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Volumn 5, Issue 1, 2014, Pages

JNK interaction with Sab mediates ER stress induced inhibition of mitochondrial respiration and cell death

Author keywords

Apoptosis; HeLa cells; Hepatocytes; Oxidative stress; Reactive oxygen species; Signal transduction

Indexed keywords

ADENOSINE TRIPHOSPHATE; BINDING PROTEIN; BREFELDIN A; CASPASE 3; CYTOCHROME C; REACTIVE OXYGEN METABOLITE; SHORT HAIRPIN RNA; STRESS ACTIVATED PROTEIN KINASE; TUNICAMYCIN;

EID: 84891794636     PISSN: None     EISSN: 20414889     Source Type: Journal    
DOI: 10.1038/cddis.2013.522     Document Type: Article
Times cited : (134)

References (42)
  • 1
    • 5644231992 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress links obesity, insulin action, and type 2 diabetes
    • Ozcan U, Cao Q, Yilmaz E, Lee AH, Iwakoshi NN, Ozdelen E et al. Endoplasmic reticulum stress links obesity, insulin action, and type 2 diabetes. Science 2004; 306: 457-461.
    • (2004) Science , vol.306 , pp. 457-461
    • Ozcan, U.1    Cao, Q.2    Yilmaz, E.3    Lee, A.H.4    Iwakoshi, N.N.5    Ozdelen, E.6
  • 3
    • 84864198388 scopus 로고    scopus 로고
    • A liver full of JNK: Signaling in regulation of cell function and disease pathogenesis, and clinical approaches
    • Seki E, Brenner DA, Karin M. A liver full of JNK: signaling in regulation of cell function and disease pathogenesis, and clinical approaches. Gastroenterology 2012; 143: 307-320.
    • (2012) Gastroenterology , vol.143 , pp. 307-320
    • Seki, E.1    Brenner, D.A.2    Karin, M.3
  • 4
    • 46649084880 scopus 로고    scopus 로고
    • Role of JNK translocation to mitochondria leading to inhibition of mitochondria bioenergetics in acetaminophen-induced liver injury
    • Hanawa N, Shinohara M, Saberi B, Gaarde WA, Han D, Kaplowitz N. Role of JNK translocation to mitochondria leading to inhibition of mitochondria bioenergetics in acetaminophen-induced liver injury. J Biol Chem 2008; 283: 13565-13577.
    • (2008) J Biol Chem , vol.283 , pp. 13565-13577
    • Hanawa, N.1    Shinohara, M.2    Saberi, B.3    Gaarde, W.A.4    Han, D.5    Kaplowitz, N.6
  • 5
    • 80053425902 scopus 로고    scopus 로고
    • C-Jun N-terminal kinase (JNK)-dependent acute liver injury from acetaminophen or tumor necrosis factor (TNF) requires mitochondrial Sab protein expression in mice
    • Win S, Than TA, Han D, Petrovic LM, Kaplowitz N. c-Jun N-terminal kinase (JNK)-dependent acute liver injury from acetaminophen or tumor necrosis factor (TNF) requires mitochondrial Sab protein expression in mice. J Biol Chem 2011; 286: 35071-35078.
    • (2011) J Biol Chem , vol.286 , pp. 35071-35078
    • Win, S.1    Than, T.A.2    Han, D.3    Petrovic, L.M.4    Kaplowitz, N.5
  • 6
    • 84873681976 scopus 로고    scopus 로고
    • Inhibition of JNK mitochondrial localization and signaling is protective against ischemia/reperfusion injury in rats
    • Chambers JW, Pachori A, Howard S, Iqbal S, LoGrasso PV. Inhibition of JNK mitochondrial localization and signaling is protective against ischemia/reperfusion injury in rats. J Biol Chem 2013; 288: 4000-4011.
    • (2013) J Biol Chem , vol.288 , pp. 4000-4011
    • Chambers, J.W.1    Pachori, A.2    Howard, S.3    Iqbal, S.4    Lograsso, P.V.5
  • 7
    • 84872356254 scopus 로고    scopus 로고
    • Blocking c-Jun N-terminal kinase (JNK) translocation to the mitochondria prevents 6-hydroxydopamine-induced toxicity in vitro and in vivo
    • Chambers JW, Howard S, LoGrasso PV. Blocking c-Jun N-terminal kinase (JNK) translocation to the mitochondria prevents 6-hydroxydopamine-induced toxicity in vitro and in vivo. J Biol Chem 2013; 288: 1079-1087.
