메뉴 건너뛰기




Volumn 4, Issue 11, 2006, Pages 2024-2041

Adaptation to ER stress is mediated by differential stabilities of pro-survival and pro-apoptotic mRNAs and proteins

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; MESSENGER RNA; PROTEIN; APOPTOSIS REGULATORY PROTEIN; HEAT SHOCK PROTEIN;

EID: 33751069967     PISSN: 15457885     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.0040374     Document Type: Article
Times cited : (675)

References (75)
  • 2
    • 0036853914 scopus 로고    scopus 로고
    • Orchestrating the unfolded protein response in health and disease
    • Kaufman RJ (2002) Orchestrating the unfolded protein response in health and disease. J Clin Invest 110: 1389-1398.
    • (2002) J Clin Invest , vol.110 , pp. 1389-1398
    • Kaufman, R.J.1
  • 4
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • Bertolotti A, Zhang Y, Hendershot LM, Harding HP, Ron D (2000) Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat Cell Biol 2: 326-332.
    • (2000) Nat Cell Biol , vol.2 , pp. 326-332
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5
  • 5
    • 0034637605 scopus 로고    scopus 로고
    • Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum
    • Liu CY, Schroder M, Kaufman RJ (2000) Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum. J Biol Chem 275: 24881-24885.
    • (2000) J Biol Chem , vol.275 , pp. 24881-24885
    • Liu, C.Y.1    Schroder, M.2    Kaufman, R.J.3
  • 6
    • 0036069980 scopus 로고    scopus 로고
    • ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals
    • Shen J, Chen X, Hendershot L, Prywes R (2002) ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev Cell 3: 99-111.
    • (2002) Dev Cell , vol.3 , pp. 99-111
    • Shen, J.1    Chen, X.2    Hendershot, L.3    Prywes, R.4
  • 7
    • 12844257546 scopus 로고    scopus 로고
    • Stable binding of ATF6 to BiP in the endoplasmic reticulum stress response
    • Shen J, Snapp EL, Lippincott-Schwartz J, Prywes R (2005) Stable binding of ATF6 to BiP in the endoplasmic reticulum stress response. Mol Cell Biol 25: 921-932.
    • (2005) Mol Cell Biol , vol.25 , pp. 921-932
    • Shen, J.1    Snapp, E.L.2    Lippincott-Schwartz, J.3    Prywes, R.4
  • 8
    • 0038043221 scopus 로고    scopus 로고
    • Structure and intermolecular interactions of the luminal dimerization domain of human IRE1alpha
    • Liu CY, Xu Z, Kaufman RJ (2003) Structure and intermolecular interactions of the luminal dimerization domain of human IRE1alpha. J Biol Chem 278: 17680-17687.
    • (2003) J Biol Chem , vol.278 , pp. 17680-17687
    • Liu, C.Y.1    Xu, Z.2    Kaufman, R.J.3
  • 9
    • 0037166237 scopus 로고    scopus 로고
    • Dimerization and release of molecular chaperone inhibition facilitate activation of eukaryotic initiation factor-2 kinase in response to endoplasmic reticulum stress
    • Ma K, Vattem KM, Wek RC (2002) Dimerization and release of molecular chaperone inhibition facilitate activation of eukaryotic initiation factor-2 kinase in response to endoplasmic reticulum stress. J Biol Chem 277: 18728-18735.
    • (2002) J Biol Chem , vol.277 , pp. 18728-18735
    • Ma, K.1    Vattem, K.M.2    Wek, R.C.3
  • 10
    • 0037066741 scopus 로고    scopus 로고
    • The luminal domain of ATF6 senses endoplasmic reticulum (ER) stress and causes translocation of ATF6 from the ER to the Golgi
    • Chen X, Shen J, Prywes R (2002) The luminal domain of ATF6 senses endoplasmic reticulum (ER) stress and causes translocation of ATF6 from the ER to the Golgi. J Biol Chem 277: 13045-13052.
