메뉴 건너뛰기




Volumn 23, Issue 1, 2016, Pages 89-98

NF-κB pathway controls mitochondrial dynamics

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONIN 60; I KAPPA B KINASE BETA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; OPTIC ATROPHY 1 PROTEIN; PARKIN; PROTEIN; PROTEIN BAX; UNCLASSIFIED DRUG; GUANOSINE TRIPHOSPHATASE; I KAPPA B KINASE; NEMO PROTEIN, MOUSE; OPA1 PROTEIN (GTPASE), MOUSE; SIGNAL PEPTIDE; UBIQUITIN PROTEIN LIGASE;

EID: 84949533451     PISSN: 13509047     EISSN: 14765403     Source Type: Journal    
DOI: 10.1038/cdd.2015.42     Document Type: Article
Times cited : (67)

References (31)
  • 1
    • 67650243261 scopus 로고    scopus 로고
    • Parkin-induced mitophagy in the pathogenesis of Parkinson disease
    • Narendra D, Tanaka A, Suen DF, Youle RJ. Parkin-induced mitophagy in the pathogenesis of Parkinson disease. Autophagy 2009; 5: 706-708.
    • (2009) Autophagy , vol.5 , pp. 706-708
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 2
    • 73449111577 scopus 로고    scopus 로고
    • Mitochondrial autophagy as a compensatory response to PINK1 deficiency
    • Cherra 3rd SJ , Dagda RK, Tandon A, Chu CT. Mitochondrial autophagy as a compensatory response to PINK1 deficiency. Autophagy 2009; 5: 1213-1214.
    • (2009) Autophagy , vol.5 , pp. 1213-1214
    • Cherra, S.J.1    Dagda, R.K.2    Tandon, A.3    Chu, C.T.4
  • 4
    • 77951181836 scopus 로고    scopus 로고
    • PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy
    • Matsuda N, Sato S, Shiba K, Okatsu K, Saisho K, Gautier CA et al. PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy. J Cell Biol 2010; 189: 211-221.
    • (2011) J Cell Biol , vol.189 , pp. 211-221
    • Matsuda, N.1    Sato, S.2    Shiba, K.3    Okatsu, K.4    Saisho, K.5    Gautier, C.A.6
  • 5
    • 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.
    • (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
  • 6
    • 78650729600 scopus 로고    scopus 로고
    • Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin
    • Tanaka A, Cleland MM, Xu S, Narendra DP, Suen DF, Karbowski M et al. Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin. J Cell Biol 2010; 191: 1367-1380.
    • (2011) J 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
  • 7
    • 79960493052 scopus 로고    scopus 로고
    • Parkin promotes the ubiquitination and degradation of the mitochondrial fusion factor mitofusin 1
    • Glauser L, Sonnay S, Stafa K, Moore DJ. Parkin promotes the ubiquitination and degradation of the mitochondrial fusion factor mitofusin 1. J Neurochem 2011; 118: 636-645.
    • (2011) J Neurochem , vol.118 , pp. 636-645
    • Glauser, L.1    Sonnay, S.2    Stafa, K.3    Moore, D.J.4
  • 8
    • 79551548511 scopus 로고    scopus 로고
    • PINK1-parkin-dependent mitophagy involves ubiquitination of mitofusins 1 and 2: Implications for Parkinson disease pathogenesis
    • Gegg ME, Schapira AH. PINK1-parkin-dependent mitophagy involves ubiquitination of mitofusins 1 and 2: implications for Parkinson disease pathogenesis. Autophagy 2011; 7: 243-245.
    • (2011) Autophagy , vol.7 , pp. 243-245
    • Gegg, M.E.1    Schapira, A.H.2
  • 10
    • 84872860661 scopus 로고    scopus 로고
    • Mitochondrial quality control turns out to be the principal suspect in parkin and PINK1-related autosomal recessive Parkinson's disease
