메뉴 건너뛰기




Volumn 34, Issue 4, 2014, Pages 699-710

Correction: "SirT3 regulates a novel arm of the mitochondrial unfolded protein response" [34, 4, 699-710, (2014)] DOI: https://doi.org/10.1128/MCB.01337-13;SirT3 regulates the mitochondrial unfolded protein response

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CATALASE; EPHRIN RECEPTOR B1; ESTROGEN RECEPTOR ALPHA; GREEN FLUORESCENT PROTEIN; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; HEAT SHOCK PROTEIN 90; LAMIN A; LAMIN C; MANGANESE SUPEROXIDE DISMUTASE; MESSENGER RNA; PARKIN; REACTIVE OXYGEN METABOLITE; SIRTUIN 3; TRANSCRIPTION FACTOR FKHRL1; TUBULIN; TUMOR SUPPRESSOR PROTEIN;

EID: 84892989225     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.00191-17     Document Type: Erratum
Times cited : (226)

References (43)
  • 1
    • 84858604270 scopus 로고    scopus 로고
    • Metabolic reprogramming: a cancer hallmark even Warburg did not anticipate
    • Ward PS, Thompson CB. 2012. Metabolic reprogramming: a cancer hallmark even Warburg did not anticipate. Cancer Cell 21:297-308. http: //dx.doi.org/10.1016/j.ccr.2012.02.014.
    • (2012) Cancer Cell , vol.21 , pp. 297-308
    • Ward, P.S.1    Thompson, C.B.2
  • 2
    • 84868019043 scopus 로고    scopus 로고
    • Cancer cell metabolism: one hallmark, many faces
    • Cantor JR, Sabatini DM. 2012. Cancer cell metabolism: one hallmark, many faces. Cancer Discov. 2:881-898. http://dx.doi.org/10.1158/2159-8290.CD-12-0345.
    • (2012) Cancer Discov. , vol.2 , pp. 881-898
    • Cantor, J.R.1    Sabatini, D.M.2
  • 3
    • 77951432631 scopus 로고    scopus 로고
    • The causes of cancer revisited: "mitochondrial malignancy" and ROS-induced oncogenic transformation-why mitochondria are targets for cancer therapy
    • Ralph SJ, Rodriguez-Enriquez S, Neuzil J, Saavedra E, Moreno-Sanchez R. 2010. The causes of cancer revisited: "mitochondrial malignancy" and ROS-induced oncogenic transformation-why mitochondria are targets for cancer therapy. Mol. Aspects Med. 31:145-170. http://dx.doi.org/10 .1016/j.mam.2010.02.008.
    • (2010) Mol. Aspects Med. , vol.31 , pp. 145-170
    • Ralph, S.J.1    Rodriguez-Enriquez, S.2    Neuzil, J.3    Saavedra, E.4    Moreno-Sanchez, R.5
  • 4
    • 77956186783 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes
    • Hamanaka RB, Chandel NS. 2010. Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes. Trends Biochem. Sci. 35:505-513. http://dx.doi.org/10.1016/j.tibs.2010.04.002.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 505-513
    • Hamanaka, R.B.1    Chandel, N.S.2
  • 6
    • 80054746880 scopus 로고    scopus 로고
    • Mitochondrial sirtuins in the regulation of mitochondrial activity and metabolic adaptation
    • Lombard DB, Tishkoff DX, Bao J. 2011. Mitochondrial sirtuins in the regulation of mitochondrial activity and metabolic adaptation. Handb. Exp. Pharmacol. 206:163-188. http://dx.doi.org/10.1007/978-3-642-21631-2_8.