    • (2013) J Biol Chem , vol.288 , pp. 1079-1087
    • Chambers, J.W.1    Howard, S.2    Lograsso, P.V.3
  • 8
    • 33750440743 scopus 로고    scopus 로고
    • ER stress-induced apoptosis and caspase-12 activation occurs downstream of mitochondrial apoptosis involving Apaf-1
    • Shiraishi H, Okamoto H, Yoshimura A, Yoshida H. ER stress-induced apoptosis and caspase-12 activation occurs downstream of mitochondrial apoptosis involving Apaf-1. J Cell Sci 2006; 119: 3958-3966.
    • (2006) J Cell Sci , vol.119 , pp. 3958-3966
    • Shiraishi, H.1    Okamoto, H.2    Yoshimura, A.3    Yoshida, H.4
  • 9
    • 79952264011 scopus 로고    scopus 로고
    • Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress
    • Tabas I, Ron D. Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress. Nat Cell Biol 2011; 13: 184-190.
    • (2011) Nat Cell Biol , vol.13 , pp. 184-190
    • Tabas, I.1    Ron, D.2
  • 10
    • 0036312001 scopus 로고    scopus 로고
    • Endoplasmic reticulum stressinduced cell death requires mitochondrial membrane permeabilization
    • Boya P, Cohen I, Zamzami N, Vieira HL, Kroemer G. Endoplasmic reticulum stressinduced cell death requires mitochondrial membrane permeabilization. Cell Death Differ 2002; 9: 465-467.
    • (2002) Cell Death Differ , vol.9 , pp. 465-467
    • Boya, P.1    Cohen, I.2    Zamzami, N.3    Vieira, H.L.4    Kroemer, G.5
  • 11
    • 0034723235 scopus 로고    scopus 로고
    • Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1
    • Urano F, Wang X, Bertolotti A, Zhang Y, Chung P, Harding HP et al. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 2000; 287: 664-666.
    • (2000) Science , vol.287 , pp. 664-666
    • Urano, F.1    Wang, X.2    Bertolotti, A.3    Zhang, Y.4    Chung, P.5    Harding, H.P.6
  • 12
    • 0036606540 scopus 로고    scopus 로고
    • ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
    • Nishitoh H, Matsuzawa A, Tobiume K, Saegusa K, Takeda K, Inoue K et al. ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev 2002; 16: 1345-1355.
    • (2002) Genes Dev , vol.16 , pp. 1345-1355
    • Nishitoh, H.1    Matsuzawa, A.2    Tobiume, K.3    Saegusa, K.4    Takeda, K.5    Inoue, K.6
  • 13
    • 10644233167 scopus 로고    scopus 로고
    • CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum
    • Marciniak SJ, Yun CY, Oyadomari S, Novoa I, Zhang Y, Jungreis R et al. CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum. Genes Dev 2004; 18: 3066-3077.
    • (2004) Genes Dev , vol.18 , pp. 3066-3077
    • Marciniak, S.J.1    Yun, C.Y.2    Oyadomari, S.3    Novoa, I.4    Zhang, Y.5    Jungreis, R.6
  • 15
    • 70349696241 scopus 로고    scopus 로고
    • Calcium/calmodulindependent protein kinase II links ER stress with Fas and mitochondrial apoptosis pathways
    • Timmins JM, Ozcan L, Seimon TA, Li G, Malagelada C, Backs J et al. Calcium/calmodulindependent protein kinase II links ER stress with Fas and mitochondrial apoptosis pathways. J Clin Invest 2009; 119: 2925-2941.
    • (2009) J Clin Invest , vol.119 , pp. 2925-2941
    • Timmins, J.M.1    Ozcan, L.2    Seimon, T.A.3    Li, G.4    Malagelada, C.5    Backs, J.6
  • 16
    • 84855696465 scopus 로고    scopus 로고
    • MTORC1 serves ER stress-triggered apoptosis via selective activation of the IRE1-JNK pathway
    • Kato H, Nakajima S, Saito Y, Takahashi S, Katoh R, Kitamura M. mTORC1 serves ER stress-triggered apoptosis via selective activation of the IRE1-JNK pathway. Cell Death Differ 2012; 19: 310-320.