    • (2002) J Biol Chem , vol.277 , pp. 13045-13052
    • Chen, X.1    Shen, J.2    Prywes, R.3
  • 11
    • 0032693671 scopus 로고    scopus 로고
    • Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
    • Haze K, Yoshida H, Yanagi H, Yura T, Mori K (1999) Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol Biol Cell 10: 3787-3799.
    • (1999) Mol Biol Cell , vol.10 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 12
    • 0041731803 scopus 로고    scopus 로고
    • A serine protease inhibitor prevents endoplasmic reticulum stress-induced cleavage but not transport of the membrane-bound transcription factor ATF6
    • Okada T, Haze K, Nadanaka S, Yoshida H, Seidah NG, et al. (2003) A serine protease inhibitor prevents endoplasmic reticulum stress-induced cleavage but not transport of the membrane-bound transcription factor ATF6. J Biol Chem 278: 31024-31032.
    • (2003) J Biol Chem , vol.278 , pp. 31024-31032
    • Okada, T.1    Haze, K.2    Nadanaka, S.3    Yoshida, H.4    Seidah, N.G.5
  • 13
    • 0034282912 scopus 로고    scopus 로고
    • Activation of ATF6 and an ATF6 DNA binding site by the endoplasmic reticulum stress response
    • Wang Y, Shen J, Arenzana N, Tirasophon W, Kaufman RJ, et al. (2000) Activation of ATF6 and an ATF6 DNA binding site by the endoplasmic reticulum stress response. J Biol Chem 275: 27013-27020.
    • (2000) J Biol Chem , vol.275 , pp. 27013-27020
    • Wang, Y.1    Shen, J.2    Arenzana, N.3    Tirasophon, W.4    Kaufman, R.J.5
  • 14
    • 0034515724 scopus 로고    scopus 로고
    • ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs
    • Ye J, Rawson RB, Komuro R, Chen X, Dave UP, et al. (2000) ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs. Mol Cell 6: 1355-1364.
    • (2000) Mol Cell , vol.6 , pp. 1355-1364
    • Ye, J.1    Rawson, R.B.2    Komuro, R.3    Chen, X.4    Dave, U.P.5
  • 15
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum- resident kinase
    • Harding HP, Zhang Y, Ron D (1999) Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 397: 271-274.
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 16
    • 0033634641 scopus 로고    scopus 로고
    • Perk is essential for translational regulation and cell survival during the unfolded protein response
    • Harding HP, Zhang Y, Bertolotti A, Zeng H, Ron D (2000) Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol Cell 5: 897-904.
    • (2000) Mol Cell , vol.5 , pp. 897-904
    • Harding, H.P.1    Zhang, Y.2    Bertolotti, A.3    Zeng, H.4    Ron, D.5
  • 17
    • 0037416211 scopus 로고    scopus 로고
    • Stress-induced gene expression requires programmed recovery from translational repression
    • Novoa I, Zhang Y, Zeng H, Jungreis R, Harding HP, et al. (2003) Stress-induced gene expression requires programmed recovery from translational repression. EMBO J 22: 1180-1187.
    • (2003) EMBO J , vol.22 , pp. 1180-1187
    • Novoa, I.1    Zhang, Y.2    Zeng, H.3    Jungreis, R.4    Harding, H.P.5
  • 18
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding HP, Novoa I, Zhang Y, Zeng H, Wek R, et al. (2000) Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol Cell 6: 1099-1108.
    • (2000) Mol Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3    Zeng, H.4    Wek, R.5
  • 19
    • 5444264022 scopus 로고    scopus 로고
    • Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response
    • Lu PD, Harding HP, Ron D (2004) Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response. J Cell Biol 167: 27-33.
    • (2004) J Cell Biol , vol.167 , pp. 27-33
    • Lu, P.D.1    Harding, H.P.2    Ron, D.3
  • 20
    • 0034973982 scopus 로고    scopus 로고
    • Translational control is required for the unfolded protein response and in vivo glucose homeostasis
    • Scheuner D, Song B, McEwen E, Liu C, Laybutt R, et al. (2001) Translational control is required for the unfolded protein response and in vivo glucose homeostasis. Mol Cell 7: 1165-1176.
