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Volumn 22, Issue 12, 2015, Pages 1032-1046

Hypoxia Activation of Mitophagy and Its Role in Disease Pathogenesis

Author keywords

[No Author keywords available]

Indexed keywords

ATG32 PROTEIN; FUN14 DOMAIN CONTAINING 1 PROTEIN; OUTER MEMBRANE PROTEIN; PARKIN; PROTEIN BNIP3; RECEPTOR; UNCLASSIFIED DRUG; APOPTOSIS REGULATORY PROTEIN;

EID: 84926624248     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2014.6204     Document Type: Review
Times cited : (92)

References (161)
  • 1
    • 0038156122 scopus 로고    scopus 로고
    • The proapoptotic factor Nix is coexpressed with BclxL during terminal erythroid differentiation
    • Aerbajinai W, Giattina M, Lee YT, Raffeld M, and Miller JL. The proapoptotic factor Nix is coexpressed with BclxL during terminal erythroid differentiation. Blood 102: 712-717, 2003.
    • (2003) Blood , vol.102 , pp. 712-717
    • Aerbajinai, W.1    Giattina, M.2    Lee, Y.T.3    Raffeld, M.4    Miller, J.L.5
  • 3
    • 38949119423 scopus 로고    scopus 로고
    • Hypoxia induces autophagic cell death in apoptosis-competent cells through a mechanism involving BNIP3
    • Azad MB, Chen Y, Henson ES, Cizeau J, McMillan-Ward E, Israels SJ, and Gibson SB. Hypoxia induces autophagic cell death in apoptosis-competent cells through a mechanism involving BNIP3. Autophagy 4: 195-204, 2008.
    • (2008) Autophagy , vol.4 , pp. 195-204
    • Azad, M.B.1    Chen, Y.2    Henson, E.S.3    Cizeau, J.4    McMillan-Ward, E.5    Israels, S.J.6    Gibson, S.B.7
  • 4
    • 68549135295 scopus 로고    scopus 로고
    • Hypoxia-induced BNIP3 expression and mitophagy: In vivo comparison of the rat and the hypoxia-tolerant mole rat, Spalax ehrenbergi
    • Band M, Joel A, Hernandez A, and Avivi A. Hypoxia-induced BNIP3 expression and mitophagy: in vivo comparison of the rat and the hypoxia-tolerant mole rat, Spalax ehrenbergi. FASEB J 23: 2327-2335, 2009.
    • (2009) FASEB J , vol.23 , pp. 2327-2335
    • Band, M.1    Joel, A.2    Hernandez, A.3    Avivi, A.4
  • 5
    • 66349121718 scopus 로고    scopus 로고
    • Hypoxia-induced autophagy is mediated through hypoxia-inducible factor induction of BNIP3 and BNIP3L via their BH3 domains
    • Bellot G, Garcia-Medina R, Gounon P, Chiche J, Roux D, Pouyssegur J, and Mazure NM. Hypoxia-induced autophagy is mediated through hypoxia-inducible factor induction of BNIP3 and BNIP3L via their BH3 domains. Mol Cell Biol 29: 2570-2581, 2009.
    • (2009) Mol Cell Biol , vol.29 , pp. 2570-2581
    • Bellot, G.1    Garcia-Medina, R.2    Gounon, P.3    Chiche, J.4    Roux, D.5    Pouyssegur, J.6    Mazure, N.M.7
  • 6
    • 84873685781 scopus 로고    scopus 로고
    • Hypoxia, MTOR and autophagy: Converging on senescence or quiescence
    • Blagosklonny MV. Hypoxia, MTOR and autophagy: converging on senescence or quiescence. Autophagy 9: 260-262, 2013.
    • (2013) Autophagy , vol.9 , pp. 260-262
    • Blagosklonny, M.V.1
  • 7
  • 9
    • 0035282782 scopus 로고    scopus 로고
    • Regulation of mitochondrial respiration by nitric oxide inhibition of cytochrome c oxidase
    • Brown GC. Regulation of mitochondrial respiration by nitric oxide inhibition of cytochrome c oxidase. Biochim Biophys Acta 1504: 46-57, 2001.
    • (2001) Biochim Biophys Acta , vol.1504 , pp. 46-57
    • Brown, G.C.1
  • 10
    • 0028291271 scopus 로고
    • Effects of hypoxia on membrane potential and intracellular calcium in rat neonatal carotid body type I cells
    • Buckler KJ and Vaughan-Jones RD. Effects of hypoxia on membrane potential and intracellular calcium in rat neonatal carotid body type I cells. J Physiol 476: 423-428, 1994.
    • (1994) J Physiol , vol.476 , pp. 423-428
    • Buckler, K.J.1    Vaughan-Jones, R.D.2
  • 11
    • 84858701257 scopus 로고    scopus 로고
    • Spatial parkin translocation and degradation of damaged mitochondria via mitophagy in live cortical neurons
    • Cai Q, Zakaria HM, Simone A, and Sheng ZH. Spatial parkin translocation and degradation of damaged mitochondria via mitophagy in live cortical neurons. Curr Biol 22: 545-552, 2012.
    • (2012) Curr Biol , vol.22 , pp. 545-552
    • Cai, Q.1    Zakaria, H.M.2    Simone, A.3    Sheng, Z.H.4
  • 12
    • 0035378322 scopus 로고    scopus 로고
    • Functional mitochondria are required for amyloid beta-mediated neurotoxicity
    • Cardoso SM, Santos S, Swerdlow RH, and Oliveira CR. Functional mitochondria are required for amyloid beta-mediated neurotoxicity. FASEB J 15: 1439-1441, 2001.