    • (2012) Cell Death Differ , vol.19 , pp. 310-320
    • Kato, H.1    Nakajima, S.2    Saito, Y.3    Takahashi, S.4    Katoh, R.5    Kitamura, M.6
  • 17
    • 70349905357 scopus 로고    scopus 로고
    • Role of ERO1-alphamediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis
    • Li G, Mongillo M, Chin KT, Harding H, Ron D, Marks AR et al. Role of ERO1-alphamediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis. J Cell Biol 2009; 186: 783-792.
    • (2009) J Cell Biol , vol.186 , pp. 783-792
    • Li, G.1    Mongillo, M.2    Chin, K.T.3    Harding, H.4    Ron, D.5    Marks, A.R.6
  • 18
    • 80051704067 scopus 로고    scopus 로고
    • The sarcoplasmic reticulum luminal thiol oxidase ERO1 regulates cardiomyocyte excitation-coupled calcium release and response to hemodynamic load
    • Chin KT, Kang G, Qu J, Gardner LB, Coetzee WA, Zito E et al. The sarcoplasmic reticulum luminal thiol oxidase ERO1 regulates cardiomyocyte excitation-coupled calcium release and response to hemodynamic load. FASEB J 2011; 25: 2583-2591.
    • (2011) FASEB J , vol.25 , pp. 2583-2591
    • Chin, K.T.1    Kang, G.2    Qu, J.3    Gardner, L.B.4    Coetzee, W.A.5    Zito, E.6
  • 19
    • 0020643801 scopus 로고
    • 2+ from a nonmitochondrial intracellular store in pancreatic acinar cells by inositol-1,4,5-trisphosphate
    • 2+ from a nonmitochondrial intracellular store in pancreatic acinar cells by inositol-1,4,5-trisphosphate. Nature 1983; 306: 67-69.
    • (1983) Nature , vol.306 , pp. 67-69
    • Streb, H.1    Irvine, R.F.2    Berridge, M.J.3    Schulz, I.4
  • 20
    • 0030724177 scopus 로고    scopus 로고
    • Tunicamycin increases intracellular calcium levels in bovine aortic endothelial cells
    • Buckley BJ, Whorton AR. Tunicamycin increases intracellular calcium levels in bovine aortic endothelial cells. Am J Physiol 1997; 273: 1298-1305.
    • (1997) Am J Physiol , vol.273 , pp. 1298-1305
    • Buckley, B.J.1    Whorton, A.R.2
  • 21
    • 33749022800 scopus 로고    scopus 로고
    • Structural and functional features and significance of the physical linkage between ER and mitochondria
    • Csordás G, Renken C, Várnai P, Walter L, Weaver D, Buttle KF et al. Structural and functional features and significance of the physical linkage between ER and mitochondria. J Cell Biol 2006; 174: 915-921.
    • (2006) J Cell Biol , vol.174 , pp. 915-921
    • Csordás, G.1    Renken, C.2    Várnai, P.3    Walter, L.4    Weaver, D.5    Buttle, K.F.6
  • 22
    • 0023008846 scopus 로고
    • Novel blockade by brefeldin A of intracellular transport of secretory proteins in cultured rat hepatocytes
    • Misumi Y, Misumi Y, Miki K, Takatsuki A, Tamura G, Ikehara Y. Novel blockade by brefeldin A of intracellular transport of secretory proteins in cultured rat hepatocytes. J Biol Chem 1986; 261: 11398-11403.
    • (1986) J Biol Chem , vol.261 , pp. 11398-11403
    • Misumi, Y.1    Misumi, Y.2    Miki, K.3    Takatsuki, A.4    Tamura, G.5    Ikehara, Y.6
  • 23
    • 80054051101 scopus 로고    scopus 로고
    • The regulation and physiology of mitochondrial proton leak
    • Divakaruni AS, Brand MD. The regulation and physiology of mitochondrial proton leak. Physiology 2011; 26: 192-205.