    • (2001) Mol Cell , vol.7 , pp. 1165-1176
    • Scheuner, D.1    Song, B.2    McEwen, E.3    Liu, C.4    Laybutt, R.5
  • 21
    • 0036713724 scopus 로고    scopus 로고
    • Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response
    • Okada T, Yoshida H, Akazawa R, Negishi M, Mori K (2002) Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response. Biochem J 366: 585-594.
    • (2002) Biochem J , vol.366 , pp. 585-594
    • Okada, T.1    Yoshida, H.2    Akazawa, R.3    Negishi, M.4    Mori, K.5
  • 22
    • 0037353039 scopus 로고    scopus 로고
    • An integrated stress response regulates amino acid metabolism and resistance to oxidative stress
    • Harding HP, Zhang Y, Zeng H, Novoa I, Lu PD, et al. (2003) An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol Cell 11: 619-633.
    • (2003) Mol Cell , vol.11 , pp. 619-633
    • Harding, H.P.1    Zhang, Y.2    Zeng, H.3    Novoa, I.4    Lu, P.D.5
  • 23
    • 0033598996 scopus 로고    scopus 로고
    • A role for presinilin-1 in nuclear accumulation of Ire1 fragments and induction of the mammalian unfolded protein response
    • Niwa N, Sidrauski C, Kaufman RJ, Walter P (1999) A role for presinilin-1 in nuclear accumulation of Ire1 fragments and induction of the mammalian unfolded protein response. Cell 99: 691-702.
    • (1999) Cell , vol.99 , pp. 691-702
    • Niwa, N.1    Sidrauski, C.2    Kaufman, R.J.3    Walter, P.4
  • 24
    • 0032525990 scopus 로고    scopus 로고
    • A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells
    • Tirasophon W, Welihinda AA, Kaufman RJ (1998) A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells. Genes Dev 12: 1812-1824.
    • (1998) Genes Dev , vol.12 , pp. 1812-1824
    • Tirasophon, W.1    Welihinda, A.A.2    Kaufman, R.J.3
  • 25
    • 0032190546 scopus 로고    scopus 로고
    • Cloning of mammalian Ire1 reveals diversity in the ER stress response
    • Wang XZ, Harding HP, Zhang Y, Jolicoeur EM, Kuroda M, et al. (1998) Cloning of mammalian Ire1 reveals diversity in the ER stress response. EMBO J 17: 5708-5717.
    • (1998) EMBO J , vol.17 , pp. 5708-5717
    • Wang, X.Z.1    Harding, H.P.2    Zhang, Y.3    Jolicoeur, E.M.4    Kuroda, M.5
  • 26
    • 0037011917 scopus 로고    scopus 로고
    • IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
    • Calfon M, Zeng H, Urano F, Till JH, Hubbard SR, et al. (2002) IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature 415: 92-96.
    • (2002) Nature , vol.415 , pp. 92-96
    • Calfon, M.1    Zeng, H.2    Urano, F.3    Till, J.H.4    Hubbard, S.R.5
  • 27
    • 0037083755 scopus 로고    scopus 로고
    • IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response
    • Lee K, Tirasophon W, Shen X, Michalak M, Prywes R, et al. (2002) IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response. Genes Dev 16: 452-466.
    • (2002) Genes Dev , vol.16 , pp. 452-466
    • Lee, K.1    Tirasophon, W.2    Shen, X.3    Michalak, M.4    Prywes, R.5
  • 28
    • 18244405070 scopus 로고    scopus 로고
    • Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development
    • Shen X, Ellis RE, Lee K, Liu CY, Yang K, et al. (2001) Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development. Cell 107: 893-903.
    • (2001) Cell , vol.107 , pp. 893-903
    • Shen, X.1    Ellis, R.E.2    Lee, K.3    Liu, C.Y.4    Yang, K.5
  • 29
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • Yoshida H, Matsui T, Yamamoto A, Okada T, Mori K (2001) XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 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
  • 30
    • 0142059951 scopus 로고    scopus 로고
    • XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response
    • Lee AH, Iwakoshi NN, Glimcher LH (2003) XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol Cell Biol 23: 7448-7459.