    • (2011) Handb. Exp. Pharmacol. , vol.206 , pp. 163-188
    • Lombard, D.B.1    Tishkoff, D.X.2    Bao, J.3
  • 10
    • 53549105529 scopus 로고    scopus 로고
    • SIRT3 is a stress-responsive deacetylase in cardiomyocytes that protects cells from stress-mediated cell death by deacetylation of Ku70
    • Sundaresan NR, Samant SA, Pillai VB, Rajamohan SB, Gupta MP. 2008. SIRT3 is a stress-responsive deacetylase in cardiomyocytes that protects cells from stress-mediated cell death by deacetylation of Ku70. Mol. Cell. Biol. 28:6384-6401. http://dx.doi.org/10.1128/MCB.00426-08.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 6384-6401
    • Sundaresan, N.R.1    Samant, S.A.2    Pillai, V.B.3    Rajamohan, S.B.4    Gupta, M.P.5
  • 11
    • 79952353862 scopus 로고    scopus 로고
    • Neuronal Sirt3 protects against excitotoxic injury in mouse cortical neuron culture
    • Kim SH, Lu HF, Alano CC. 2011. Neuronal Sirt3 protects against excitotoxic injury in mouse cortical neuron culture. PLoS One 6:e14731. http: //dx.doi.org/10.1371/journal.pone.0014731.
    • (2011) PLoS One , vol.6
    • Kim, S.H.1    Lu, H.F.2    Alano, C.C.3
  • 12
    • 79957441575 scopus 로고    scopus 로고
    • SIRT3 and cancer: tumor promoter or suppressor? Biochim
    • Alhazzazi TY, Kamarajan P, Verdin E, Kapila YL. 2011. SIRT3 and cancer: tumor promoter or suppressor? Biochim. Biophys. Acta 1816:80-88. http://dx.doi.org/10.1016/j.bbcan.2011.04.004.
    • (2011) Biophys. Acta , vol.1816 , pp. 80-88
    • Alhazzazi, T.Y.1    Kamarajan, P.2    Verdin, E.3    Kapila, Y.L.4
  • 13
    • 78649521247 scopus 로고    scopus 로고
    • Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation
    • Qiu X, Brown K, Hirschey MD, Verdin E, Chen D. 2010. Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation. Cell Metab. 12:662-667. http://dx.doi.org/10.1016/j.cmet.2010.11.015.
    • (2010) Cell Metab. , vol.12 , pp. 662-667
    • Qiu, X.1    Brown, K.2    Hirschey, M.D.3    Verdin, E.4    Chen, D.5
  • 14
    • 84865576222 scopus 로고    scopus 로고
    • Metabolic regulation by SIRT3: implications for tumorigenesis
    • Finley LW, Haigis MC. 2012. Metabolic regulation by SIRT3: implications for tumorigenesis. Trends Mol. Med. 18:516-523. http://dx.doi.org /10.1016/j.molmed.2012.05.004.
    • (2012) Trends Mol. Med. , vol.18 , pp. 516-523
    • Finley, L.W.1    Haigis, M.C.2
  • 15
    • 0037192473 scopus 로고    scopus 로고
    • Redox regulation of forkhead proteins through a p66shc-dependent signaling pathway
    • Nemoto S, Finkel T. 2002. Redox regulation of forkhead proteins through a p66shc-dependent signaling pathway. Science 295:2450-2452. http://dx .doi.org/10.1126/science.1069004.
    • (2002) Science , vol.295 , pp. 2450-2452
    • Nemoto, S.1    Finkel, T.2
  • 17
    • 70349208608 scopus 로고    scopus 로고
    • Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice
    • Sundaresan NR, Gupta M, Kim G, Rajamohan SB, Isbatan A, Gupta MP. 2009. Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice. J. Clin. Invest. 119:2758-2771. http://dx.doi.org/10.1172/JCI39162.
    • (2009) J. Clin. Invest. , vol.119 , pp. 2758-2771
    • Sundaresan, N.R.1    Gupta, M.2    Kim, G.3    Rajamohan, S.B.4    Isbatan, A.5    Gupta, M.P.6
  • 18
    • 84868007565 scopus 로고    scopus 로고
    • Physiological roles of mitochondrial reactive oxygen species
    • Sena LA, Chandel NS. 2012. Physiological roles of mitochondrial reactive oxygen species. Mol. Cell 48:158-167. http://dx.doi.org/10.1016/j.molcel .2012.09.025.
