메뉴 건너뛰기




Volumn 116, Issue 1, 2015, Pages 167-182

The mitochondrial dynamism-mitophagy-cell death interactome: Multiple roles performed by members of a mitochondrial molecular ensemble

Author keywords

apoptosis; autophagy; mitochondria; mitochondrial dynamics

Indexed keywords

CALCIUM; MITOCHONDRIAL PROTEIN; MITOFUSIN 1; MITOFUSIN 2;

EID: 84920872756     PISSN: 00097330     EISSN: 15244571     Source Type: Journal    
DOI: 10.1161/CIRCRESAHA.116.303554     Document Type: Review
Times cited : (155)

References (112)
  • 1
    • 0023642480 scopus 로고
    • The unmasking of mitochondrial Eve
    • Lewin R. The unmasking of mitochondrial Eve. Science. 1987;238:24-26.
    • (1987) Science , vol.238 , pp. 24-26
    • Lewin, R.1
  • 2
    • 0033525788 scopus 로고    scopus 로고
    • Mitochondrial evolution
    • Gray MW, Burger G, Lang BF. Mitochondrial evolution. Science. 1999;283:1476-1481.
    • (1999) Science , vol.283 , pp. 1476-1481
    • Gray, M.W.1    Burger, G.2    Lang, B.F.3
  • 4
    • 1542373685 scopus 로고    scopus 로고
    • Transcriptional regulatory circuits controlling mitochondrial biogenesis and function
    • Kelly DP, Scarpulla RC. Transcriptional regulatory circuits controlling mitochondrial biogenesis and function. Genes Dev. 2004;18:357-368. doi: 10.1101/gad.1177604.
    • (2004) Genes Dev. , vol.18 , pp. 357-368
    • Kelly, D.P.1    Scarpulla, R.C.2
  • 5
    • 84897113087 scopus 로고    scopus 로고
    • Mitochondrial contagion induced by Parkin deficiency in Drosophila hearts and its containment by suppressing mitofusin
    • Bhandari P, Song M, Chen Y, Burelle Y, Dorn GW II. Mitochondrial contagion induced by Parkin deficiency in Drosophila hearts and its containment by suppressing mitofusin. Circ Res. 2014;114:257-265. doi: 10.1161/CIRCRESAHA.114.302734.
    • (2014) Circ Res. , vol.114 , pp. 257-265
    • Bhandari, P.1    Song, M.2    Chen, Y.3    Burelle, Y.4    Dorn, G.W.5
  • 6
    • 79960817081 scopus 로고    scopus 로고
    • Mitochondrial fusion and division
    • Hales KG. Mitochondrial fusion and division. Nat Educ. 2010;3:12.
    • (2010) Nat Educ. , vol.3 , pp. 12
    • Hales, K.G.1
  • 7
    • 84887321199 scopus 로고    scopus 로고
    • Mitochondrial fusion directs cardiomyocyte differentiation via calcineurin and Notch signaling
    • Kasahara A, Cipolat S, Chen Y, Dorn GW II, Scorrano L. Mitochondrial fusion directs cardiomyocyte differentiation via calcineurin and Notch signaling. Science. 2013;342:734-737. doi: 10.1126/science.1241359.
    • (2013) Science , vol.342 , pp. 734-737
    • Kasahara, A.1    Cipolat, S.2    Chen, Y.3    Dorn, G.W.4    Scorrano, L.5
  • 8
    • 84880679646 scopus 로고    scopus 로고
    • Building a fission machine-structural insights into dynamin assembly and activation
    • Chappie JS, Dyda F. Building a fission machine-structural insights into dynamin assembly and activation. J Cell Sci. 2013;126:2773-2784. doi: 10.1242/jcs.108845.
    • (2013) J Cell Sci. , vol.126 , pp. 2773-2784
    • Chappie, J.S.1    Dyda, F.2
  • 9
    • 33745758647 scopus 로고    scopus 로고
    • Molecular mechanism of mitochondrial membrane fusion
    • Griffin EE, Detmer SA, Chan DC. Molecular mechanism of mitochondrial membrane fusion. Biochim Biophys Acta. 2006;1763:482-489. doi: 10.1016/j.bbamcr.2006.02.003.
    • (2006) Biochim Biophys Acta. , vol.1763 , pp. 482-489
    • Griffin, E.E.1    Detmer, S.A.2    Chan, D.C.3
  • 11
    • 84894363564 scopus 로고    scopus 로고
    • A role for myosin II in mammalian mitochondrial fission
    • Korobova F, Gauvin TJ, Higgs HN. A role for myosin II in mammalian mitochondrial fission. Curr Biol. 2014;24:409-414. doi: 10.1016/j. cub.2013.12.032.
