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Volumn 16, Issue 11, 2009, Pages 1505-1514

αNAC depletion as an initiator of ER stress-induced apoptosis in hypoxia

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; ALPHA NASCENT POLYPEPTIDE ASSOCIATED COMPLEX; CASPASE; GLUCOSE REGULATED PROTEIN 78; GLYCOGEN SYNTHASE KINASE 3BETA; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; POLYPEPTIDE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR ELF 2; UNCLASSIFIED DRUG; CHAPERONE; GLYCOGEN SYNTHASE KINASE 3; GLYCOGEN SYNTHASE KINASE 3 BETA; NASCENT POLYPEPTIDE ASSOCIATED COMPLEX; NASCENT-POLYPEPTIDE-ASSOCIATED COMPLEX; SMALL INTERFERING RNA; UBIQUITIN;

EID: 70350035643     PISSN: 13509047     EISSN: 14765403     Source Type: Journal    
DOI: 10.1038/cdd.2009.90     Document Type: Article
Times cited : (43)

References (46)
  • 1
    • 0038446405 scopus 로고    scopus 로고
    • The unfolded protein response
    • Lie CY, Kaufman RJ. The unfolded protein response. J Cell Sci 2003; 116: 1861-1862.
    • (2003) J Cell Sci , vol.116 , pp. 1861-1862
    • Lie, C.Y.1    Kaufman, R.J.2
  • 3
    • 0343330935 scopus 로고    scopus 로고
    • Nascent polypeptide-associated complex stimulates protein import into yeast mitochondria
    • Fünfschilling U, Rospert S. Nascent polypeptide-associated complex stimulates protein import into yeast mitochondria. Mol Biol Cell 1999; 10: 3289-3299.
    • (1999) Mol Biol Cell , vol.10 , pp. 3289-3299
    • Fünfschilling, U.1    Rospert, S.2
  • 4
    • 0027980239 scopus 로고
    • A protein complex required for signal-sequence-specific sorting and translocation
    • Wiedmann B, Sakai H, Davis TA, Wiedmann M. A protein complex required for signal-sequence-specific sorting and translocation. Nature 1994; 370: 434-440.
    • (1994) Nature , vol.370 , pp. 434-440
    • Wiedmann, B.1    Sakai, H.2    Davis, T.A.3    Wiedmann, M.4
  • 5
    • 0036305948 scopus 로고    scopus 로고
    • Human brain nascent polypeptide-associated complex a subunit is decreased in patients with Alzheimer's disease and Down syndrome
    • Kim SH, Shim KS, Lubec G. Human brain nascent polypeptide-associated complex a subunit is decreased in patients with Alzheimer's disease and Down syndrome. J Investing Med 2002; 50: 293-301.
    • (2002) J Investing Med , vol.50 , pp. 293-301
    • Kim, S.H.1    Shim, K.S.2    Lubec, G.3
  • 6
    • 0034637706 scopus 로고    scopus 로고
    • The identification of novel therapeutic targets for the treatment of malignant brain tumors
    • Kroes RA, Jastrow A, McLone MG, Yamamoto H, Colley P, Kersey DS et al The identification of novel therapeutic targets for the treatment of malignant brain tumors. Cancer Lett 2000; 156: 191-198.
    • (2000) Cancer Lett , vol.156 , pp. 191-198
    • Kroes, R.A.1    Jastrow, A.2    McLone, M.G.3    Yamamoto, H.4    Colley, P.5    Kersey, D.S.6
  • 7
    • 0042865992 scopus 로고    scopus 로고
    • Suppression of CED-3-independent apoptosis by mitochondrial βNAC in Caenorhabditis elegans
    • Bloss TA, Witze ES, Rothman JH. Suppression of CED-3-independent apoptosis by mitochondrial βNAC in Caenorhabditis elegans. Nature 2003; 424: 1066-1071.
    • (2003) Nature , vol.424 , pp. 1066-1071
    • Bloss, T.A.1    Witze, E.S.2    Rothman, J.H.3
  • 8
    • 0029335574 scopus 로고
    • An insertion in the BTF3 transcription factor gene leads to an early postimplantation lethality in mice
    • Den JM, Behringer RR. An insertion in the BTF3 transcription factor gene leads to an early postimplantation lethality in mice. Transgenic Res 1995; 4: 264-269.
