitophagy. J. Biol. Chem. 289 (2014), 2864–2872.
    • (2014) J. Biol. Chem. , vol.289 , pp. 2864-2872
    • Scott, I.1    Webster, B.R.2    Chan, C.K.3    Okonkwo, J.U.4    Han, K.5    Sack, M.N.6
  • 118
    • 84939820927 scopus 로고    scopus 로고
    • MiT/TFE transcription factors are activated during mitophagy downstream of Parkin and Atg5. J
    • Nezich, C.L., Wang, C., Fogel, A.I., Youle, R.J., MiT/TFE transcription factors are activated during mitophagy downstream of Parkin and Atg5. J. Cell Biol. 210 (2015), 435–450.
    • (2015) Cell Biol. , vol.210 , pp. 435-450
    • Nezich, C.L.1    Wang, C.2    Fogel, A.I.3    Youle, R.J.4
  • 119
    • 84930040430 scopus 로고    scopus 로고
    • New roles for mitochondrial proteases in health, ageing and disease
    • Quiros, P.M., Langer, T., Lopez-Otin, C., New roles for mitochondrial proteases in health, ageing and disease. Nat. Rev. Mol. Cell Biol. 16 (2015), 345–359.
    • (2015) Nat. Rev. Mol. Cell Biol. , vol.16 , pp. 345-359
    • Quiros, P.M.1    Langer, T.2    Lopez-Otin, C.3
  • 120
    • 79960716413 scopus 로고    scopus 로고
    • Regulating mitochondrial outer membrane proteins by ubiquitination and proteasomal degradation
    • Karbowski, M., Youle, R.J., Regulating mitochondrial outer membrane proteins by ubiquitination and proteasomal degradation. Curr. Opin. Cell Biol. 23 (2011), 476–482.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 476-482
    • Karbowski, M.1    Youle, R.J.2
  • 122
    • 84902682891 scopus 로고    scopus 로고
    • MUL1 acts in parallel to the PINK1/parkin pathway in regulating mitofusin and compensates for loss of PINK1/parkin
    • Yun, J., Puri, R., Yang, H., Lizzio, M.A., Wu, C., Sheng, Z.H., Guo, M., MUL1 acts in parallel to the PINK1/parkin pathway in regulating mitofusin and compensates for loss of PINK1/parkin. eLife, 3, 2014, e01958.
    • (2014) eLife , vol.3 , pp. e01958
    • Yun, J.1    Puri, R.2    Yang, H.3    Lizzio, M.A.4    Wu, C.5    Sheng, Z.H.6    Guo, M.7
  • 126
    • 84890925982 scopus 로고    scopus 로고
    • Bit-by-bit autophagic removal of parkin-labelled mitochondria
    • Yang, J.Y., Yang, W.Y., Bit-by-bit autophagic removal of parkin-labelled mitochondria. Nat. Commun, 4, 2013, 2428.
    • (2013) Nat. Commun , vol.4 , pp. 2428
    • Yang, J.Y.1    Yang, W.Y.2
  • 127
    • 84887486172 scopus 로고    scopus 로고
    • The accumulation of misfolded proteins in the mitochondrial matrix is sensed by PINK1 to induce PARK2/Parkin-mediated mitophagy of polarized mitochondria
    • Jin, S.M., Youle, R.J., The accumulation of misfolded proteins in the mitochondrial matrix is sensed by PINK1 to induce PARK2/Parkin-mediated mitophagy of polarized mitochondria. Autophagy 9 (2013), 1750–1757.
    • (2013) Autophagy , vol.9 , pp. 1750-1757
    • Jin, S.M.1    Youle, R.J.2
  • 130
    • 84889652177 scopus 로고    scopus 로고
    • Stress-regulated translational attenuation adapts mitochondrial protein import through Tim17A degradation
    • Rainbolt, T.K., Atanassova, N., Genereux, J.C., Wiseman, R.L., Stress-regulated translational attenuation adapts mitochondrial protein import through Tim17A degradation. Cell Metab. 18 (2013), 908–919.
    • (2013) Cell Metab. , vol.18 , pp. 908-919
    • Rainbolt, T.K.1    Atanassova, N.2    Genereux, J.C.3    Wiseman, R.L.4
  • 133
    • 84897863239 scopus 로고    scopus 로고
    • Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control
    • McLelland, G.L., Soubannier, V., Chen, C.X., McBride, H.M., Fon, E.A., Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control. EMBO J. 33 (2014), 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
  • 134
    • 84980027958 scopus 로고    scopus 로고
    • Syntaxin-17 delivers PINK1/parkin-dependent mitochondrial vesicles to the endolysosomal system
    • McLelland, G.L., Lee, S.A., McBride, H.M., Fon, E.A., Syntaxin-17 delivers PINK1/parkin-dependent mitochondrial vesicles to the endolysosomal system. J. Cell Biol. 214 (2016), 275–291.