    • (2003) Mol Cell Biol , vol.23 , pp. 7448-7459
    • Lee, A.H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 31
    • 0037320265 scopus 로고    scopus 로고
    • A time-dependent phase shift in the mammalian unfolded protein response
    • Yoshida H, Matsui T, Hosokawa N, Kaufman RJ, Nagata K, et al. (2003) A time-dependent phase shift in the mammalian unfolded protein response. Dev Cell 4: 265-271.
    • (2003) Dev Cell , vol.4 , pp. 265-271
    • Yoshida, H.1    Matsui, T.2    Hosokawa, N.3    Kaufman, R.J.4    Nagata, K.5
  • 32
    • 0035310752 scopus 로고    scopus 로고
    • Identification of the G13 (cAMP-response-element-binding protein-related protein) gene product related to activating transcription factor 6 as a transcriptional activator of themammalianunfolded protein response
    • Haze K, Okada T, Yoshida H, Yanagi H, Yura T, et al. (2001) Identification of the G13 (cAMP-response-element-binding protein-related protein) gene product related to activating transcription factor 6 as a transcriptional activator of themammalianunfolded protein response. Biochem J 355: 19-28.
    • (2001) Biochem J , vol.355 , pp. 19-28
    • Haze, K.1    Okada, T.2    Yoshida, H.3    Yanagi, H.4    Yura, T.5
  • 33
    • 13944263299 scopus 로고    scopus 로고
    • OASIS, a CREB/ATF-family member, modulates UPR signalling in astrocytes
    • Kondo S, Murakami T, Tatsumi K, Ogata M, Kanemoto S, et al. (2005) OASIS, a CREB/ATF-family member, modulates UPR signalling in astrocytes. Nat Cell Biol 7: 186-194.
    • (2005) Nat Cell Biol , vol.7 , pp. 186-194
    • Kondo, S.1    Murakami, T.2    Tatsumi, K.3    Ogata, M.4    Kanemoto, S.5
  • 34
    • 20944445990 scopus 로고    scopus 로고
    • Tisp40, a spermatid specific bZip transcription factor, functions by binding to the unfolded protein response element via the Rip pathway
    • Nagamori I, Yabuta N, Fujii T, Tanaka H, Yomogida K, et al. (2005) Tisp40, a spermatid specific bZip transcription factor, functions by binding to the unfolded protein response element via the Rip pathway. Genes Cells 10: 575-594.
    • (2005) Genes Cells , vol.10 , pp. 575-594
    • Nagamori, I.1    Yabuta, N.2    Fujii, T.3    Tanaka, H.4    Yomogida, K.5
  • 35
    • 0036315042 scopus 로고    scopus 로고
    • Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis
    • Raggo C, Rapin N, Stirling J, Gobeil P, Smith-Windsor E, et al. (2002) Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis. Mol Cell Biol 22: 5639-5649.
    • (2002) Mol Cell Biol , vol.22 , pp. 5639-5649
    • Raggo, C.1    Rapin, N.2    Stirling, J.3    Gobeil, P.4    Smith-Windsor, E.5
  • 36
    • 32044453080 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response
    • Zhang K, Shen X, Wu J, Sakaki K, Saunders T, et al. (2006) Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response. Cell 124: 587-599.
    • (2006) Cell , vol.124 , pp. 587-599
    • Zhang, K.1    Shen, X.2    Wu, J.3    Sakaki, K.4    Saunders, T.5
  • 37
    • 0032509216 scopus 로고    scopus 로고
    • Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors
    • Yoshida H, Haze K, Yanagi H, Yura T, Mori K (1998) Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors. J Biol Chem 273: 33741-33749.
    • (1998) J Biol Chem , vol.273 , pp. 33741-33749
    • Yoshida, H.1    Haze, K.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 38
    • 0033118409 scopus 로고    scopus 로고
    • Complexes containing activating transcription factor (ATF)/cAMP- responsive-element-binding protein (CREB) interact with the CCAAT/enhancer- binding protein (C/EBP)-ATF composite site to regulate Gadd153 expression during the stress response
    • Fawcett TW, Martindale JL, Guyton KZ, Hai T, Holbrook NJ (1999) Complexes containing activating transcription factor (ATF)/cAMP-responsive-element- binding protein (CREB) interact with the CCAAT/enhancer-binding protein (C/EBP)-ATF composite site to regulate Gadd153 expression during the stress response. Biochem J 339: 135-141.