    • (2014) Curr Biol. , vol.24 , pp. 409-414
    • Korobova, F.1    Gauvin, T.J.2    Higgs, H.N.3
  • 12
    • 84872769447 scopus 로고    scopus 로고
    • An actin-dependent step in mitochondrial fission mediated by the ER-associated formin INF2
    • Korobova F, Ramabhadran V, Higgs HN. An actin-dependent step in mitochondrial fission mediated by the ER-associated formin INF2. Science. 2013;339:464-467. doi: 10.1126/science.1228360.
    • (2013) Science , vol.339 , pp. 464-467
    • Korobova, F.1    Ramabhadran, V.2    Higgs, H.N.3
  • 13
    • 3843075121 scopus 로고    scopus 로고
    • Structural basis of mitochondrial tethering by mitofusin complexes
    • Koshiba T, Detmer SA, Kaiser JT, Chen H, McCaffery JM, Chan DC. Structural basis of mitochondrial tethering by mitofusin complexes. Science. 2004;305:858-862. doi: 10.1126/science.1099793.
    • (2004) Science , vol.305 , pp. 858-862
    • Koshiba, T.1    Detmer, S.A.2    Kaiser, J.T.3    Chen, H.4    McCaffery, J.M.5    Chan, D.C.6
  • 14
    • 84878228268 scopus 로고    scopus 로고
    • Mitochondrial dynamism and cardiac fate-A personal perspective
    • Dorn GW II. Mitochondrial dynamism and cardiac fate-a personal perspective. Circ J. 2013;77:1370-1379.
    • (2013) Circ J. , vol.77 , pp. 1370-1379
    • Dorn, G.W.1
  • 16
    • 68149103297 scopus 로고    scopus 로고
    • Mitofusins and OPA1 mediate sequential steps in mitochondrial membrane fusion
    • Song Z, Ghochani M, McCaffery JM, Frey TG, Chan DC. Mitofusins and OPA1 mediate sequential steps in mitochondrial membrane fusion. Mol Biol Cell. 2009;20:3525-3532. doi: 10.1091/mbc.E09-03-0252.
    • (2009) Mol Biol Cell. , vol.20 , pp. 3525-3532
    • Song, Z.1    Ghochani, M.2    McCaffery, J.M.3    Frey, T.G.4    Chan, D.C.5
  • 18
    • 55749090654 scopus 로고    scopus 로고
    • The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila
    • Deng H, Dodson MW, Huang H, Guo M. The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila. Proc Natl Acad Sci U S A. 2008;105:14503-14508. doi: 10.1073/pnas.0803998105.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 14503-14508
    • Deng, H.1    Dodson, M.W.2    Huang, H.3    Guo, M.4
  • 19
    • 0037455575 scopus 로고    scopus 로고
    • Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development
    • Chen H, Detmer SA, Ewald AJ, Griffin EE, Fraser SE, Chan DC. Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development. J Cell Biol. 2003;160:189-200. doi: 10.1083/jcb.200211046.
    • (2003) J Cell Biol. , vol.160 , pp. 189-200
    • Chen, H.1    Detmer, S.A.2    Ewald, A.J.3    Griffin, E.E.4    Fraser, S.E.5    Chan, D.C.6
  • 20
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • de Brito OM, Scorrano L. Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature. 2008;456:605-610. doi: 10.1038/nature07534.
    • (2008) Nature , vol.456 , pp. 605-610
    • De Brito, O.M.1    Scorrano, L.2
  • 21
    • 22544451586 scopus 로고    scopus 로고
    • Disruption of fusion results in mitochondrial heterogeneity and dysfunction
    • Chen H, Chomyn A, Chan DC. Disruption of fusion results in mitochondrial heterogeneity and dysfunction. J Biol Chem. 2005;280:26185-26192. doi: 10.1074/jbc.M503062200.
    • (2005) J Biol Chem. , vol.280 , pp. 26185-26192
    • Chen, H.1    Chomyn, A.2    Chan, D.C.3
  • 22
    • 34547601410 scopus 로고    scopus 로고
    • Mitochondrial fusion protects against neurodegeneration in the cerebellum
    • Chen H, McCaffery JM, Chan DC. Mitochondrial fusion protects against neurodegeneration in the cerebellum. Cell. 2007;130:548-562. doi: 10.1016/j.cell.2007.06.026.
    • (2007) Cell. , vol.130 , pp. 548-562
    • Chen, H.1    McCaffery, J.M.2    Chan, D.C.3
  • 23
    • 77951737783 scopus 로고    scopus 로고
    • Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations
    • Chen H, Vermulst M, Wang YE, Chomyn A, Prolla TA, McCaffery JM, Chan DC. Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations. Cell. 2010;141:280-289. doi: 10.1016/j.cell.2010.02.026.