    • (2011) Physiology , vol.26 , pp. 192-205
    • Divakaruni, A.S.1    Brand, M.D.2
  • 24
    • 79955544880 scopus 로고    scopus 로고
    • Mitochondrial c-Jun N-terminal kinase (JNK) signaling initiates physiological changes resulting in amplification of reactive oxygen species generation
    • Chambers JW, LoGrasso PV. Mitochondrial c-Jun N-terminal kinase (JNK) signaling initiates physiological changes resulting in amplification of reactive oxygen species generation. J Biol Chem 2011; 286: 16052-16062.
    • (2011) J Biol Chem , vol.286 , pp. 16052-16062
    • Chambers, J.W.1    Lograsso, P.V.2
  • 25
    • 80051999961 scopus 로고    scopus 로고
    • Selective inhibition of mitochondrial JNK signaling achieved using peptide mimicry of the Sab kinase interacting motif-1 (KIM1)
    • Chambers JW, Cherry L, Laughlin JD, Figuera-Losada M, Lograsso PV. Selective inhibition of mitochondrial JNK signaling achieved using peptide mimicry of the Sab kinase interacting motif-1 (KIM1). ACS Chem Biol 2011; 6: 808-818.
    • (2011) ACS Chem Biol , vol.6 , pp. 808-818
    • Chambers, J.W.1    Cherry, L.2    Laughlin, J.D.3    Figuera-Losada, M.4    Lograsso, P.V.5
  • 26
    • 10644248287 scopus 로고    scopus 로고
    • Sab (SH3BP5), a novel mitochondria-localized JNK-interacting protein
    • Wiltshire C, Gillespie DA, May GH. Sab (SH3BP5), a novel mitochondria-localized JNK-interacting protein. Biochem Soc Trans 2004; 32: 1075-1077.
    • (2004) Biochem Soc Trans , vol.32 , pp. 1075-1077
    • Wiltshire, C.1    Gillespie, D.A.2    May, G.H.3
  • 27
    • 77955824765 scopus 로고    scopus 로고
    • An intimate liaison: Spatial organization of the endoplasmic reticulum-mitochondria relationship
    • de Brito OM, Scorrano L. An intimate liaison: spatial organization of the endoplasmic reticulum-mitochondria relationship. EMBO J 2010; 29: 2715-2723.
    • (2010) EMBO J , vol.29 , pp. 2715-2723
    • De Brito, O.M.1    Scorrano, L.2
  • 29
    • 84881345531 scopus 로고    scopus 로고
    • Mitochondrial dysfunction indirectly elevates ROS production by the endoplasmic reticulum
    • Murphy MP. Mitochondrial dysfunction indirectly elevates ROS production by the endoplasmic reticulum. Cell Metab 2013; 18: 145-146.
    • (2013) Cell Metab , vol.18 , pp. 145-146
    • Murphy, M.P.1
  • 31
    • 35848957485 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and oxidative stress: A vicious cycle or a double-edged sword?
    • Malhotra JD, Kaufman RJ. Endoplasmic reticulum stress and oxidative stress: a vicious cycle or a double-edged sword? Antioxid Redox Signal 2007; 9: 2277-2293.
    • (2007) Antioxid Redox Signal , vol.9 , pp. 2277-2293
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 32
    • 47349099011 scopus 로고    scopus 로고
    • 2+ release through inositol 1,4,5-trisphosphate receptors and inhibits Ca2+ uptake by mitochondria without affecting ER calcium store content
    • 2+ release through inositol 1,4,5-trisphosphate receptors and inhibits Ca2+ uptake by mitochondria without affecting ER calcium store content. Cell Calcium 2008; 44: 324-338.
    • (2008) Cell Calcium , vol.44 , pp. 324-338
    • Hanson, C.J.1    Bootman, M.D.2    Distelhorst, C.W.3    Wojcikiewicz, R.J.4    Roderick, H.L.5
  • 33
    • 44749089373 scopus 로고    scopus 로고
    • High-and low-calcium-dependent mechanisms of mitochondrial calcium signalling
    • Spät A, Szanda G, Csordás G, Hajnóczky G. High-and low-calcium-dependent mechanisms of mitochondrial calcium signalling. Cell Calcium 2008; 44: 51-63.