    • (2001) FASEB J , vol.15 , pp. 1439-1441
    • Cardoso, S.M.1    Santos, S.2    Swerdlow, R.H.3    Oliveira, C.R.4
  • 13
  • 19
    • 77951096150 scopus 로고    scopus 로고
    • Mitochondrial dynamics-fusion, fission, movement, and mitophagy-in neurodegenerative diseases
    • Chen H and Chan DC. Mitochondrial dynamics-fusion, fission, movement, and mitophagy-in neurodegenerative diseases. Hum Mol Genet 18: R169-R176, 2009.
    • (2009) Hum Mol Genet , vol.18 , pp. R169-R176
    • Chen, H.1    Chan, D.C.2
  • 20
    • 84876531457 scopus 로고    scopus 로고
    • PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria
    • Chen Y and Dorn GW, 2nd. PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria. Science 340: 471-475, 2013.
    • (2013) Science , vol.340 , pp. 471-475
    • Chen, Y.1    Dorn, G.W.2
  • 23
    • 0036162636 scopus 로고    scopus 로고
    • Nitric oxide and cytochrome oxidase: Substrate, inhibitor or effector?
    • Cooper CE. Nitric oxide and cytochrome oxidase: substrate, inhibitor or effector? Trends Biochem Sci 27: 33-39, 2002.
    • (2002) Trends Biochem Sci , vol.27 , pp. 33-39
    • Cooper, C.E.1
  • 24
    • 34447509483 scopus 로고    scopus 로고
    • Nitric oxide regulation of mitochondrial oxygen consumption II: Molecular mechanism and tissue physiology
    • Cooper CE and Giulivi C. Nitric oxide regulation of mitochondrial oxygen consumption II: molecular mechanism and tissue physiology. Am J Physiol Cell Physiol 292: C1993-C2003, 2007.
    • (2007) Am J Physiol Cell Physiol , vol.292 , pp. C1993-C2003
    • Cooper, C.E.1    Giulivi, C.2
  • 25
    • 84865176138 scopus 로고    scopus 로고
    • Locus-specific mutation databases for neurodegenerative brain diseases
    • Cruts M, Theuns J, and Van Broeckhoven C. Locus-specific mutation databases for neurodegenerative brain diseases. Hum Mutat 33: 1340-1344, 2012.
    • (2012) Hum Mutat , vol.33 , pp. 1340-1344
    • Cruts, M.1    Theuns, J.2    Van Broeckhoven, C.3
  • 26
    • 3042562282 scopus 로고    scopus 로고
    • Pivotal role of the cell death factor BNIP3 in ceramide-induced autophagic cell death in malignant glioma cells
    • Daido S, Kanzawa T, Yamamoto A, Takeuchi H, Kondo Y, and Kondo S. Pivotal role of the cell death factor BNIP3 in ceramide-induced autophagic cell death in malignant glioma cells. Cancer Res 64: 4286-4293, 2004.
    • (2004) Cancer Res , vol.64 , pp. 4286-4293
    • Daido, S.1    Kanzawa, T.2    Yamamoto, A.3    Takeuchi, H.4    Kondo, Y.5    Kondo, S.6
  • 28
    • 77956252454 scopus 로고    scopus 로고
    • Nix is critical to two distinct phases of mitophagy, reactive oxygen species-mediated autophagy induction and Parkin-ubiquitin-p62-mediated mitochondrial priming
    • Ding WX, Ni HM, Li M, Liao Y, Chen X, Stolz DB, Dorn GW, 2nd, and Yin XM. Nix is critical to two distinct phases of mitophagy, reactive oxygen species-mediated autophagy induction and Parkin-ubiquitin-p62-mediated mitochondrial priming. J Biol Chem 285: 27879-27890, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 27879-27890
    • Ding, W.X.1    Ni, H.M.2    Li, M.3    Liao, Y.4    Chen, X.5    Stolz, D.B.6    Dorn, G.W.7    Yin, X.M.8
  • 29
    • 77955514158 scopus 로고    scopus 로고
    • Mitochondrial pruning by Nix and BNip3: An essential function for cardiac-expressed death factors
    • Dorn GW, 2nd. Mitochondrial pruning by Nix and BNip3: an essential function for cardiac-expressed death factors. J Cardiovasc Transl Res 3: 374-383, 2010.
    • (2010) J Cardiovasc Transl Res , vol.3 , pp. 374-383
    • Dorn, G.W.1
  • 30
    • 24144458255 scopus 로고    scopus 로고
    • CNS mitochondria in neurodegenerative disorders
    • Dubinsky JM. CNS mitochondria in neurodegenerative disorders. Antioxid Redox Signal 7: 1089-1091, 2005.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 1089-1091
    • Dubinsky, J.M.1
  • 32
    • 70350064297 scopus 로고    scopus 로고
    • The HIF1alpha-inducible pro-cell death gene BNIP3 is a novel target of SIM2s repression through cross-talk on the hypoxia response element
    • Farrall AL and Whitelaw ML. The HIF1alpha-inducible pro-cell death gene BNIP3 is a novel target of SIM2s repression through cross-talk on the hypoxia response element. Oncogene 28: 3671-3680, 2009.
    • (2009) Oncogene , vol.28 , pp. 3671-3680
    • Farrall, A.L.1    Whitelaw, M.L.2
  • 33
    • 84860709659 scopus 로고    scopus 로고
    • FOXO3a regulates reactive oxygen metabolism by inhibiting mitochondrial gene expression
    • Ferber EC, Peck B, Delpuech O, Bell GP, East P, and Schulze A. FOXO3a regulates reactive oxygen metabolism by inhibiting mitochondrial gene expression. Cell Death Differ 19: 968-979, 2012.