    • (2016) J. Cell Biol. , vol.214 , pp. 275-291
    • McLelland, G.L.1    Lee, S.A.2    McBride, H.M.3    Fon, E.A.4
  • 135
    • 84888163960 scopus 로고    scopus 로고
    • Involvement of mitochondrial dynamics in the segregation of mitochondrial matrix proteins during stationary phase mitophagy
    • Abeliovich, H., Zarei, M., Rigbolt, K.T., Youle, R.J., Dengjel, J., Involvement of mitochondrial dynamics in the segregation of mitochondrial matrix proteins during stationary phase mitophagy. Nat. Commun., 4, 2013, 2789.
    • (2013) Nat. Commun. , vol.4 , pp. 2789
    • Abeliovich, H.1    Zarei, M.2    Rigbolt, K.T.3    Youle, R.J.4    Dengjel, J.5
  • 136
    • 84971519354 scopus 로고    scopus 로고
    • Selective sorting and destruction of mitochondrial membrane proteins in aged yeast
    • Hughes, A.L., Hughes, C.E., Henderson, K.A., Yazvenko, N., Gottschling, D.E., Selective sorting and destruction of mitochondrial membrane proteins in aged yeast. eLife, 5, 2016, e13943.
    • (2016) eLife , vol.5 , pp. e13943
    • Hughes, A.L.1    Hughes, C.E.2    Henderson, K.A.3    Yazvenko, N.4    Gottschling, D.E.5
  • 137
    • 84864744900 scopus 로고    scopus 로고
    • Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR activation
    • Nargund, A.M., Pellegrino, M.W., Fiorese, C.J., Baker, B.M., Haynes, C.M., Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR activation. Science 337 (2012), 587–590.
    • (2012) Science , vol.337 , pp. 587-590
    • Nargund, A.M.1    Pellegrino, M.W.2    Fiorese, C.J.3    Baker, B.M.4    Haynes, C.M.5
  • 138
    • 33748901113 scopus 로고    scopus 로고
    • Ubiquitin-like protein 5 positively regulates chaperone gene expression in the mitochondrial unfolded protein response
    • Benedetti, C., Haynes, C.M., Yang, Y., Harding, H.P., Ron, D., Ubiquitin-like protein 5 positively regulates chaperone gene expression in the mitochondrial unfolded protein response. Genetics 174 (2006), 229–239.
    • (2006) Genetics , vol.174 , pp. 229-239
    • Benedetti, C.1    Haynes, C.M.2    Yang, Y.3    Harding, H.P.4    Ron, D.5
  • 139
    • 34848861368 scopus 로고    scopus 로고
    • ClpP mediates activation of a mitochondrial unfolded protein response in C. elegans
    • Haynes, C.M., Petrova, K., Benedetti, C., Yang, Y., Ron, D., ClpP mediates activation of a mitochondrial unfolded protein response in C. elegans. Dev. Cell 13 (2007), 467–480.
    • (2007) Dev. Cell , vol.13 , pp. 467-480
    • Haynes, C.M.1    Petrova, K.2    Benedetti, C.3    Yang, Y.4    Ron, D.5
  • 140
    • 84926180334 scopus 로고    scopus 로고
    • Mitochondrial and nuclear accumulation of the transcription factor ATFS-1 promotes OXPHOS recovery during the UPR(mt)
    • Nargund, A.M., Fiorese, C.J., Pellegrino, M.W., Deng, P., Haynes, C.M., Mitochondrial and nuclear accumulation of the transcription factor ATFS-1 promotes OXPHOS recovery during the UPR(mt). Mol. Cell 58 (2015), 123–133.
    • (2015) Mol. Cell , vol.58 , pp. 123-133
    • Nargund, A.M.1    Fiorese, C.J.2    Pellegrino, M.W.3    Deng, P.4    Haynes, C.M.5
  • 141
    • 84990040254 scopus 로고    scopus 로고
    • Mitochondrial unfolded protein response controls matrix pre-RNA processing and translation
    • Munch, C., Harper, J.W., Mitochondrial unfolded protein response controls matrix pre-RNA processing and translation. Nature 534 (2016), 710–713.
    • (2016) Nature , vol.534 , pp. 710-713
    • Munch, C.1    Harper, J.W.2
  • 144
    • 37849048003 scopus 로고    scopus 로고
    • Discovery of genes activated by the mitochondrial unfolded protein response (mtUPR) and cognate promoter elements
    • Aldridge, J.E., Horibe, T., Hoogenraad, N.J., Discovery of genes activated by the mitochondrial unfolded protein response (mtUPR) and cognate promoter elements. PLoS One, 2, 2007, e874.
    • (2007) PLoS One , vol.2 , pp. e874
    • Aldridge, J.E.1    Horibe, T.2    Hoogenraad, N.J.3
  • 146
  • 148
    • 84940517301 scopus 로고    scopus 로고
    • A cytosolic network suppressing mitochondria-mediated proteostatic stress and cell death
    • Wang, X., Chen, X.J., A cytosolic network suppressing mitochondria-mediated proteostatic stress and cell death. Nature 524 (2015), 481–484.