    • (2010) Cell. , vol.141 , pp. 280-289
    • Chen, H.1    Vermulst, M.2    Wang, Y.E.3    Chomyn, A.4    Prolla, T.A.5    McCaffery, J.M.6    Chan, D.C.7
  • 24
    • 84856109625 scopus 로고    scopus 로고
    • Mitochondrial fusion is essential for organelle function and cardiac homeostasis
    • Chen Y, Liu Y, Dorn GW II. Mitochondrial fusion is essential for organelle function and cardiac homeostasis. Circ Res. 2011;109:1327-1331. doi: 10.1161/CIRCRESAHA.111.258723.
    • (2011) Circ Res. , vol.109 , pp. 1327-1331
    • Chen, Y.1    Liu, Y.2    Dorn, G.W.3
  • 26
    • 85060472723 scopus 로고    scopus 로고
    • A brief history of: Velcro
    • June 15
    • Suddath C. A brief history of: Velcro. Time Magazine. June 15, 2010.
    • (2010) Time Magazine.
    • Suddath, C.1
  • 27
    • 77957284223 scopus 로고    scopus 로고
    • Two close, too close: Sarcoplasmic reticulummitochondrial crosstalk and cardiomyocyte fate
    • Dorn GW II, Scorrano L. Two close, too close: sarcoplasmic reticulummitochondrial crosstalk and cardiomyocyte fate. Circ Res. 2010;107:689-699. doi: 10.1161/CIRCRESAHA.110.225714.
    • (2010) Circ Res. , vol.107 , pp. 689-699
    • Dorn, G.W.1    Scorrano, L.2
  • 30
    • 84872680832 scopus 로고    scopus 로고
    • SR and mitochondria: Calcium cross-talk between kissing cousins
    • Dorn GW II, Maack C. SR and mitochondria: calcium cross-talk between kissing cousins. J Mol Cell Cardiol. 2013;55:42-49. doi: 10.1016/j. yjmcc.2012.07.015.
    • (2013) J Mol Cell Cardiol. , vol.55 , pp. 42-49
    • Dorn, G.W.1    Maack, C.2
  • 31
    • 84867722747 scopus 로고    scopus 로고
    • Physiological roles of the permeability transition pore
    • Brenner C, Moulin M. Physiological roles of the permeability transition pore. Circ Res. 2012;111:1237-1247. doi: 10.1161/CIRCRESAHA.112.265942.
    • (2012) Circ Res. , vol.111 , pp. 1237-1247
    • Brenner, C.1    Moulin, M.2
  • 32
    • 84864547810 scopus 로고    scopus 로고
    • Mitofusins and the mitochondrial permeability transition: The potential downside of mitochondrial fusion
    • Papanicolaou KN, Phillippo MM, Walsh K. Mitofusins and the mitochondrial permeability transition: the potential downside of mitochondrial fusion. Am J Physiol Heart Circ Physiol. 2012;303:H243-H255. doi: 10.1152/ajpheart.00185.2012.
    • (2012) Am J Physiol Heart Circ Physiol. , vol.303 , pp. H243-H255
    • Papanicolaou, K.N.1    Phillippo, M.M.2    Walsh, K.3
  • 33
    • 38349184844 scopus 로고    scopus 로고
    • Nix-mediated apoptosis links myocardial fibrosis, cardiac remodeling, and hypertrophy decompensation
    • Diwan A, Wansapura J, Syed FM, Matkovich SJ, Lorenz JN, Dorn GW II. Nix-mediated apoptosis links myocardial fibrosis, cardiac remodeling, and hypertrophy decompensation. Circulation. 2008;117:396-404. doi: 10.1161/CIRCULATIONAHA.107.727073.
    • (2008) Circulation , vol.117 , pp. 396-404
    • Diwan, A.1    Wansapura, J.2    Syed, F.M.3    Matkovich, S.J.4    Lorenz, J.N.5    Dorn, G.W.6
  • 37
    • 77952683069 scopus 로고    scopus 로고
    • Dual autonomous mitochondrial cell death pathways are activated by Nix/BNip3L and induce cardiomyopathy
    • Chen Y, Lewis W, Diwan A, Cheng EH, Matkovich SJ, Dorn GW II. Dual autonomous mitochondrial cell death pathways are activated by Nix/BNip3L and induce cardiomyopathy. Proc Natl Acad Sci U S A. 2010;107:9035-9042. doi: 10.1073/pnas.0914013107.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 9035-9042
    • Chen, Y.1    Lewis, W.2    Diwan, A.3    Cheng, E.H.4    Matkovich, S.J.5    Dorn, G.W.6
  • 39
    • 84879240043 scopus 로고    scopus 로고
    • Potential role of BNIP3 in cardiac remodeling, myocardial stiffness, and endoplasmic reticulum: Mitochondrial calcium homeostasis in diastolic and systolic heart failure
    • Chaanine AH, Gordon RE, Kohlbrenner E, Benard L, Jeong D, Hajjar RJ. Potential role of BNIP3 in cardiac remodeling, myocardial stiffness, and endoplasmic reticulum: mitochondrial calcium homeostasis in diastolic and systolic heart failure. Circ Heart Fail. 2013;6:572-583. doi: 10.1161/CIRCHEARTFAILURE.112.000200.