    • (2012) Cell Death Differ , vol.19 , pp. 968-979
    • Ferber, E.C.1    Peck, B.2    Delpuech, O.3    Bell, G.P.4    East, P.5    Schulze, A.6
  • 36
    • 66449083078 scopus 로고    scopus 로고
    • ULK1 center dot ATG13 center dot FIP200 complex mediates mTOR signaling and is essential for autophagy
    • Ganley IG, Lam DH, Wang JR, Ding XJ, Chen S, and Jiang XJ. ULK1 center dot ATG13 center dot FIP200 complex mediates mTOR signaling and is essential for autophagy. J Biol Chem 284: 12297-12305, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 12297-12305
    • Ganley, I.G.1    Lam, D.H.2    Wang, J.R.3    Ding, X.J.4    Chen, S.5    Jiang, X.J.6
  • 37
    • 78649463381 scopus 로고    scopus 로고
    • Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy
    • Gegg ME, Cooper JM, Chau KY, Rojo M, Schapira AH, and Taanman JW. Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy. Hum Mol Genet 19: 4861-4870, 2010.
    • (2010) Hum Mol Genet , vol.19 , pp. 4861-4870
    • Gegg, M.E.1    Cooper, J.M.2    Chau, K.Y.3    Rojo, M.4    Schapira, A.H.5    Taanman, J.W.6
  • 40
    • 79955623510 scopus 로고    scopus 로고
    • During autophagy mitochondria elongate, are spared from degradation and sustain cell viability
    • Gomes LC, Di Benedetto G, and Scorrano L. During autophagy mitochondria elongate, are spared from degradation and sustain cell viability. Nat Cell Biol 13: 589-598, 2011.
    • (2011) Nat Cell Biol , vol.13 , pp. 589-598
    • Gomes, L.C.1    Di Benedetto, G.2    Scorrano, L.3
  • 42
    • 39849094082 scopus 로고    scopus 로고
    • Transient hypoxia stimulates mitochondrial biogenesis in brain subcortex by a neuronal nitric oxide synthase-dependent mechanism
    • Gutsaeva DR, Carraway MS, Suliman HB, Demchenko IT, Shitara H, Yonekawa H, and Piantadosi CA. Transient hypoxia stimulates mitochondrial biogenesis in brain subcortex by a neuronal nitric oxide synthase-dependent mechanism. J Neurosci 28: 2015-2024, 2008.
    • (2008) J Neurosci , vol.28 , pp. 2015-2024
    • Gutsaeva, D.R.1    Carraway, M.S.2    Suliman, H.B.3    Demchenko, I.T.4    Shitara, H.5    Yonekawa, H.6    Piantadosi, C.A.7
  • 46
    • 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 RA, Quinsay MN, Orogo AM, Giang K, Rikka S, and Gustafsson AB. 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: 19094-19104, 2012.
    • (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
  • 48
    • 0035925098 scopus 로고    scopus 로고
    • Tumor hypoxia: Definitions and current clinical, biologic, and molecular aspects
    • Hockel M and Vaupel P. Tumor hypoxia: definitions and current clinical, biologic, and molecular aspects. J Natl Cancer Inst 93: 266-276, 2001.
    • (2001) J Natl Cancer Inst , vol.93 , pp. 266-276
    • Hockel, M.1    Vaupel, P.2
  • 52
    • 0033549869 scopus 로고    scopus 로고
    • Bcl-2/E1B 19 kDa-interacting protein 3-like protein (Bnip3L) interacts with Bcl-2/Bcl-x(L) and induces apoptosis by altering mitochondrial membrane permeability
    • Imazu T, Shimizu S, Tagami S, Matsushima M, Nakamura Y, Miki T, Okuyama A, and Tsujimoto Y. Bcl-2/E1B 19 kDa-interacting protein 3-like protein (Bnip3L) interacts with Bcl-2/Bcl-x(L) and induces apoptosis by altering mitochondrial membrane permeability. Oncogene 18: 4523-4529, 1999.
    • (1999) Oncogene , vol.18 , pp. 4523-4529
    • Imazu, T.1    Shimizu, S.2    Tagami, S.3    Matsushima, M.4    Nakamura, Y.5    Miki, T.6    Okuyama, A.7    Tsujimoto, Y.8
  • 53
    • 84857850213 scopus 로고    scopus 로고
    • Structures containing Atg9A and the ULK1 complex independently target depolarized mitochondria at initial stages of Parkin-mediated mitophagy
    • Itakura E, Kishi-Itakura C, Koyama-Honda I, and Mizushima N. Structures containing Atg9A and the ULK1 complex independently target depolarized mitochondria at initial stages of Parkin-mediated mitophagy. J Cell Sci 125: 1488-1499, 2012.
    • (2012) J Cell Sci , vol.125 , pp. 1488-1499
    • Itakura, E.1    Kishi-Itakura, C.2    Koyama-Honda, I.3    Mizushima, N.4
  • 54
    • 1842404697 scopus 로고
    • Reactive oxygen species during ischemia reflow injury in isolated perfused rat-liver
    • Jaeschke H, Smith CV, and Mitchell JR. Reactive oxygen species during ischemia reflow injury in isolated perfused rat-liver. J Clin Invest 81: 1240-1246, 1988.
    • (1988) J Clin Invest , vol.81 , pp. 1240-1246
    • Jaeschke, H.1    Smith, C.V.2    Mitchell, J.R.3
  • 57
    • 84891738225 scopus 로고    scopus 로고
    • Autophagy and human diseases
    • Jiang P and Mizushima N. Autophagy and human diseases. Cell Res 24: 69-79, 2014.