    • (1999) Biochem J , vol.339 , pp. 135-141
    • Fawcett, T.W.1    Martindale, J.L.2    Guyton, K.Z.3    Hai, T.4    Holbrook, N.J.5
  • 39
    • 0036314984 scopus 로고    scopus 로고
    • Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response
    • Ma Y, Brewer JW, Diehl JA, Hendershot LM (2002) Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response. J Mol Biol 318: 1351-1365.
    • (2002) J Mol Biol , vol.318 , pp. 1351-1365
    • Ma, Y.1    Brewer, J.W.2    Diehl, J.A.3    Hendershot, L.M.4
  • 40
    • 0032054744 scopus 로고    scopus 로고
    • CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum
    • Zinszner H, Kuroda M, Wang X, Batchvarova N, Lightfoot RT, et al. (1998) CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum. Genes Dev 12: 982-995.
    • (1998) Genes Dev , vol.12 , pp. 982-995
    • Zinszner, H.1    Kuroda, M.2    Wang, X.3    Batchvarova, N.4    Lightfoot, R.T.5
  • 41
    • 0037317592 scopus 로고    scopus 로고
    • Growth arrest and DNA damage-inducible protein GADD34 targets protein phosphatase 1 alpha to the endoplasmic reticulum and promotes dephosphorylation of the alpha subunit of eukaryotic translation initiation factor 2
    • Brush MH, Weiser DC, Shenolikar S (2003) Growth arrest and DNA damage-inducible protein GADD34 targets protein phosphatase 1 alpha to the endoplasmic reticulum and promotes dephosphorylation of the alpha subunit of eukaryotic translation initiation factor 2. Mol Cell Biol 23: 1292-1303.
    • (2003) Mol Cell Biol , vol.23 , pp. 1292-1303
    • Brush, M.H.1    Weiser, D.C.2    Shenolikar, S.3
  • 42
    • 0041703031 scopus 로고    scopus 로고
    • The function of GADD34 is a recovery from a shutoff of protein synthesis induced by ER stress: Elucidation by GADD34-deficient mice
    • Kojima E, Takeuchi A, Haneda M, Yagi A, Hasegawa T, et al. (2003) The function of GADD34 is a recovery from a shutoff of protein synthesis induced by ER stress: elucidation by GADD34-deficient mice. FASEB J 17: 1573-1575.
    • (2003) FASEB J , vol.17 , pp. 1573-1575
    • Kojima, E.1    Takeuchi, A.2    Haneda, M.3    Yagi, A.4    Hasegawa, T.5
  • 43
    • 0035947778 scopus 로고    scopus 로고
    • Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha
    • Novoa I, Zeng H, Harding HP, Ron D (2001) Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha. J Cell Biol 153: 1011-1022.
    • (2001) J Cell Biol , vol.153 , pp. 1011-1022
    • Novoa, I.1    Zeng, H.2    Harding, H.P.3    Ron, D.4
  • 44
    • 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, et al. (2004) CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum. Genes Dev 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
  • 45
    • 0035144493 scopus 로고    scopus 로고
    • Gadd153 sensitizes cells to endoplasmic reticulum stress by downregulating Bcl2 and perturbing the cellular redox state
    • McCullough KD, Martindale JL, Klotz LO, Aw TY, Holbrook NJ (2001) Gadd153 sensitizes cells to endoplasmic reticulum stress by downregulating Bcl2 and perturbing the cellular redox state. Mol Cell Biol 21: 1249-1259.