    • Corti O, Brice A. Mitochondrial quality control turns out to be the principal suspect in parkin and PINK1-related autosomal recessive Parkinson's disease. Curr Opin Neurobiol 2013; 23: 100-108.
    • (2013) Curr Opin Neurobiol , vol.23 , pp. 100-108
    • Corti, O.1    Brice, A.2
  • 11
    • 33847191686 scopus 로고    scopus 로고
    • Parkin mediates neuroprotection through activation of IkappaB kinase/nuclear factor-kappaB signaling
    • Henn IH, Bouman L, Schlehe JS, Schlierf A, Schramm JE, Wegener E et al. Parkin mediates neuroprotection through activation of IkappaB kinase/nuclear factor-kappaB signaling. J Neurosci 2007; 27: 1868-1878.
    • (2007) J Neurosci , vol.27 , pp. 1868-1878
    • Henn, I.H.1    Bouman, L.2    Schlehe, J.S.3    Schlierf, A.4    Schramm, J.E.5    Wegener, E.6
  • 12
    • 77949478474 scopus 로고    scopus 로고
    • Phosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NF-kappaB signaling
    • Sha D, Chin LS, Li L. Phosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NF-kappaB signaling. Hum Mol Genet 2010; 19: 352-363.
    • (2011) Hum Mol Genet , vol.19 , pp. 352-363
    • Sha, D.1    Chin, L.S.2    Li, L.3
  • 14
    • 77957252647 scopus 로고    scopus 로고
    • The IKK complex, a central regulator of NF-kappaB activation
    • Israel A. The IKK complex, a central regulator of NF-kappaB activation. Cold Spring Harb Perspect Biol 2010; 2: a000158.
    • (2011) Cold Spring Harb Perspect Biol , vol.2 , pp. a000158
    • Israel, A.1
  • 15
    • 33745685054 scopus 로고    scopus 로고
    • Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling
    • Cipolat S, Rudka T, Hartmann D, Costa V, Serneels L, Craessaerts K et al. Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling. Cell 2006; 126: 163-175.
    • (2006) Cell , vol.126 , pp. 163-175
    • Cipolat, S.1    Rudka, T.2    Hartmann, D.3    Costa, V.4    Serneels, L.5    Craessaerts, K.6
  • 18
    • 0037424239 scopus 로고    scopus 로고
    • Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis
    • Olichon A, Baricault L, Gas N, Guillou E, Valette A, Belenguer P et al. Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis. J Biol Chem 2003; 278: 7743-7746.
    • (2003) J Biol Chem , vol.278 , pp. 7743-7746
    • Olichon, A.1    Baricault, L.2    Gas, N.3    Guillou, E.4    Valette, A.5    Belenguer, P.6
  • 19
    • 27444446030 scopus 로고    scopus 로고
    • Release of OPA1 during apoptosis participates in the rapid and complete release of cytochrome c and subsequent mitochondrial fragmentation
    • Arnoult D, Grodet A, Lee YJ, Estaquier J, Blackstone C. Release of OPA1 during apoptosis participates in the rapid and complete release of cytochrome c and subsequent mitochondrial fragmentation. J Biol Chem 2005; 280: 35742-35750.
    • (2005) J Biol Chem , vol.280 , pp. 35742-35750
    • Arnoult, D.1    Grodet, A.2    Lee, Y.J.3    Estaquier, J.4    Blackstone, C.5
  • 20
    • 34548349869 scopus 로고    scopus 로고
    • OPA1 processing reconstituted in yeast depends on the subunit composition of the m-AAA protease in mitochondria
    • Duvezin-Caubet S, Koppen M, Wagener J, Zick M, Israel L, Bernacchia A et al. OPA1 processing reconstituted in yeast depends on the subunit composition of the m-AAA protease in mitochondria. Mol Biol Cell 2007; 18: 3582-3590.
    • (2007) Mol Biol Cell , vol.18 , pp. 3582-3590
    • Duvezin-Caubet, S.1    Koppen, M.2    Wagener, J.3    Zick, M.4    Israel, L.5    Bernacchia, A.6