    • (2014) Cell Res , vol.24 , pp. 69-79
    • Jiang, P.1    Mizushima, N.2
  • 60
    • 67650264633 scopus 로고    scopus 로고
    • Atg32 is a mitochondrial protein that confers selectivity during mitophagy
    • Kanki T, Wang K, Cao Y, Baba M, and Klionsky DJ. 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
  • 63
    • 33751169387 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 (HIF-1)
    • Ke Q and Costa M. Hypoxia-inducible factor-1 (HIF-1). Mol Pharmacol 70: 1469-1480, 2006.
    • (2006) Mol Pharmacol , vol.70 , pp. 1469-1480
    • Ke, Q.1    Costa, M.2
  • 65
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • Kim J, Kundu M, Viollet B, and Guan KL. AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nat Cell Biol 13: 132-141, 2011.
    • (2011) Nat Cell Biol , vol.13 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Guan, K.L.4
  • 67
    • 33644614520 scopus 로고    scopus 로고
    • HIF-1-mediated expression of pyruvate dehydrogenase kinase: A metabolic switch required for cellular adaptation to hypoxia
    • Kim JW, Tchernyshyov I, Semenza GL, and Dang CV. HIF-1-mediated expression of pyruvate dehydrogenase kinase: a metabolic switch required for cellular adaptation to hypoxia. Cell Metab 3: 177-185, 2006.
    • (2006) Cell Metab , vol.3 , pp. 177-185
    • Kim, J.W.1    Tchernyshyov, I.2    Semenza, G.L.3    Dang, C.V.4
  • 69
    • 4644273585 scopus 로고    scopus 로고
    • Uth1p is involved in the autophagic degradation of mitochondria
    • Kissova I, Deffieu M, Manon S, and Camougrand N. Uth1p is involved in the autophagic degradation of mitochondria. J Biol Chem 279: 39068-39074, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 39068-39074
    • Kissova, I.1    Deffieu, M.2    Manon, S.3    Camougrand, N.4
  • 74
    • 84867724832 scopus 로고    scopus 로고
    • Mitochondria and mitophagy the yin and yang of cell death control
    • Kubli DA and Gustafsson AB. Mitochondria and mitophagy the yin and yang of cell death control. Circ Res 111: 1208-1221, 2012.
    • (2012) Circ Res , vol.111 , pp. 1208-1221
    • Kubli, D.A.1    Gustafsson, A.B.2
  • 75
    • 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 CY, Wu J, Zhao F, Zhang J, Selak MA, Ney PA, and Thompson CB. Ulk1 plays a critical role in the autophagic clearance of mitochondria and ribosomes during reticulocyte maturation. Blood 112: 1493-1502, 2008.
    • (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
  • 76
    • 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 SM, Kane LA, and Youle RJ. Role of PINK1 binding to the TOM complex and alternate intracellular membranes in recruitment and activation of the E3 ligase Parkin. Dev Cell 22: 320-333, 2012.
    • (2012) Dev Cell , vol.22 , pp. 320-333
    • Lazarou, M.1    Jin, S.M.2    Kane, L.A.3    Youle, R.J.4
  • 77
    • 80355127945 scopus 로고    scopus 로고
    • Mitochondrial autophagy by Bnip3 involves Drp1-mediated mitochondrial fission and recruitment of Parkin in cardiac myocytes
    • Lee Y, Lee HY, Hanna RA, and Gustafsson AB. Mitochondrial autophagy by Bnip3 involves Drp1-mediated mitochondrial fission and recruitment of Parkin in cardiac myocytes. Am J Physiol Heart Circ Physiol 301: H1924-H1931, 2011.
    • (2011) Am J Physiol Heart Circ Physiol , vol.301 , pp. H1924-H1931
    • Lee, Y.1    Lee, H.Y.2    Hanna, R.A.3    Gustafsson, A.B.4
  • 79
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • Lin MT and Beal MF. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 443: 787-795, 2006.
    • (2006) Nature , vol.443 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 80
    • 84874931751 scopus 로고    scopus 로고
    • Reactive oxygen species and the free radical theory of aging
    • Liochev SI. Reactive oxygen species and the free radical theory of aging. Free Radic Biol Med 60: 1-4, 2013.
    • (2013) Free Radic Biol Med , vol.60 , pp. 1-4
    • Liochev, S.I.1
  • 82
    • 80052711240 scopus 로고    scopus 로고
    • Altered fusion dynamics underlie unique morphological changes in mitochondria during hypoxia-reoxygenation stress
    • Liu X and Hajnoczky G. Altered fusion dynamics underlie unique morphological changes in mitochondria during hypoxia-reoxygenation stress. Cell Death Differ 18: 1561-1572, 2011.
    • (2011) Cell Death Differ , vol.18 , pp. 1561-1572
    • Liu, X.1    Hajnoczky, G.2
  • 83
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X, Kim CN, Yang J, Jemmerson R, and Wang X. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 86: 147-157, 1996.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 84
    • 0029759933 scopus 로고    scopus 로고
    • Oxygen-sensing by ion channels and the regulation of cellular functions
    • Lopez-Barneo J. Oxygen-sensing by ion channels and the regulation of cellular functions. Trends Neurosci 19: 435-440, 1996.
    • (1996) Trends Neurosci , vol.19 , pp. 435-440
    • Lopez-Barneo, J.1
  • 85
    • 84887495000 scopus 로고    scopus 로고
    • Regulation and function of mitophagy in development and cancer
    • Lu H, Li G, Liu L, Feng L, Wang X, and Jin H. Regulation and function of mitophagy in development and cancer. Autophagy 9: 1720-1736, 2013.