    • (1995) Transgenic Res , vol.4 , pp. 264-269
    • Den, J.M.1    Behringer, R.R.2
  • 9
    • 0033960927 scopus 로고    scopus 로고
    • Beicaudal encodes the Drosophila beta NAC homolog, a component of the ribosomal translational machinery
    • Markesic DC, Gajewski KM, Nazimiec ME, Beckingham K. Beicaudal encodes the Drosophila beta NAC homolog, a component of the ribosomal translational machinery. Development 2000; 127: 559-572.
    • (2000) Development , vol.127 , pp. 559-572
    • Markesic, D.C.1    Gajewski, K.M.2    Nazimiec, M.E.3    Beckingham, K.4
  • 10
    • 0033616846 scopus 로고    scopus 로고
    • Initial characterization of the nascent polypeptide-associated complex in yeast
    • Reimann B, Bradsher J, Franke J, Hartmann E, Wiedmann M, Prehn S et al. Initial characterization of the nascent polypeptide-associated complex in yeast. Yeast 1999; 15: 397-407.
    • (1999) Yeast , vol.15 , pp. 397-407
    • Reimann, B.1    Bradsher, J.2    Franke, J.3    Hartmann, E.4    Wiedmann, M.5    Prehn, S.6
  • 12
    • 2942590732 scopus 로고    scopus 로고
    • Exploiting tumor hypoxia in cancer treatment
    • Brown JM, Wilson WR. Exploiting tumor hypoxia in cancer treatment. Nat Rev Cancer 2004; 4: 437-447.
    • (2004) Nat Rev Cancer , vol.4 , pp. 437-447
    • Brown, J.M.1    Wilson, W.R.2
  • 14
  • 15
    • 0043037253 scopus 로고    scopus 로고
    • Endoplasmic reticulum: A primary target in various acute disorders and degenerative diseases of the brain
    • Paschen W. Endoplasmic reticulum: A primary target in various acute disorders and degenerative diseases of the brain. Cell Calcium 2003; 34: 365-383.
    • (2003) Cell Calcium , vol.34 , pp. 365-383
    • Paschen, W.1
  • 16
    • 24644487812 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress response and neurodegeneration
    • Paschen W, Mengesdorf T. Endoplasmic reticulum stress response and neurodegeneration. Cell Calcium 2005; 38: 409-415.
    • (2005) Cell Calcium , vol.38 , pp. 409-415
    • Paschen, W.1    Mengesdorf, T.2
  • 19
    • 17844409295 scopus 로고    scopus 로고
    • Interaction of the taxilin family with the nascent polypeptide-associated complex that is involved in the transcriptional and translational processes
    • Yoshida K, Nogami S, Satoh S, Tanaka-Nakadate S, Hiraishi H, Terano A et al. Interaction of the taxilin family with the nascent polypeptide-associated complex that is involved in the transcriptional and translational processes. Genes to Cells 2005; 10: 465-476.
    • (2005) Genes to Cells , vol.10 , pp. 465-476
    • Yoshida, K.1    Nogami, S.2    Satoh, S.3    Tanaka-Nakadate, S.4    Hiraishi, H.5    Terano, A.6
  • 20
    • 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 XZ, Bertolotti A, Zhang Y, Chung P, Harding PHP 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.Z.2    Bertolotti, A.3    Zhang, Y.4    Chung, P.5    Harding, P.H.P.6
  • 21
    • 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
  • 22
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE in response to ER stress to produce a highly active transcription factor
    • Yoshida H, Matsui T, Yamamoto A, Okada T, Mori K. XBP1 mRNA is induced by ATF6 and spliced by IRE in response to ER stress to produce a highly active transcription factor. Cell 2001; 107: 881-891.
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 23
    • 34548299555 scopus 로고    scopus 로고
    • Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability
    • Ding WX, Ni HM, Gao W, Yoshimori T, Stolz DB, Ron D et al. Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability. Am J Pathol 2007; 171: 513-524.
    • (2007) Am J Pathol , vol.171 , pp. 513-524
    • Ding, W.X.1    Ni, H.M.2    Gao, W.3    Yoshimori, T.4    Stolz, D.B.5    Ron, D.6
  • 24
    • 34249088952 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced cell death mediated by the proteasome
    • Egger L, Madden DT, Rhême C, Rao RV, Bredesen DE. Endoplasmic reticulum stress-induced cell death mediated by the proteasome. Cell Death Differ 2007; 14: 1172-1180.
    • (2007) Cell Death Differ , vol.14 , pp. 1172-1180
    • Egger, L.1    Madden, D.T.2    Rhême, C.3    Rao, R.V.4    Bredesen, D.E.5
  • 25
    • 1842843860 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program
    • Rao R, Ellerby HM, Bredesen DE. Coupling endoplasmic reticulum stress to the cell death program. Cell Death Differ 2004; 11: 372-380.