  • 22
  • 23
    • 69249096578 scopus 로고    scopus 로고
    • Loss of parkin or PINK1 function increases Drp1-dependent mitochondrial fragmentation
    • Lutz AK, Exner N, Fett ME, Schlehe JS, Kloos K, Lämmermann K et al. Loss of parkin or PINK1 function increases Drp1-dependent mitochondrial fragmentation. J Biol Chem 2009; 284: 22938-22951.
    • (2009) J Biol Chem , vol.284 , pp. 22938-22951
    • Lutz, A.K.1    Exner, N.2    Fett, M.E.3    Schlehe, J.S.4    Kloos, K.5    Lämmermann, K.6
  • 24
    • 77956095537 scopus 로고    scopus 로고
    • Mitochondria and cell death: Outer membrane permeabilization and beyond
    • Tait SW, Green DR. Mitochondria and cell death: outer membrane permeabilization and beyond. Nat Rev Mol Cell Biol 2010; 11: 621-632.
    • (2011) Nat Rev Mol Cell Biol , vol.11 , pp. 621-632
    • Tait, S.W.1    Green, D.R.2
  • 25
    • 0035957653 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK: A requisite gateway to mitochondrial dysfunction and death
    • Wei MC, Zong WX, Cheng EH, Lindsten T, Panoutsakopoulou V, Ross AJ et al. Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death. Science 2001; 292: 727-730.
    • (2001) Science , vol.292 , pp. 727-730
    • Wei, M.C.1    Zong, W.X.2    Cheng, E.H.3    Lindsten, T.4    Panoutsakopoulou, V.5    Ross, A.J.6
  • 26
    • 0037338634 scopus 로고    scopus 로고
    • Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death
    • Darios F, Corti O, Lücking CB, Hampe C, Muriel MP, Abbas N et al. Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death. Hum Mol Genet 2003; 12: 517-526.
    • (2003) Hum Mol Genet , vol.12 , pp. 517-526
    • Darios, F.1    Corti, O.2    Lücking, C.B.3    Hampe, C.4    Muriel, M.P.5    Abbas, N.6
  • 27
  • 28
    • 0037193473 scopus 로고    scopus 로고
    • Intrinsic and extrinsic pathway signaling during neuronal apoptosis: Lessons from the analysis of mutant mice
    • Putcha GV, Harris CA, Moulder KL, Easton RM, Thompson CB, Johnson Jr EM . Intrinsic and extrinsic pathway signaling during neuronal apoptosis: lessons from the analysis of mutant mice. J Cell Biol 2002; 157: 441-453.
    • (2002) J Cell Biol , vol.157 , pp. 441-453
    • Putcha, G.V.1    Harris, C.A.2    Moulder, K.L.3    Easton, R.M.4    Thompson, C.B.5    Johnson, E.M.6
  • 30
    • 84912123834 scopus 로고    scopus 로고
    • Parkin sensitizes toward apoptosis induced by mitochondrial depolarization through promoting degradation of Mcl-1
    • Carroll RG, Hollville E, Martin SJ. Parkin sensitizes toward apoptosis induced by mitochondrial depolarization through promoting degradation of Mcl-1. Cell Rep 2014; 9: 1538-1553.
    • (2014) Cell Rep , vol.9 , pp. 1538-1553
    • Carroll, R.G.1    Hollville, E.2    Martin, S.J.3
  • 31
    • 0031438851 scopus 로고    scopus 로고
    • Analysis of the mechanism of loss of trophic factor dependence associated with neuronal maturation: A phenotype indistinguishable from Bax deletion
    • Easton RM, Deckwerth TL, Parsadanian AS, Johnson Jr EM. Analysis of the mechanism of loss of trophic factor dependence associated with neuronal maturation: a phenotype indistinguishable from Bax deletion. J Neurosci 1997; 17: 9656-9666.
    • (1997) J Neurosci , vol.17 , pp. 9656-9666
    • Easton, R.M.1    Deckwerth, T.L.2    Parsadanian, A.S.3    Johnson, E.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.