    • (2013) Autophagy , vol.9 , pp. 1720-1736
    • Lu, H.1    Li, G.2    Liu, L.3    Feng, L.4    Wang, X.5    Jin, H.6
  • 87
    • 34250894388 scopus 로고    scopus 로고
    • BH3- only proteins and BH3 mimetics induce autophagy by competitively disrupting the interaction between Beclin 1 and Bcl-2/Bcl-X-L
    • Maiuri MC, Criollo A, Tasdemir E, Vicencio JM, Tajeddine N, Hickman JA, Geneste O, and Kroemer G. BH3- only proteins and BH3 mimetics induce autophagy by competitively disrupting the interaction between Beclin 1 and Bcl-2/Bcl-X-L. Autophagy 3: 374-376, 2007.
    • (2007) Autophagy , vol.3 , pp. 374-376
    • Maiuri, M.C.1    Criollo, A.2    Tasdemir, E.3    Vicencio, J.M.4    Tajeddine, N.5    Hickman, J.A.6    Geneste, O.7    Kroemer, G.8
  • 88
    • 34548188741 scopus 로고    scopus 로고
    • Self-eating and self-killing: Crosstalk between autophagy and apoptosis
    • Maiuri MC, Zalckvar E, Kimchi A, and Kroemer G. Self-eating and self-killing: crosstalk between autophagy and apoptosis. Nat Rev Mol Cell Biol 8: 741-752, 2007.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 741-752
    • Maiuri, M.C.1    Zalckvar, E.2    Kimchi, A.3    Kroemer, G.4
  • 90
    • 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, and Klionsky DJ. 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
  • 91
    • 79958219318 scopus 로고    scopus 로고
    • Two MAPK-signaling pathways are required for mitophagy in Saccharomyces cerevisiae
    • Mao K, Wang K, Zhao M, Xu T, and Klionsky DJ. Two MAPK-signaling pathways are required for mitophagy in Saccharomyces cerevisiae. J Cell Biol 193: 755-767, 2011.
    • (2011) J Cell Biol , vol.193 , pp. 755-767
    • Mao, K.1    Wang, K.2    Zhao, M.3    Xu, T.4    Klionsky, D.J.5
  • 93
    • 0346027211 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor-1alpha by nitric oxide through mitochondria-dependent and -independent pathways
    • Mateo J, Garcia-Lecea M, Cadenas S, Hernandez C, and Moncada S. Regulation of hypoxia-inducible factor-1alpha by nitric oxide through mitochondria-dependent and -independent pathways. Biochem J 376: 537-544, 2003.
    • (2003) Biochem J , vol.376 , pp. 537-544
    • Mateo, J.1    Garcia-Lecea, M.2    Cadenas, S.3    Hernandez, C.4    Moncada, S.5
  • 94
    • 79959999581 scopus 로고    scopus 로고
    • Microautophagy in mammalian cells revisiting a 40-year-old conundrum
    • Mijaljica D, Prescott M, and Devenish RJ. Microautophagy in mammalian cells revisiting a 40-year-old conundrum. Autophagy 7: 673-682, 2011.
    • (2011) Autophagy , vol.7 , pp. 673-682
    • Mijaljica, D.1    Prescott, M.2    Devenish, R.J.3
  • 95
    • 36249025723 scopus 로고    scopus 로고
    • Autophagy: Process and function
    • Mizushima N. Autophagy: process and function. Genes Dev 21: 2861-2873, 2007.
    • (2007) Genes Dev , vol.21 , pp. 2861-2873
    • Mizushima, N.1
  • 97
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra D, Tanaka A, Suen DF, and Youle RJ. 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
  • 99
    • 84865536459 scopus 로고    scopus 로고
    • The mitochondrial Dnm1-like fission component is required for lgA2-induced mitophagy but dispensable for starvation-induced mitophagy in Ustilago maydis
    • Nieto-Jacobo F, Pasch D, and Basse CW. The mitochondrial Dnm1-like fission component is required for lgA2-induced mitophagy but dispensable for starvation-induced mitophagy in Ustilago maydis. Eukaryot Cell 11: 1154-1166, 2012.
    • (2012) Eukaryot Cell , vol.11 , pp. 1154-1166
    • Nieto-Jacobo, F.1    Pasch, D.2    Basse, C.W.3
  • 101
    • 34250898919 scopus 로고    scopus 로고
    • Mdm38 protein depletion causes loss of mitochondrial K+/H+ exchange activity, osmotic swelling and mitophagy
    • Nowikovsky K, Reipert S, Devenish RJ, and Schweyen RJ. Mdm38 protein depletion causes loss of mitochondrial K+/H+ exchange activity, osmotic swelling and mitophagy. Cell Death Differ 14: 1647-1656, 2007.
    • (2007) Cell Death Differ , vol.14 , pp. 1647-1656
    • Nowikovsky, K.1    Reipert, S.2    Devenish, R.J.3    Schweyen, R.J.4
  • 102
    • 77954104112 scopus 로고    scopus 로고
    • Genetic etiology of Parkinson disease associated with mutations in the SNCA, PARK2, PINK1, PARK7, and LRRK2 genes: A mutation update
    • Nuytemans K, Theuns J, Cruts M, and Van Broeckhoven C. Genetic etiology of Parkinson disease associated with mutations in the SNCA, PARK2, PINK1, PARK7, and LRRK2 genes: a mutation update. Hum Mutat 31: 763-780, 2010.