    • (2001) Mol Cell Biol , vol.21 , pp. 1249-1259
    • McCullough, K.D.1    Martindale, J.L.2    Klotz, L.O.3    Aw, T.Y.4    Holbrook, N.J.5
  • 46
    • 8544283103 scopus 로고    scopus 로고
    • CHOP is involved in endoplasmic reticulum stress-induced apoptosis by enhancing DR5 expression in human carcinoma cells
    • Yamaguchi H, Wang HG (2004) CHOP is involved in endoplasmic reticulum stress-induced apoptosis by enhancing DR5 expression in human carcinoma cells. J Biol Chem 279: 45495-45502.
    • (2004) J Biol Chem , vol.279 , pp. 45495-45502
    • Yamaguchi, H.1    Wang, H.G.2
  • 47
    • 31444449462 scopus 로고    scopus 로고
    • Role of the unfolded protein response in cell death
    • Kim R, Emi M, Tanabe K, Murakami S (2005) Role of the unfolded protein response in cell death. Apoptosis 11: 5-13.
    • (2005) Apoptosis , vol.11 , pp. 5-13
    • Kim, R.1    Emi, M.2    Tanabe, K.3    Murakami, S.4
  • 48
    • 33646373219 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced apoptosis: Multiple pathways and activation of p53-up-regulated modulator of apoptosis (PUMA) and NOXA by p53
    • Li J, Lee B, Lee AS (2006) Endoplasmic reticulum stress-induced apoptosis: Multiple pathways and activation of p53-up-regulated modulator of apoptosis (PUMA) and NOXA by p53. J Biol Chem 281: 7260-7270.
    • (2006) J Biol Chem , vol.281 , pp. 7260-7270
    • Li, J.1    Lee, B.2    Lee, A.S.3
  • 49
    • 26444442450 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress: Cell life and death decisions
    • Xu C, Bailly-Maitre B, Reed JC (2005) Endoplasmic reticulum stress: Cell life and death decisions. J Clin Invest 115: 2656-2664.
    • (2005) J Clin Invest , vol.115 , pp. 2656-2664
    • Xu, C.1    Bailly-Maitre, B.2    Reed, J.C.3
  • 50
    • 7744232493 scopus 로고    scopus 로고
    • Misfolded proteins, endoplasmic reticulum stress and neurodegeneration
    • Rao RV, Bredesen DE (2004) Misfolded proteins, endoplasmic reticulum stress and neurodegeneration. Curr Opin Cell Biol 16: 653-662.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 653-662
    • Rao, R.V.1    Bredesen, D.E.2
  • 51
    • 1842843860 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program
    • Rao RV, Ellerby HM, Bredesen DE (2004) Coupling endoplasmic reticulum stress to the cell death program. Cell Death Differ 11: 372-380.
    • (2004) Cell Death Differ , vol.11 , pp. 372-380
    • Rao, R.V.1    Ellerby, H.M.2    Bredesen, D.E.3
  • 52
    • 0842285401 scopus 로고    scopus 로고
    • Cytoprotection by pre-emptive conditional phosphorylation of translation initiation factor 2
    • Lu PD, Jousse C, Marciniak SJ, Zhang Y, Novoa I, et al. (2004) Cytoprotection by pre-emptive conditional phosphorylation of translation initiation factor 2. EMBO J 23: 169-179.
    • (2004) EMBO J , vol.23 , pp. 169-179
    • Lu, P.D.1    Jousse, C.2    Marciniak, S.J.3    Zhang, Y.4    Novoa, I.5
  • 53
    • 0345599024 scopus 로고    scopus 로고
    • Inhibition of a constitutive translation initiation factor 2alpha phosphatase, CReP, promotes survival of stressed cells
    • Jousse C, Oyadomari S, Novoa I, Lu P, Zhang Y, et al. (2003) Inhibition of a constitutive translation initiation factor 2alpha phosphatase, CReP, promotes survival of stressed cells. J Cell Biol 163: 767-775.
    • (2003) J Cell Biol , vol.163 , pp. 767-775
    • Jousse, C.1    Oyadomari, S.2    Novoa, I.3    Lu, P.4    Zhang, Y.5
  • 54
    • 0346331895 scopus 로고    scopus 로고
    • Stressed-out B cells? Plasma-cell differentiation and the unfolded protein response
    • Gass JN, Gunn KE, Sriburi R, Brewer JW (2004) Stressed-out B cells? Plasma-cell differentiation and the unfolded protein response. Trends Immunol 25: 17-24.