    • (2012) Mol. Cell , vol.48 , pp. 158-167
    • Sena, L.A.1    Chandel, N.S.2
  • 19
    • 0347285295 scopus 로고    scopus 로고
    • A trip to the ER: coping with stress
    • Rutkowski DT, Kaufman RJ. 2004. A trip to the ER: coping with stress. Trends Cell Biol. 14:20-28. http://dx.doi.org/10.1016/j.tcb.2003.11.001.
    • (2004) Trends Cell Biol. , vol.14 , pp. 20-28
    • Rutkowski, D.T.1    Kaufman, R.J.2
  • 21
    • 0033081478 scopus 로고    scopus 로고
    • Retrograde Ca2 signaling in C2C12 skeletal myocytes in response to mitochondrial genetic and metabolic stress: a novel mode of inter-organelle crosstalk
    • Biswas G, Adebanjo OA, Freedman BD, Anandatheerthavarada HK, Vijayasarathy C, Zaidi M, Kotlikoff M, Avadhani NG. 1999. Retrograde Ca2 signaling in C2C12 skeletal myocytes in response to mitochondrial genetic and metabolic stress: a novel mode of inter-organelle crosstalk. EMBO J. 18:522-533. http://dx.doi.org/10.1093/emboj/18.3.522.
    • (1999) EMBO J. , vol.18 , pp. 522-533
    • Biswas, G.1    Adebanjo, O.A.2    Freedman, B.D.3    Anandatheerthavarada, H.K.4    Vijayasarathy, C.5    Zaidi, M.6    Kotlikoff, M.7    Avadhani, N.G.8
  • 22
    • 37849048003 scopus 로고    scopus 로고
    • Discovery of genes activated by the mitochondrial unfolded protein response (mtUPR) and cog-nate promoter elements
    • Aldridge JE, Horibe T, Hoogenraad NJ. 2007. Discovery of genes activated by the mitochondrial unfolded protein response (mtUPR) and cog-nate promoter elements. PLoS One 2:e874. http://dx.doi.org/10.1371 /journal.pone.0000874.
    • (2007) PLoS One , vol.2
    • Aldridge, J.E.1    Horibe, T.2    Hoogenraad, N.J.3
  • 23
    • 34250811284 scopus 로고    scopus 로고
    • Mitochondrial-nuclear communications
    • Ryan MT, Hoogenraad NJ. 2007. Mitochondrial-nuclear communications. Annu. Rev. Biochem. 76:701-722. http://dx.doi.org/10.1146/annurev.biochem .76.052305.091720.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 701-722
    • Ryan, M.T.1    Hoogenraad, N.J.2
  • 24
    • 84871734834 scopus 로고    scopus 로고
    • Signaling the mitochondrial unfolded protein response
    • Pellegrino MW, Nargund AM, Haynes CM. 2013. Signaling the mitochondrial unfolded protein response. Biochim. Biophys. Acta 1833:410-416. http://dx.doi.org/10.1016/j.bbamcr.2012.02.019.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 410-416
    • Pellegrino, M.W.1    Nargund, A.M.2    Haynes, C.M.3
  • 26
    • 37849038317 scopus 로고    scopus 로고
    • The chop gene contains an element for the positive regulation of the mitochondrial unfolded protein response
    • Horibe T, Hoogenraad NJ. 2007. The chop gene contains an element for the positive regulation of the mitochondrial unfolded protein response. PLoS One 2:e835. http://dx.doi.org/10.1371/journal.pone.0000835.
    • (2007) PLoS One , vol.2
    • Horibe, T.1    Hoogenraad, N.J.2
  • 27
    • 34848861368 scopus 로고    scopus 로고
    • ClpP mediates activation of a mitochondrial unfolded protein response in C
    • Haynes CM, Petrova K, Benedetti C, Yang Y, Ron D. 2007. ClpP mediates activation of a mitochondrial unfolded protein response in C. elegans. Dev. Cell 13:467-480. http://dx.doi.org/10.1016/j.devcel.2007.07 .016.