    • (2010) Hum Mutat , vol.31 , pp. 763-780
    • Nuytemans, K.1    Theuns, J.2    Cruts, M.3    Van Broeckhoven, C.4
  • 103
    • 0032945622 scopus 로고    scopus 로고
    • A novel adenovirus E1B19K-binding protein B5 inhibits apoptosis induced by Nip3 by forming a heterodimer through the C-terminal hydrophobic region
    • Ohi N, Tokunaga A, Tsunoda H, Nakano K, Haraguchi K, Oda K, Motoyama N, and Nakajima T. A novel adenovirus E1B19K-binding protein B5 inhibits apoptosis induced by Nip3 by forming a heterodimer through the C-terminal hydrophobic region. Cell Death Differ 6: 314-325, 1999.
    • (1999) Cell Death Differ , vol.6 , pp. 314-325
    • Ohi, N.1    Tokunaga, A.2    Tsunoda, H.3    Nakano, K.4    Haraguchi, K.5    Oda, K.6    Motoyama, N.7    Nakajima, T.8
  • 104
    • 67650246357 scopus 로고    scopus 로고
    • Mitochondria-anchored receptor Atg32 mediates degradation of mitochondria via selective autophagy
    • Okamoto K, Kondo-Okamoto N, and 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
  • 105
    • 84876335261 scopus 로고    scopus 로고
    • Mitophagy in neurodegeneration and aging
    • Palikaras K and Tavernarakis N. Mitophagy in neurodegeneration and aging. Front Genet 3: 297, 2012.
    • (2012) Front Genet , vol.3 , pp. 297
    • Palikaras, K.1    Tavernarakis, N.2
  • 106
    • 33644622570 scopus 로고    scopus 로고
    • HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption
    • Papandreou I, Cairns RA, Fontana L, Lim AL, and Denko NC. HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption. Cell Metab 3: 187-197, 2006.
    • (2006) Cell Metab , vol.3 , pp. 187-197
    • Papandreou, I.1    Cairns, R.A.2    Fontana, L.3    Lim, A.L.4    Denko, N.C.5
  • 110
    • 0030937718 scopus 로고    scopus 로고
    • Activation of hypoxia-inducible factor-1; definition of regulatory domains within the alpha subunit
    • Pugh CW, O'Rourke JF, Nagao M, Gleadle JM, and Ratcliffe PJ. Activation of hypoxia-inducible factor-1; definition of regulatory domains within the alpha subunit. J Biol Chem 272: 11205-11214, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 11205-11214
    • Pugh, C.W.1    O'Rourke, J.F.2    Nagao, M.3    Gleadle, J.M.4    Ratcliffe, P.J.5
  • 111
    • 77957683915 scopus 로고    scopus 로고
    • Bnip3-mediated mitochondrial autophagy is independent of the mitochondrial permeability transition pore
    • Quinsay MN, Thomas RL, Lee Y, and Gustafsson AB. Bnip3-mediated mitochondrial autophagy is independent of the mitochondrial permeability transition pore. Autophagy 6: 855-862, 2010.
    • (2010) Autophagy , vol.6 , pp. 855-862
    • Quinsay, M.N.1    Thomas, R.L.2    Lee, Y.3    Gustafsson, A.B.4
  • 112
    • 79959987510 scopus 로고    scopus 로고
    • Tubular network formation protects mitochondria from autophagosomal degradation during nutrient starvation
    • Rambold AS, Kostelecky B, Elia N, and Lippincott- Schwartz J. Tubular network formation protects mitochondria from autophagosomal degradation during nutrient starvation. Proc Natl Acad Sci U S A 108: 10190-10195, 2011.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 10190-10195
    • Rambold, A.S.1    Kostelecky, B.2    Elia, N.3    Lippincott- Schwartz, J.4
  • 113
    • 77955131007 scopus 로고    scopus 로고
    • Plasma membrane contributes to the formation of pre-autophagosomal structures
    • Ravikumar B, Moreau K, Jahreiss L, Puri C, and Rubinsztein DC. Plasma membrane contributes to the formation of pre-autophagosomal structures. Nat Cell Biol 12: 747-757, 2010.
    • (2010) Nat Cell Biol , vol.12 , pp. 747-757
    • Ravikumar, B.1    Moreau, K.2    Jahreiss, L.3    Puri, C.4    Rubinsztein, D.C.5
  • 114
    • 0033984094 scopus 로고    scopus 로고
    • BNIP3 heterodimerizes with Bcl-2/Bcl-X-L and induces cell death independent of a Bcl-2 homology 3 (BH3) domain at both mitochondrial and nonmitochondrial sites
    • Ray R, Chen G, Vande Velde C, Cizeau J, Park JH, Reed JC, Gietz RD, and Greenberg AH. BNIP3 heterodimerizes with Bcl-2/Bcl-X-L and induces cell death independent of a Bcl-2 homology 3 (BH3) domain at both mitochondrial and nonmitochondrial sites. J Biol Chem 275: 1439-1448, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 1439-1448
    • Ray, R.1    Chen, G.2    Vande Velde, C.3    Cizeau, J.4    Park, J.H.5    Reed, J.C.6    Gietz, R.D.7    Greenberg, A.H.8
  • 115
    • 33644606491 scopus 로고    scopus 로고
    • Tracker dyes to probe mitochondrial autophagy (mitophagy) in rat hepatocytes
    • Rodriguez-Enriquez S, Kim I, Currin RT, and Lemasters JJ. Tracker dyes to probe mitochondrial autophagy (mitophagy) in rat hepatocytes. Autophagy 2: 39-46, 2006.