    • (2004) Cell Death Differ , vol.11 , pp. 372-380
    • Rao, R.1    Ellerby, H.M.2    Bredesen, D.E.3
  • 26
    • 23844481790 scopus 로고    scopus 로고
    • Caspase-12 and caspase-4 are not required for caspase-dependent endoplasmic reticulum stress-induced apoptosis
    • Obeng EA, Boise LH. Caspase-12 and caspase-4 are not required for caspase-dependent endoplasmic reticulum stress-induced apoptosis. J Biol Chem 2005; 280: 29578-29587.
    • (2005) J Biol Chem , vol.280 , pp. 29578-29587
    • Obeng, E.A.1    Boise, L.H.2
  • 28
    • 12144289805 scopus 로고    scopus 로고
    • GSK3β-dependent phosphorylation of the NAC coactivator regulates its nuclear translocation and proteasome-mediated degradation
    • Quélo I, Akhouayri O, Prud'homme J, St-Arnaud R. GSK3β-dependent phosphorylation of the NAC coactivator regulates its nuclear translocation and proteasome-mediated degradation. Biochemstry 2004; 43: 2906-2914.
    • (2004) Biochemstry , vol.43 , pp. 2906-2914
    • Quélo, I.1    Akhouayri, O.2    Prud'homme, J.3    St-Arnaud, R.4
  • 29
    • 0029776032 scopus 로고    scopus 로고
    • A molecular mechanism for the effect of lithium on development
    • Klein PS, Melton DA. A molecular mechanism for the effect of lithium on development. Proc Natl Acad Sci USA 1996; 93: 8455-8459.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8455-8459
    • Klein, P.S.1    Melton, D.A.2
  • 30
    • 0042379932 scopus 로고    scopus 로고
    • Lithium and GSK-3: One inhibitor, two inhibitory actions, multiple outcomes
    • Jope RS. Lithium and GSK-3: One inhibitor, two inhibitory actions, multiple outcomes. Trends Pharmacol Sci 2003; 24: 441-443.
    • (2003) Trends Pharmacol Sci , vol.24 , pp. 441-443
    • Jope, R.S.1
  • 31
    • 3042635178 scopus 로고    scopus 로고
    • GSK3 inhibitors: Development and therapeutic potential
    • Cohen P, Goedert M. GSK3 inhibitors: Development and therapeutic potential. Nat Rev Drug Discov 2004; 3: 479-487.
    • (2004) Nat Rev Drug Discov , vol.3 , pp. 479-487
    • Cohen, P.1    Goedert, M.2
  • 33
    • 1842614335 scopus 로고    scopus 로고
    • Involvement of ERK MAP kinase in endoplasmic reticulum stress in SH-SY5Y human neuroblastoma cells
    • Arai K, Lee SR, van Leyen K, Kurose H, Lo EH. Involvement of ERK MAP kinase in endoplasmic reticulum stress in SH-SY5Y human neuroblastoma cells. J Neurochemistry 2004; 89: 232-239.
    • (2004) J Neurochemistry , vol.89 , pp. 232-239
    • Arai, K.1    Lee, S.R.2    van Leyen, K.3    Kurose, H.4    Lo, E.H.5
  • 34
    • 0035854661 scopus 로고    scopus 로고
    • Predominant identification of RNA-binding proteins in Fas-induced apoptosis by proteome analysis
    • Thiede B, Dimmler C, Siejak F, Rude T. Predominant identification of RNA-binding proteins in Fas-induced apoptosis by proteome analysis. J Biol Chem 2001; 276: 26044-26050.
    • (2001) J Biol Chem , vol.276 , pp. 26044-26050
    • Thiede, B.1    Dimmler, C.2    Siejak, F.3    Rude, T.4
  • 35
    • 0034528831 scopus 로고    scopus 로고
    • The α AND β subunit of the nascent polypeptide-associated complex have distinct functions
    • Beatrix B, Sakai H, Wiedmann M. The α AND β subunit of the nascent polypeptide-associated complex have distinct functions. J Biol Chem 2000; 275: 37838-37845.
    • (2000) J Biol Chem , vol.275 , pp. 37838-37845
    • Beatrix, B.1    Sakai, H.2    Wiedmann, M.3
  • 37
    • 0031888576 scopus 로고    scopus 로고
    • The alpha chain of the nascent polypeptide-asssociated complex functions as a transcriptional coactivator
    • Yotov WV, Moreau A, St-Arnaud R. The alpha chain of the nascent polypeptide-asssociated complex functions as a transcriptional coactivator. Mol Cell Biol 1998; 18: 1303-1311.