    • (2013) Circ Heart Fail. , vol.6 , pp. 572-583
    • Chaanine, A.H.1    Gordon, R.E.2    Kohlbrenner, E.3    Benard, L.4    Jeong, D.5    Hajjar, R.J.6
  • 40
    • 70349668309 scopus 로고    scopus 로고
    • BNIP3 mediates cell death by different pathways following localization to endoplasmic reticulum and mitochondrion
    • Zhang L, Li L, Liu H, Borowitz JL, Isom GE. BNIP3 mediates cell death by different pathways following localization to endoplasmic reticulum and mitochondrion. FASEB J. 2009;23:3405-3414. doi: 10.1096/fj.08-124354.
    • (2009) FASEB J. , vol.23 , pp. 3405-3414
    • Zhang, L.1    Li, L.2    Liu, H.3    Borowitz, J.L.4    Isom, G.E.5
  • 42
    • 33747586139 scopus 로고    scopus 로고
    • Mitochondrial buffering of calcium in the heart: Potential mechanism for linking cyclic energetic cost with energy supply?
    • Sullivan PG, Balke CW, Esser KA. Mitochondrial buffering of calcium in the heart: potential mechanism for linking cyclic energetic cost with energy supply? Circ Res. 2006;99:109-110. doi: 10.1161/01. RES.0000234949.61052.9f.
    • (2006) Circ Res. , vol.99 , pp. 109-110
    • Sullivan, P.G.1    Balke, C.W.2    Esser, K.A.3
  • 43
    • 0033835494 scopus 로고    scopus 로고
    • Serrate and Notch specify cell fates in the heart field by suppressing cardiomyogenesis
    • Rones MS, McLaughlin KA, Raffin M, Mercola M. Serrate and Notch specify cell fates in the heart field by suppressing cardiomyogenesis. Development. 2000;127:3865-3876.
    • (2000) Development , vol.127 , pp. 3865-3876
    • Rones, M.S.1    McLaughlin, K.A.2    Raffin, M.3    Mercola, M.4
  • 44
    • 33746517512 scopus 로고    scopus 로고
    • Induction of cardiogenesis in embryonic stem cells via downregulation of Notch1 signaling
    • Nemir M, Croquelois A, Pedrazzini T, Radtke F. Induction of cardiogenesis in embryonic stem cells via downregulation of Notch1 signaling. Circ Res. 2006;98:1471-1478. doi: 10.1161/01.RES.0000226497.52052.2a.
    • (2006) Circ Res. , vol.98 , pp. 1471-1478
    • Nemir, M.1    Croquelois, A.2    Pedrazzini, T.3    Radtke, F.4
  • 45
    • 84876531457 scopus 로고    scopus 로고
    • PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria
    • Chen Y, Dorn GW II. PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria. Science. 2013;340:471-475. doi: 10.1126/science.1231031.
    • (2013) Science , vol.340 , pp. 471-475
    • Chen, Y.1    Dorn, G.W.2
  • 46
    • 80054787664 scopus 로고    scopus 로고
    • What genetics tells us about the causes and mechanisms of Parkinson's disease
    • Corti O, Lesage S, Brice A. What genetics tells us about the causes and mechanisms of Parkinson's disease. Physiol Rev. 2011;91:1161-1218. doi: 10.1152/physrev.00022.2010.
    • (2011) Physiol Rev. , vol.91 , pp. 1161-1218
    • Corti, O.1    Lesage, S.2    Brice, A.3
  • 47
    • 66949152096 scopus 로고    scopus 로고
    • Parkinson's disease
    • Lees AJ, Hardy J, Revesz T. Parkinson's disease. Lancet. 2009;373:2055-2066. doi: 10.1016/S0140-6736(09)60492-X.