    • (2006) Autophagy , vol.2 , pp. 39-46
    • Rodriguez-Enriquez, S.1    Kim, I.2    Currin, R.T.3    Lemasters, J.J.4
  • 116
    • 84892859905 scopus 로고    scopus 로고
    • Interactions between autophagy receptors and ubiquitin-like proteins form the molecular basis for selective autophagy
    • Rogov V, Dotsch V, Johansen T, and Kirkin V. Interactions between autophagy receptors and ubiquitin-like proteins form the molecular basis for selective autophagy. Mol Cell 53: 167-178, 2014.
    • (2014) Mol Cell , vol.53 , pp. 167-178
    • Rogov, V.1    Dotsch, V.2    Johansen, T.3    Kirkin, V.4
  • 120
    • 77951768486 scopus 로고    scopus 로고
    • Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids
    • Sancak Y, Bar-Peled L, Zoncu R, Markhard AL, Nada S, and Sabatini DM. Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids. Cell 141: 290-303, 2010.
    • (2010) Cell , vol.141 , pp. 290-303
    • Sancak, Y.1    Bar-Peled, L.2    Zoncu, R.3    Markhard, A.L.4    Nada, S.5    Sabatini, D.M.6
  • 126
    • 84856739946 scopus 로고    scopus 로고
    • Hypoxia-inducible factors in physiology and medicine
    • Semenza GL. Hypoxia-inducible factors in physiology and medicine. Cell 148: 399-408, 2012.
    • (2012) Cell , vol.148 , pp. 399-408
    • Semenza, G.L.1
  • 128
    • 79953211917 scopus 로고    scopus 로고
    • Nutrient starvation elicits an acute autophagic response mediated by Ulk1 dephosphorylation and its subsequent dissociation from AMPK
    • Shang LB, Chen S, Du FH, Li S, Zhao LP, and Wang XD. Nutrient starvation elicits an acute autophagic response mediated by Ulk1 dephosphorylation and its subsequent dissociation from AMPK. Proc Natl Acad Sci U S A 108: 4788-4793, 2011.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 4788-4793
    • Shang, L.B.1    Chen, S.2    Du, F.H.3    Li, S.4    Zhao, L.P.5    Wang, X.D.6
  • 129
    • 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, and Hattori N. PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of Parkin and regulates mitophagy. Sci Rep 2: 1002, 2012.
    • (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
  • 130
    • 84870013071 scopus 로고    scopus 로고
    • Voltage-dependent anion channels (VDACs) recruit Parkin to defective mitochondria to promote mitochondrial autophagy
    • Sun Y, Vashisht AA, Tchieu J, Wohlschlegel JA, and Dreier L. Voltage-dependent anion channels (VDACs) recruit Parkin to defective mitochondria to promote mitochondrial autophagy. J Biol Chem 287: 40652-40660, 2012.
    • (2012) J Biol Chem , vol.287 , pp. 40652-40660
    • Sun, Y.1    Vashisht, A.A.2    Tchieu, J.3    Wohlschlegel, J.A.4    Dreier, L.5
  • 132
    • 84876499607 scopus 로고    scopus 로고
    • Bif-1 haploinsufficiency promotes chromosomal instability and accelerates Myc-driven lymphomagenesis via suppression of mitophagy
    • Takahashi Y, Hori T, Cooper TK, Liao J, Desai N, Serfass JM, Young MM, Park S, Izu Y, and Wang HG. Bif-1 haploinsufficiency promotes chromosomal instability and accelerates Myc-driven lymphomagenesis via suppression of mitophagy. Blood 121: 1622-1632, 2013.
    • (2013) Blood , vol.121 , pp. 1622-1632
    • Takahashi, Y.1    Hori, T.2    Cooper, T.K.3    Liao, J.4    Desai, N.5    Serfass, J.M.6    Young, M.M.7    Park, S.8    Izu, Y.9    Wang, H.G.10
  • 134
    • 34247172582 scopus 로고    scopus 로고
    • Aup1p, a yeast mitochondrial protein phosphatase homolog, is required for efficient stationary phase mitophagy and cell survival
    • Tal R, Winter G, Ecker N, Klionsky DJ, and Abeliovich H. Aup1p, a yeast mitochondrial protein phosphatase homolog, is required for efficient stationary phase mitophagy and cell survival. J Biol Chem 282: 5617-5624, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 5617-5624
    • Tal, R.1    Winter, G.2    Ecker, N.3    Klionsky, D.J.4    Abeliovich, H.5
  • 140
    • 0029051439 scopus 로고
    • Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension
    • Wang GL, Jiang BH, Rue EA, and Semenza GL. Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension. Proc Natl Acad Sci U S A 92: 5510-5514, 1995.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 5510-5514
    • Wang, G.L.1    Jiang, B.H.2    Rue, E.A.3    Semenza, G.L.4
  • 141
    • 79953231682 scopus 로고    scopus 로고
    • Parkin ubiquitinates Drp1 for proteasome-dependent degradation: Implication of dysregulated mitochondrial dynamics in Parkinson disease
    • Wang H, Song P, Du L, Tian W, Yue W, Liu M, Li D, Wang B, Zhu Y, Cao C, Zhou J, and Chen Q. Parkin ubiquitinates Drp1 for proteasome-dependent degradation: implication of dysregulated mitochondrial dynamics in Parkinson disease. J Biol Chem 286: 11649-11658, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 11649-11658
    • Wang, H.1    Song, P.2    Du, L.3    Tian, W.4    Yue, W.5    Liu, M.6    Li, D.7    Wang, B.8    Zhu, Y.9    Cao, C.10    Zhou, J.11    Chen, Q.12
  • 143
    • 12444279265 scopus 로고
    • On the origin of cancer cells
    • Warburg O. On the origin of cancer cells. Science 123: 309-314, 1956.