    • (1998) Mol Cell Biol , vol.18 , pp. 1303-1311
    • Yotov, W.V.1    Moreau, A.2    St-Arnaud, R.3
  • 39
    • 0344642999 scopus 로고    scopus 로고
    • The alpha-chain of the nascent polypeptide-associated complex binds to and regulates FADD function
    • Stilo R, Liguoro D, di Jeso B, Leonardi A, Vito P. The alpha-chain of the nascent polypeptide-associated complex binds to and regulates FADD function. Biochem Biophys Res Commun 2003; 303: 1034-1041.
    • (2003) Biochem Biophys Res Commun , vol.303 , pp. 1034-1041
    • Stilo, R.1    Liguoro, D.2    di Jeso, B.3    Leonardi, A.4    Vito, P.5
  • 40
    • 34250812108 scopus 로고    scopus 로고
    • Identification of mRNA that continue to associate with polysomes during hypoxia
    • Thomas JD, Johannes GJ. Identification of mRNA that continue to associate with polysomes during hypoxia. RNA 2007; 13: 1116-1131.
    • (2007) RNA , vol.13 , pp. 1116-1131
    • Thomas, J.D.1    Johannes, G.J.2
  • 41
    • 18144390490 scopus 로고    scopus 로고
    • The crystal structure of archaeal nascent polypeptide-associated complex (NAC) reveals a unique fold and the presence of a ubiquitin-associated domain
    • Spreter T, Pech M, Beatrix B. The crystal structure of archaeal nascent polypeptide-associated complex (NAC) reveals a unique fold and the presence of a ubiquitin-associated domain. J Biol Chem 2005; 280: 15849-15854.
    • (2005) J Biol Chem , vol.280 , pp. 15849-15854
    • Spreter, T.1    Pech, M.2    Beatrix, B.3
  • 42
    • 33846008044 scopus 로고    scopus 로고
    • The yeast Ccr4-Not complex controls ubiquitination of the nascent-associated polypeptide (NAC-EDG) complex
    • Panasenko O, Landrieux E, Feuermann M, Finka A, Paquet N, Collart MA. The yeast Ccr4-Not complex controls ubiquitination of the nascent-associated polypeptide (NAC-EDG) complex. J Biol Chem 2006; 281: 31389-31398.
    • (2006) J Biol Chem , vol.281 , pp. 31389-31398
    • Panasenko, O.1    Landrieux, E.2    Feuermann, M.3    Finka, A.4    Paquet, N.5    Collart, M.A.6
  • 43
    • 40749094856 scopus 로고    scopus 로고
    • Activation of the PI3-K/AKT pathway and implications for radioresistance mechanisms in head and neck cancer
    • Bussink J, van der Kogel AJ, Kaanders JHAM. Activation of the PI3-K/AKT pathway and implications for radioresistance mechanisms in head and neck cancer. Lancet Oncol 2008; 9: 288-296.
    • (2008) Lancet Oncol , vol.9 , pp. 288-296
    • Bussink, J.1    van der Kogel, A.J.2    Kaanders, J.H.A.M.3
  • 44
    • 0036830441 scopus 로고    scopus 로고
    • Enhanced glycogen synthase kinase-3β activity mediates hypoxia-induced apoptosis of vascular smooth muscle cells and is prevented by glucose transport and metabolism
    • Loberg RD, Vesely E, Brosius III FC. Enhanced glycogen synthase kinase-3β activity mediates hypoxia-induced apoptosis of vascular smooth muscle cells and is prevented by glucose transport and metabolism. J Biol Chem 2002; 277: 41667-41673.
    • (2002) J Biol Chem , vol.277 , pp. 41667-41673
    • Loberg, R.D.1    Vesely, E.2    Brosius III, F.C.3
  • 45
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • Cross DAE, Alessi DR, Cohen P, Andjelkovich M, Hemmings BA. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 1995; 378: 785-789.
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.E.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 46
    • 23944525536 scopus 로고    scopus 로고
    • Casein kinase II phosphorylation regulates alphaNAC sucellular localization and transcriptional coactivating activity
    • Quélo I, Gauthier C, St-Arnaud R. Casein kinase II phosphorylation regulates alphaNAC sucellular localization and transcriptional coactivating activity. Gene Expr 2005; 12: 151-163.
    • (2005) Gene Expr , vol.12 , pp. 151-163
    • Quélo, I.1    Gauthier, C.2    St-Arnaud, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.