    • (2009) Lancet. , vol.373 , pp. 2055-2066
    • Lees, A.J.1    Hardy, J.2    Revesz, T.3
  • 49
    • 67649399288 scopus 로고    scopus 로고
    • Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission
    • Dagda RK, Cherra SJ III, Kulich SM, Tandon A, Park D, Chu CT. Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission. J Biol Chem. 2009;284:13843-13855. doi: 10.1074/jbc.M808515200.
    • (2009) J Biol Chem. , vol.284 , pp. 13843-13855
    • Dagda, R.K.1    Cherra, S.J.2    Kulich, S.M.3    Tandon, A.4    Park, D.5    Chu, C.T.6
  • 50
    • 0016772917 scopus 로고
    • Ultrastructure of skeletal muscle in patients with Parkinson's disease and upper motor lesions
    • Ahlqvist G, Landin S, Wroblewski R. Ultrastructure of skeletal muscle in patients with Parkinson's disease and upper motor lesions. Lab Invest. 1975;32:673-679.
    • (1975) Lab Invest. , vol.32 , pp. 673-679
    • Ahlqvist, G.1    Landin, S.2    Wroblewski, R.3
  • 51
    • 79958172986 scopus 로고    scopus 로고
    • Preconditioning involves selective mitophagy mediated by Parkin and p62/SQSTM1
    • Huang C, Andres AM, Ratliff EP, Hernandez G, Lee P, Gottlieb RA. Preconditioning involves selective mitophagy mediated by Parkin and p62/SQSTM1. PLoS One. 2011;6:e20975. doi: 10.1371/journal. pone.0020975.
    • (2011) PLoS One. , vol.6 , pp. e20975
    • Huang, C.1    Andres, A.M.2    Ratliff, E.P.3    Hernandez, G.4    Lee, P.5    Gottlieb, R.A.6
  • 53
    • 84901751574 scopus 로고    scopus 로고
    • Ubiquitin is phosphorylated by PINK1 to activate parkin
    • Koyano F, Okatsu K, Kosako H, et al. Ubiquitin is phosphorylated by PINK1 to activate parkin. Nature. 2014;510:162-166. doi: 10.1038/nature13392.
    • (2014) Nature , vol.510 , pp. 162-166
    • Koyano, F.1    Okatsu, K.2    Kosako, H.3
  • 54
    • 84876296881 scopus 로고    scopus 로고
    • Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization
    • Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW. Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization. Nature. 2013;496:372-376. doi: 10.1038/nature12043.
    • (2013) Nature , vol.496 , pp. 372-376
    • Sarraf, S.A.1    Raman, M.2    Guarani-Pereira, V.3    Sowa, M.E.4    Huttlin, E.L.5    Gygi, S.P.6    Harper, J.W.7
  • 56
    • 75949098487 scopus 로고    scopus 로고
    • PINK1-dependent recruitment of Parkin to mitochondria in mitophagy
    • Vives-Bauza C, Zhou C, Huang Y, et al. PINK1-dependent recruitment of Parkin to mitochondria in mitophagy. Proc Natl Acad Sci U S A. 2010;107:378-383. doi: 10.1073/pnas.0911187107.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 378-383
    • Vives-Bauza, C.1    Zhou, C.2    Huang, Y.3
  • 58
    • 78649685455 scopus 로고    scopus 로고
    • Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL
    • Jin SM, Lazarou M, Wang C, Kane LA, Narendra DP, Youle RJ. Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL. J Cell Biol. 2010;191:933-942. doi: 10.1083/jcb.201008084.
    • (2010) J 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
  • 59
    • 79959344616 scopus 로고    scopus 로고
    • PTEN-inducible kinase 1 (PINK1)/Park6 is indispensable for normal heart function
    • Billia F, Hauck L, Konecny F, Rao V, Shen J, Mak TW. PTEN-inducible kinase 1 (PINK1)/Park6 is indispensable for normal heart function. Proc Natl Acad Sci U S A. 2011;108:9572-9577. doi: 10.1073/pnas.1106291108.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 9572-9577
    • Billia, F.1    Hauck, L.2    Konecny, F.3    Rao, V.4    Shen, J.5    Mak, T.W.6
  • 61
    • 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. 2012;2:1002. doi: 10.1038/srep01002.
    • (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
  • 64
    • 84868127674 scopus 로고    scopus 로고
    • Loss of Mfn2 results in progressive, retrograde degeneration of dopaminergic neurons in the nigrostriatal circuit
    • Pham AH, Meng S, Chu QN, Chan DC. Loss of Mfn2 results in progressive, retrograde degeneration of dopaminergic neurons in the nigrostriatal circuit. Hum Mol Genet. 2012;21:4817-4826. doi: 10.1093/hmg/dds311.