    • (1956) Science , vol.123 , pp. 309-314
    • Warburg, O.1
  • 144
    • 64549112144 scopus 로고    scopus 로고
    • Pink1 forms a multiprotein complex with miro and milton, linking Pink1 function to mitochondrial trafficking
    • Weihofen A, Thomas KJ, Ostaszewski BL, Cookson MR, and Selkoe DJ. Pink1 forms a multiprotein complex with miro and milton, linking Pink1 function to mitochondrial trafficking. Biochemistry 48: 2045-2052, 2009.
    • (2009) Biochemistry , vol.48 , pp. 2045-2052
    • Weihofen, A.1    Thomas, K.J.2    Ostaszewski, B.L.3    Cookson, M.R.4    Selkoe, D.J.5
  • 145
    • 79957534572 scopus 로고    scopus 로고
    • Targeting hypoxia in cancer therapy
    • Wilson WR and Hay MP. Targeting hypoxia in cancer therapy. Nat Rev Cancer 11: 393-410, 2011.
    • (2011) Nat Rev Cancer , vol.11 , pp. 393-410
    • Wilson, W.R.1    Hay, M.P.2
  • 146
    • 84878256973 scopus 로고    scopus 로고
    • Metabolism: Putting energy into mitophagy
    • Wrighton KH. Metabolism: putting energy into mitophagy. Nat Rev Mol Cell Biol 14: 324, 2013.
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 324
    • Wrighton, K.H.1
  • 148
    • 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, Gehrke S, Imai Y, Huang Z, Ouyang Y, Wang JW, Yang L, Beal MF, Vogel H, and Lu B. Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of Drosophila Pink1 is rescued by Parkin. Proc Natl Acad Sci U S A 103: 10793-10798, 2006.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 10793-10798
    • Yang, Y.1    Gehrke, S.2    Imai, Y.3    Huang, Z.4    Ouyang, Y.5    Wang, J.W.6    Yang, L.7    Beal, M.F.8    Vogel, H.9    Lu, B.10
  • 149
    • 0032524656 scopus 로고    scopus 로고
    • Adenovirus E1B-19K/BCL-2 interacting protein BNIP3 contains a BH3 domain and a mitochondrial targeting sequence
    • Yasuda M, Theodorakis P, Subramanian T, and Chinnadurai G. Adenovirus E1B-19K/BCL-2 interacting protein BNIP3 contains a BH3 domain and a mitochondrial targeting sequence. J Biol Chem 273: 12415-12421, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 12415-12421
    • Yasuda, M.1    Theodorakis, P.2    Subramanian, T.3    Chinnadurai, G.4
  • 151
    • 71649112895 scopus 로고    scopus 로고
    • 3D tomography reveals connections between the phagophore and endoplasmic reticulum
    • Yla-Anttila P, Vihinen H, Jokita E, and Eskelinen EL. 3D tomography reveals connections between the phagophore and endoplasmic reticulum. Autophagy 5: 1180-1185, 2009.
    • (2009) Autophagy , vol.5 , pp. 1180-1185
    • Yla-Anttila, P.1    Vihinen, H.2    Jokita, E.3    Eskelinen, E.L.4
  • 152
    • 79957472437 scopus 로고    scopus 로고
    • Parkin mediates proteasome-dependent protein degradation and rupture of the outer mitochondrial membrane
    • Yoshii SR, Kishi C, Ishihara N, and 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
  • 154
    • 67549101188 scopus 로고    scopus 로고
    • Role of BNIP3 and NIX in cell death, autophagy, and mitophagy
    • Zhang J and Ney PA. Role of BNIP3 and NIX in cell death, autophagy, and mitophagy. Cell Death Differ 16: 939-946, 2009.
    • (2009) Cell Death Differ , vol.16 , pp. 939-946
    • Zhang, J.1    Ney, P.A.2
  • 155
    • 67650230871 scopus 로고    scopus 로고
    • Mitochondrial clearance is regulated by Atg7-dependent and -independent mechanisms during reticulocyte maturation
    • Zhang J, Randall MS, Loyd MR, Dorsey FC, Kundu M, Cleveland JL, and Ney PA. 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    Randall, M.S.2    Loyd, M.R.3    Dorsey, F.C.4    Kundu, M.5    Cleveland, J.L.6    Ney, P.A.7
  • 156
    • 73949124173 scopus 로고    scopus 로고
    • Adipose-specific deletion of autophagy-related gene 7 (atg7) in mice reveals a role in adipogenesis
    • Zhang Y, Goldman S, Baerga R, Zhao Y, Komatsu M, and Jin S. Adipose-specific deletion of autophagy-related gene 7 (atg7) in mice reveals a role in adipogenesis. Proc Natl Acad Sci U S A 106: 19860-19865, 2009.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 19860-19865
    • Zhang, Y.1    Goldman, S.2    Baerga, R.3    Zhao, Y.4    Komatsu, M.5    Jin, S.6
  • 160
    • 77950384477 scopus 로고    scopus 로고
    • Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin
    • Ziviani E, Tao RN, and Whitworth AJ. Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin. Proc Natl Acad Sci U S A 107: 5018-5023, 2010.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 5018-5023
    • Ziviani, E.1    Tao, R.N.2    Whitworth, A.J.3
  • 161
    • 80555143078 scopus 로고    scopus 로고
    • mTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H+-ATPase
    • Zoncu R, Bar-Peled L, Efeyan A, Wang SY, Sancak Y, and Sabatini DM. mTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H+-ATPase. Science 334: 678-683, 2011.
    • (2011) Science , vol.334 , pp. 678-683
    • Zoncu, R.1    Bar-Peled, L.2    Efeyan, A.3    Wang, S.Y.4    Sancak, Y.5    Sabatini, D.M.6


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