    • (2008) Cell Calcium , vol.44 , pp. 51-63
    • Spät, A.1    Szanda, G.2    Csordás, G.3    Hajnóczky, G.4
  • 34
    • 84876063014 scopus 로고    scopus 로고
    • Regulation of drug-induced liver injury by signal transduction pathways: Critical role of mitochondria
    • Han D, Dara L, Win S, Than TA, Yuan L, Abbasi SQ et al. Regulation of drug-induced liver injury by signal transduction pathways: critical role of mitochondria. Trends Pharmacol Sci 2013; 34: 243-253.
    • (2013) Trends Pharmacol Sci , vol.34 , pp. 243-253
    • Han, D.1    Dara, L.2    Win, S.3    Than, T.A.4    Yuan, L.5    Abbasi, S.Q.6
  • 37
    • 11844284861 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK regulate the type 1 inositol trisphosphate receptor and calcium leak from the endoplasmic reticulum
    • Oakes SA, Scorrano L, Opferman JT, Bassik MC, Nishino M, Pozzan T et al. Proapoptotic BAX and BAK regulate the type 1 inositol trisphosphate receptor and calcium leak from the endoplasmic reticulum. Proc Natl Acad Sci USA 2005; 102: 105-110.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 105-110
    • Oakes, S.A.1    Scorrano, L.2    Opferman, J.T.3    Bassik, M.C.4    Nishino, M.5    Pozzan, T.6
  • 38
    • 46449116985 scopus 로고    scopus 로고
    • Calcium-induced generation of reactive oxygen species in brain mitochondria is mediated by permeability transition
    • Hansson MJ, Månsson R, Morota S, Uchino H, Kallur T, Sumi T et al. Calcium-induced generation of reactive oxygen species in brain mitochondria is mediated by permeability transition. Free Radic Biol Med 2008; 45: 284-294.
    • (2008) Free Radic Biol Med , vol.45 , pp. 284-294
    • Hansson, M.J.1    Månsson, R.2    Morota, S.3    Uchino, H.4    Kallur, T.5    Sumi, T.6
  • 40
    • 34248641140 scopus 로고    scopus 로고
    • Suppression of endoplasmic reticulum stress-induced caspase activation and cell death by the overexpression of Bcl-xL or Bcl-2
    • Murakami Y, Aizu-Yokota E, Sonoda Y, Ohta S, Kasahara T. Suppression of endoplasmic reticulum stress-induced caspase activation and cell death by the overexpression of Bcl-xL or Bcl-2. J Biochem 2007; 141: 401-410.
    • (2007) J Biochem , vol.141 , pp. 401-410
    • Murakami, Y.1    Aizu-Yokota, E.2    Sonoda, Y.3    Ohta, S.4    Kasahara, T.5
  • 41
    • 84855838914 scopus 로고    scopus 로고
    • Regulation of brefeldin A-induced ER stress and apoptosis by mitochondrial NADP-dependent isocitrate dehydrogenase
    • Moon JL, Kim SY, Shin SW, Park JW. Regulation of brefeldin A-induced ER stress and apoptosis by mitochondrial NADP-dependent isocitrate dehydrogenase. Biochem Biophys Res Commun 2012; 417: 760-764.
    • (2012) Biochem Biophys Res Commun , vol.417 , pp. 760-764
    • Moon, J.L.1    Kim, S.Y.2    Shin, S.W.3    Park, J.W.4
  • 42
    • 79959360187 scopus 로고    scopus 로고
    • Role of cAMP-responsive element-binding protein (CREB)-regulated transcription coactivator 3 (CRTC3) in the initiation of mitochondrial biogenesis and stress response in liver cells
    • Than TA, Lou H, Ji C, Win S, Kaplowitz N. Role of cAMP-responsive element-binding protein (CREB)-regulated transcription coactivator 3 (CRTC3) in the initiation of mitochondrial biogenesis and stress response in liver cells. J Biol Chem 2011; 286: 22047-22054.
    • (2011) J Biol Chem , vol.286 , pp. 22047-22054
    • Than, T.A.1    Lou, H.2    Ji, C.3    Win, S.4    Kaplowitz, N.5


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