    • (2012) Hum Mol Genet. , vol.21 , pp. 4817-4826
    • Pham, A.H.1    Meng, S.2    Chu, Q.N.3    Chan, D.C.4
  • 67
    • 84878118233 scopus 로고    scopus 로고
    • Parkin overexpression during aging reduces proteotoxicity, alters mitochondrial dynamics, and extends lifespan
    • Rana A, Rera M, Walker DW. Parkin overexpression during aging reduces proteotoxicity, alters mitochondrial dynamics, and extends lifespan. Proc Natl Acad Sci U S A. 2013;110:8638-8643. doi: 10.1073/pnas.1216197110.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 8638-8643
    • Rana, A.1    Rera, M.2    Walker, D.W.3
  • 68
    • 84871453443 scopus 로고    scopus 로고
    • Parkin induces apoptotic cell death in TNF-α-treated cervical cancer cells
    • Lee K, Lee MH, Kang YW, Rhee KJ, Kim TU, Kim YS. Parkin induces apoptotic cell death in TNF-α-treated cervical cancer cells. BMB Rep. 2012;45:526-531.
    • (2012) BMB Rep. , vol.45 , pp. 526-531
    • Lee, K.1    Lee, M.H.2    Kang, Y.W.3    Rhee, K.J.4    Kim, T.U.5    Kim, Y.S.6
  • 69
    • 84862295360 scopus 로고    scopus 로고
    • Guidelines for the use and interpretation of assays for monitoring autophagy
    • Klionsky DJ, Abdalla FC, Abeliovich H, et al. Guidelines for the use and interpretation of assays for monitoring autophagy. Autophagy. 2012;8:445-544.
    • (2012) Autophagy. , vol.8 , pp. 445-544
    • Klionsky, D.J.1    Abdalla, F.C.2    Abeliovich, H.3
  • 70
    • 33947401472 scopus 로고    scopus 로고
    • Autophagosome-lysosome fusion depends on the pH in acidic compartments in CHO cells
    • Kawai A, Uchiyama H, Takano S, Nakamura N, Ohkuma S. Autophagosome-lysosome fusion depends on the pH in acidic compartments in CHO cells. Autophagy. 2007;3:154-157.
    • (2007) Autophagy. , vol.3 , pp. 154-157
    • Kawai, A.1    Uchiyama, H.2    Takano, S.3    Nakamura, N.4    Ohkuma, S.5
  • 73
    • 84894165975 scopus 로고    scopus 로고
    • Cardiac mitochondria and reactive oxygen species generation
    • Chen YR, Zweier JL. Cardiac mitochondria and reactive oxygen species generation. Circ Res. 2014;114:524-537. doi: 10.1161/CIRCRESAHA.114.300559.
    • (2014) Circ Res. , vol.114 , pp. 524-537
    • Chen, Y.R.1    Zweier, J.L.2
  • 74
    • 84860196585 scopus 로고    scopus 로고
    • Cardiac aging: From molecular mechanisms to significance in human health and disease
    • Dai DF, Chen T, Johnson SC, Szeto H, Rabinovitch PS. Cardiac aging: from molecular mechanisms to significance in human health and disease. Antioxid Redox Signal. 2012;16:1492-1526. doi: 10.1089/ars.2011.4179.
    • (2012) Antioxid Redox Signal. , vol.16 , pp. 1492-1526
    • Dai, D.F.1    Chen, T.2    Johnson, S.C.3    Szeto, H.4    Rabinovitch, P.S.5
  • 75
    • 0038411479 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
    • Salmeen A, Andersen JN, Myers MP, Meng TC, Hinks JA, Tonks NK, Barford D. Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate. Nature. 2003;423:769-773. doi: 10.1038/nature01680.
    • (2003) Nature , vol.423 , pp. 769-773
    • Salmeen, A.1    Andersen, J.N.2    Myers, M.P.3    Meng, T.C.4    Hinks, J.A.5    Tonks, N.K.6    Barford, D.7
  • 76
    • 84904734344 scopus 로고    scopus 로고
    • Super-suppression of mitochondrial reactive oxygen species signaling impairs compensatory autophagy in primary mitophagic cardiomyopathy
    • Song M, Chen Y, Gong G, Murphy E, Rabinovitch PS, Dorn GW II. Super-suppression of mitochondrial reactive oxygen species signaling impairs compensatory autophagy in primary mitophagic cardiomyopathy. Circ Res. 2014;115:348-353. doi: 10.1161/CIRCRESAHA.115.304384.
    • (2014) Circ Res. , vol.115 , pp. 348-353
    • Song, M.1    Chen, Y.2    Gong, G.3    Murphy, E.4    Rabinovitch, P.S.5    Dorn, G.W.6
  • 81
    • 77955514158 scopus 로고    scopus 로고
    • Mitochondrial pruning by Nix and BNip3: An essential function for cardiac-expressed death factors
    • Dorn GW II. Mitochondrial pruning by Nix and BNip3: an essential function for cardiac-expressed death factors. J Cardiovasc Transl Res. 2010;3:374-383. doi: 10.1007/s12265-010-9174-x.