    • (2007) elegans. Dev. Cell , vol.13 , pp. 467-480
    • Haynes, C.M.1    Petrova, K.2    Benedetti, C.3    Yang, Y.4    Ron, D.5
  • 28
    • 45149128904 scopus 로고    scopus 로고
    • Mitochondrial protein quality control by the proteasome involves ubiquitination and the protease Omi
    • Radke S, Chander H, Schafer P, Meiss G, Kruger R, Schulz JB, Germain D. 2008. Mitochondrial protein quality control by the proteasome involves ubiquitination and the protease Omi. J. Biol. Chem. 283:12681-12685. http://dx.doi.org/10.1074/jbc.C800036200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 12681-12685
    • Radke, S.1    Chander, H.2    Schafer, P.3    Meiss, G.4    Kruger, R.5    Schulz, J.B.6    Germain, D.7
  • 30
    • 79955549674 scopus 로고    scopus 로고
    • Estrogen receptor mediates a distinct mitochondrial unfolded protein response
    • Papa L, Germain D. 2011. Estrogen receptor mediates a distinct mitochondrial unfolded protein response. J. Cell Sci. 124:1396-1402. http://dx .doi.org/10.1242/jcs.078220.
    • (2011) J. Cell Sci. , vol.124 , pp. 1396-1402
    • Papa, L.1    Germain, D.2
  • 31
    • 78649300971 scopus 로고    scopus 로고
    • p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both
    • Narendra D, Kane LA, Hauser DN, Fearnley IM, Youle RJ. 2010. p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both. Autophagy 6:1090-1106. http://dx.doi.org/10.4161/auto.6.8.13426.
    • (2010) Autophagy , vol.6 , pp. 1090-1106
    • Narendra, D.1    Kane, L.A.2    Hauser, D.N.3    Fearnley, I.M.4    Youle, R.J.5
  • 32
    • 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, Youle RJ. 2010. Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin. J. Cell Biol. 191:1367-1380. http://dx.doi .org/10.1083/jcb.201007013.
    • (2010) 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    Youle, R.J.7
  • 35
    • 41849128523 scopus 로고    scopus 로고
    • The FoxO code
    • Calnan DR, Brunet A. 2008. The FoxO code. Oncogene 27:2276-2288. http://dx.doi.org/10.1038/onc.2008.21.
    • (2008) Oncogene , vol.27 , pp. 2276-2288
    • Calnan, D.R.1    Brunet, A.2
  • 36
    • 34249281690 scopus 로고    scopus 로고
    • Stressing the role of FoxO proteins in lifespan and disease
    • van der Horst A, Burgering BM. 2007. Stressing the role of FoxO proteins in lifespan and disease. Nat. Rev. Mol. Cell Biol. 8:440-450. http://dx.doi .org/10.1038/nrm2190.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 440-450
    • van der Horst, A.1    Burgering, B.M.2
  • 37
    • 25444442080 scopus 로고    scopus 로고
    • Triple layer control: phosphorylation, acetylation and ubiquitination of FOXO proteins
    • Vogt PK, Jiang H, Aoki M. 2005. Triple layer control: phosphorylation, acetylation and ubiquitination of FOXO proteins. Cell Cycle 4:908-913. http://dx.doi.org/10.4161/cc.4.7.1796.
    • (2005) Cell Cycle , vol.4 , pp. 908-913
    • Vogt, P.K.1    Jiang, H.2    Aoki, M.3
  • 40
    • 0025341052 scopus 로고
    • Identification of a 66 KDa protein associated with yeast mitochondrial ATP synthase as heat shock protein hsp60
    • Gray RE, Grasso DG, Maxwell RJ, Finnegan PM, Nagley P, Devenish RJ. 1990. Identification of a 66 KDa protein associated with yeast mitochondrial ATP synthase as heat shock protein hsp60. FEBS Lett. 268:265-268. http://dx.doi.org/10.1016/0014-5793(90)81024-I.
    • (1990) FEBS Lett. , vol.268 , pp. 265-268
    • Gray, R.E.1    Grasso, D.G.2    Maxwell, R.J.3    Finnegan, P.M.4    Nagley, P.5    Devenish, R.J.6
  • 43
    • 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, Youle RJ. 2012. 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. http://dx.doi .org/10.1016/j.devcel.2011.12.014.
    • (2012) Dev. Cell , vol.22 , pp. 320-333
    • Lazarou, M.1    Jin, S.M.2    Kane, L.A.3    Youle, R.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.