    • (2015) Nature , vol.524 , pp. 481-484
    • Wang, X.1    Chen, X.J.2
  • 149
    • 84884313897 scopus 로고    scopus 로고
    • Tissue- and cell-type-specific manifestations of heteroplasmic mtDNA 3243A>G mutation in human induced pluripotent stem cell-derived disease model
    • Hamalainen, R.H., Manninen, T., Koivumaki, H., Kislin, M., Otonkoski, T., Suomalainen, A., Tissue- and cell-type-specific manifestations of heteroplasmic mtDNA 3243A>G mutation in human induced pluripotent stem cell-derived disease model. Proc. Natl. Acad. Sci. USA 110 (2013), E3622–E3630.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. E3622-E3630
    • Hamalainen, R.H.1    Manninen, T.2    Koivumaki, H.3    Kislin, M.4    Otonkoski, T.5    Suomalainen, A.6
  • 150
    • 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 (2010), 11835–11840.
    • (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
  • 153
    • 84970973729 scopus 로고    scopus 로고
    • Maintenance and propagation of a deleterious mitochondrial genome by the mitochondrial unfolded protein response
    • Lin, Y.F., Schulz, A.M., Pellegrino, M.W., Lu, Y., Shaham, S., Haynes, C.M., Maintenance and propagation of a deleterious mitochondrial genome by the mitochondrial unfolded protein response. Nature 533 (2016), 416–419.
    • (2016) Nature , vol.533 , pp. 416-419
    • Lin, Y.F.1    Schulz, A.M.2    Pellegrino, M.W.3    Lu, Y.4    Shaham, S.5    Haynes, C.M.6
  • 154
    • 84912048734 scopus 로고    scopus 로고
    • Parkin modulates heteroplasmy of truncated mtDNA in Caenorhabditis elegans
    • Valenci, I., Yonai, L., Bar-Yaacov, D., Mishmar, D., Ben-Zvi, A., Parkin modulates heteroplasmy of truncated mtDNA in Caenorhabditis elegans. Mitochondrion 20 (2015), 64–70.
    • (2015) Mitochondrion , vol.20 , pp. 64-70
    • Valenci, I.1    Yonai, L.2    Bar-Yaacov, D.3    Mishmar, D.4    Ben-Zvi, A.5
  • 156
  • 158
    • 85009106959 scopus 로고    scopus 로고
    • Parkin deficiency accelerates consequences of mitochondrial DNA deletions and Parkinsonism
    • Song, L., McMackin, M., Nguyen, A., Cortopassi, G., Parkin deficiency accelerates consequences of mitochondrial DNA deletions and Parkinsonism. Neurobiol. Dis. 100 (2017), 30–38.
    • (2017) Neurobiol. Dis. , vol.100 , pp. 30-38
    • Song, L.1    McMackin, M.2    Nguyen, A.3    Cortopassi, G.4
  • 159
    • 84921369563 scopus 로고    scopus 로고
    • The roles of PINK1, parkin, and mitochondrial fidelity in Parkinson's disease
    • Pickrell, A.M., Youle, R.J., The roles of PINK1, parkin, and mitochondrial fidelity in Parkinson's disease. Neuron 85 (2015), 257–273.
    • (2015) Neuron , vol.85 , pp. 257-273
    • Pickrell, A.M.1    Youle, R.J.2
  • 162
    • 79961239061 scopus 로고    scopus 로고
    • Impaired mitochondrial transport and Parkin-independent degeneration of respiratory chain-deficient dopamine neurons in vivo
    • Sterky, F.H., Lee, S., Wibom, R., Olson, L., Larsson, N.G., Impaired mitochondrial transport and Parkin-independent degeneration of respiratory chain-deficient dopamine neurons in vivo. Proc. Natl. Acad. Sci. USA 108 (2011), 12937–12942.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 12937-12942
    • Sterky, F.H.1    Lee, S.2    Wibom, R.3    Olson, L.4    Larsson, N.G.5
  • 165
    • 84949663455 scopus 로고    scopus 로고
    • alpha-MHC MitoTimer mouse: In vivo mitochondrial turnover model reveals remarkable mitochondrial heterogeneity in the heart
    • Stotland, A., Gottlieb, R.A., alpha-MHC MitoTimer mouse: In vivo mitochondrial turnover model reveals remarkable mitochondrial heterogeneity in the heart. J. Mol. Cell. Cardiol. 90 (2016), 53–58.
    • (2016) J. Mol. Cell. Cardiol. , vol.90 , pp. 53-58
    • Stotland, A.1    Gottlieb, R.A.2
  • 166
    • 80052145606 scopus 로고    scopus 로고
    • A sensitive and quantitative technique for detecting autophagic events based on lysosomal delivery
    • Katayama, H., Kogure, T., Mizushima, N., Yoshimori, T., Miyawaki, A., A sensitive and quantitative technique for detecting autophagic events based on lysosomal delivery. Chem. Biol. 18 (2011), 1042–1052.
    • (2011) Chem. Biol. , vol.18 , pp. 1042-1052
    • Katayama, H.1    Kogure, T.2    Mizushima, N.3    Yoshimori, T.4    Miyawaki, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.