    • (2010) J Cardiovasc Transl Res. , vol.3 , pp. 374-383
    • Dorn, G.W.1
  • 83
    • 77953122645 scopus 로고    scopus 로고
    • LC3 and GATE-16/GABARAP subfamilies are both essential yet act differently in autophagosome biogenesis
    • Weidberg H, Shvets E, Shpilka T, Shimron F, Shinder V, Elazar Z. LC3 and GATE-16/GABARAP subfamilies are both essential yet act differently in autophagosome biogenesis. EMBO J. 2010;29:1792-1802. doi: 10.1038/emboj.2010.74.
    • (2010) EMBO J. , vol.29 , pp. 1792-1802
    • Weidberg, H.1    Shvets, E.2    Shpilka, T.3    Shimron, F.4    Shinder, V.5    Elazar, Z.6
  • 84
    • 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 II, 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. 2010;285:27879-27890. doi: 10.1074/jbc.M110.119537.
    • (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
  • 90
    • 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, Gustafsson ÅB. Microtubule-associated protein 1 light chain 3 (LC3) interacts with Bnip3 protein to selectively remove endoplasmic reticulum and mitochondria via autophagy. J Biol Chem. 2012;287:19094-19104. doi: 10.1074/jbc. M111.322933.
    • (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 Å., B.6
  • 93
    • 84885825015 scopus 로고    scopus 로고
    • Attenuation of doxorubicin-induced cardiotoxicity by mdivi-1: A mitochondrial division/mitophagy inhibitor
    • Gharanei M, Hussain A, Janneh O, Maddock H. Attenuation of doxorubicin-induced cardiotoxicity by mdivi-1: a mitochondrial division/mitophagy inhibitor. PLoS One. 2013;8:e77713. doi: 10.1371/journal. pone.0077713.
    • (2013) PLoS One. , vol.8 , pp. e77713
    • Gharanei, M.1    Hussain, A.2    Janneh, O.3    Maddock, H.4
  • 94
    • 84858970970 scopus 로고    scopus 로고
    • Mitochondrial division/mitophagy inhibitor (Mdivi) ameliorates pressure overload induced heart failure
    • Givvimani S, Munjal C, Tyagi N, Sen U, Metreveli N, Tyagi SC. Mitochondrial division/mitophagy inhibitor (Mdivi) ameliorates pressure overload induced heart failure. PLoS One. 2012;7:e32388. doi: 10.1371/journal.pone.0032388.
    • (2012) PLoS One. , vol.7 , pp. e32388
    • Givvimani, S.1    Munjal, C.2    Tyagi, N.3    Sen, U.4    Metreveli, N.5    Tyagi, S.C.6
  • 95
    • 77952236126 scopus 로고    scopus 로고
    • Inhibiting mitochondrial fission protects the heart against ischemia/reperfusion injury
    • Ong SB, Subrayan S, Lim SY, Yellon DM, Davidson SM, Hausenloy DJ. Inhibiting mitochondrial fission protects the heart against ischemia/reperfusion injury. Circulation. 2010;121:2012-2022. doi: 10.1161/CIRCULATIONAHA.109.906610.
    • (2010) Circulation , vol.121 , pp. 2012-2022
    • Ong, S.B.1    Subrayan, S.2    Lim, S.Y.3    Yellon, D.M.4    Davidson, S.M.5    Hausenloy, D.J.6
  • 96
    • 84894535372 scopus 로고    scopus 로고
    • Dynamin-related protein 1 (Drp1)-mediated diastolic dysfunction in myocardial ischemia-reperfusion injury: Therapeutic benefits of Drp1 inhibition to reduce mitochondrial fission
    • Sharp WW, Fang YH, Han M, Zhang HJ, Hong Z, Banathy A, Morrow E, Ryan JJ, Archer SL. Dynamin-related protein 1 (Drp1)-mediated diastolic dysfunction in myocardial ischemia-reperfusion injury: therapeutic benefits of Drp1 inhibition to reduce mitochondrial fission. FASEB J. 2014;28:316-326. doi: 10.1096/fj.12-226225.
    • (2014) FASEB J. , vol.28 , pp. 316-326
    • Sharp, W.W.1    Fang, Y.H.2    Han, M.3    Zhang, H.J.4    Hong, Z.5    Banathy, A.6    Morrow, E.7    Ryan, J.J.8    Archer, S.L.9
  • 97
    • 84890317515 scopus 로고    scopus 로고
    • Acute inhibition of excessive mitochondrial fission after myocardial infarction prevents long-term cardiac dysfunction
    • Disatnik MH, Ferreira JC, Campos JC, Gomes KS, Dourado PM, Qi X, Mochly-Rosen D. Acute inhibition of excessive mitochondrial fission after myocardial infarction prevents long-term cardiac dysfunction. J Am Heart Assoc. 2013;2:e000461. doi: 10.1161/JAHA.113.000461.
    • (2013) J Am Heart Assoc. , vol.2 , pp. e000461
    • Disatnik, M.H.1    Ferreira, J.C.2    Campos, J.C.3    Gomes, K.S.4    Dourado, P.M.5    Qi, X.6    Mochly-Rosen, D.7
  • 98
    • 34248182897 scopus 로고    scopus 로고
    • Bax/Bak promote sumoylation of DRP1 and its stable association with mitochondria during apoptotic cell death
    • Wasiak S, Zunino R, McBride HM. Bax/Bak promote sumoylation of DRP1 and its stable association with mitochondria during apoptotic cell death. J Cell Biol. 2007;177:439-450. doi: 10.1083/jcb.200610042.
    • (2007) J Cell Biol. , vol.177 , pp. 439-450
    • Wasiak, S.1    Zunino, R.2    McBride, H.M.3
  • 103
    • 15844407874 scopus 로고    scopus 로고
    • Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death
    • Nakagawa T, Shimizu S, Watanabe T, Yamaguchi O, Otsu K, Yamagata H, Inohara H, Kubo T, Tsujimoto Y. Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. Nature. 2005;434:652-658. doi: 10.1038/nature03317.
    • (2005) Nature , vol.434 , pp. 652-658
    • Nakagawa, T.1    Shimizu, S.2    Watanabe, T.3    Yamaguchi, O.4    Otsu, K.5    Yamagata, H.6    Inohara, H.7    Kubo, T.8    Tsujimoto, Y.9
  • 106
    • 4944222095 scopus 로고    scopus 로고
    • Drp-1-dependent division of the mitochondrial network blocks intraorganellar Ca2+ waves and protects against Ca2+-mediated apoptosis
    • Szabadkai G, Simoni AM, Chami M, Wieckowski MR, Youle RJ, Rizzuto R. Drp-1-dependent division of the mitochondrial network blocks intraorganellar Ca2+ waves and protects against Ca2+-mediated apoptosis. Mol Cell. 2004;16:59-68. doi: 10.1016/j.molcel.2004.09.026.
    • (2004) Mol Cell. , vol.16 , pp. 59-68
    • Szabadkai, G.1    Simoni, A.M.2    Chami, M.3    Wieckowski, M.R.4    Youle, R.J.5    Rizzuto, R.6
  • 107
    • 84859962717 scopus 로고    scopus 로고
    • The ubiquitin E3 ligase parkin regulates the proapoptotic function of Bax
    • Johnson BN, Berger AK, Cortese GP, Lavoie MJ. The ubiquitin E3 ligase parkin regulates the proapoptotic function of Bax. Proc Natl Acad Sci U S A. 2012;109:6283-6288. doi: 10.1073/pnas.1113248109.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 6283-6288
    • Johnson, B.N.1    Berger, A.K.2    Cortese, G.P.3    Lavoie, M.J.4
  • 109
    • 0036236634 scopus 로고    scopus 로고
    • Programmed death phenomena: From organelle to organism
    • Skulachev VP. Programmed death phenomena: from organelle to organism. Ann N Y Acad Sci. 2002;959:214-237.
    • (2002) Ann N y Acad Sci. , vol.959 , pp. 214-237
    • Skulachev, V.P.1
  • 110
    • 27644575235 scopus 로고    scopus 로고
    • Macroautophagy versus mitochondrial autophagy: A question of fate?
    • Kundu M, Thompson CB. Macroautophagy versus mitochondrial autophagy: a question of fate? Cell Death Differ. 2005;12 (suppl 2):1484-1489. doi: 10.1038/sj.cdd.4401780.
    • (2005) Cell Death Differ. , vol.12 , pp. 1484-1489
    • Kundu, M.1    Thompson, C.B.2
  • 112
    • 77955398958 scopus 로고    scopus 로고
    • Parkin overexpression selects against a deleterious mtDNA mutation in heteroplasmic cybrid cells
    • Suen DF, Narendra DP, Tanaka A, Manfredi G, Youle RJ. Parkin overexpression selects against a deleterious mtDNA mutation in heteroplasmic cybrid cells. Proc Natl Acad Sci U S A. 2010;107:11835-11840. doi: 10.1073/pnas.0914569107.
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.