    • (2004) Trends Immunol , vol.25 , pp. 17-24
    • Gass, J.N.1    Gunn, K.E.2    Sriburi, R.3    Brewer, J.W.4
  • 55
    • 16244405250 scopus 로고    scopus 로고
    • Hepatitis C virus, ER stress, and oxidative stress
    • Tardif KD, Waris G, Siddiqui A (2005) Hepatitis C virus, ER stress, and oxidative stress. Trends Microbiol 13: 159-163.
    • (2005) Trends Microbiol , vol.13 , pp. 159-163
    • Tardif, K.D.1    Waris, G.2    Siddiqui, A.3
  • 56
    • 0036895383 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the development of diabetes: A review
    • Harding HP, Ron D (2002) Endoplasmic reticulum stress and the development of diabetes: A review. Diabetes 51: S455-S461.
    • (2002) Diabetes , vol.51
    • Harding, H.P.1    Ron, D.2
  • 57
    • 24644487812 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress response and neurodegeneration
    • Pachen W, Mengesdorf T (2005) Endoplasmic reticulum stress response and neurodegeneration. Cell Calcium 38: 409-415.
    • (2005) Cell Calcium , vol.38 , pp. 409-415
    • Pachen, W.1    Mengesdorf, T.2
  • 58
    • 0031960313 scopus 로고    scopus 로고
    • A tool coming of age: Thapsigargin as an inhibitor of sarco-endoplasmic reticulum Ca2+-ATPases
    • Treiman M, Caspersen C, Christensen SB (1998) A tool coming of age: Thapsigargin as an inhibitor of sarco-endoplasmic reticulum Ca2+-ATPases. Trends Parmacol Sci 19: 131-135.
    • (1998) Trends Parmacol Sci , vol.19 , pp. 131-135
    • Treiman, M.1    Caspersen, C.2    Christensen, S.B.3
  • 59
    • 0035937852 scopus 로고    scopus 로고
    • Oligosaccharide-based information in endoplasmic reticulum quality control and other biological systems
    • Lehrman MA (2001) Oligosaccharide-based information in endoplasmic reticulum quality control and other biological systems. J Biol Chem 276: 8623-8626.
    • (2001) J Biol Chem , vol.276 , pp. 8623-8626
    • Lehrman, M.A.1
  • 60
    • 0026636937 scopus 로고
    • Preferential synthesis of the 78-Kd glucose regulated protein in glucocorticoid-treated S49 mouse lymphoma cells
    • Lam M, Vimmerstedt LJ, Schlatter LK, Hensold JO, Distelhorst CW (1992) Preferential synthesis of the 78-Kd glucose regulated protein in glucocorticoid-treated S49 mouse lymphoma cells. Blood 79: 3285-3292.
    • (1992) Blood , vol.79 , pp. 3285-3292
    • Lam, M.1    Vimmerstedt, L.J.2    Schlatter, L.K.3    Hensold, J.O.4    Distelhorst, C.W.5
  • 61
    • 0027534594 scopus 로고
    • Relationship between defective mouse mammary tumor virus envelope glycoprotein synthesis and GRP78 synthesis in glucocorticoid-treated mouse lymphoma cells. Evidence for translational control of GRP78 synthesis
    • Ulatowski LM, Lam M, Vanderburg G, Stallcup MR, Distelhorst CW (1993) Relationship between defective mouse mammary tumor virus envelope glycoprotein synthesis and GRP78 synthesis in glucocorticoid-treated mouse lymphoma cells. Evidence for translational control of GRP78 synthesis. J Biol Chem 268: 7482-7488.
    • (1993) J Biol Chem , vol.268 , pp. 7482-7488
    • Ulatowski, L.M.1    Lam, M.2    Vanderburg, G.3    Stallcup, M.R.4    Distelhorst, C.W.5
  • 62
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard L, Helenius A (2003) Quality control in the endoplasmic reticulum. Nat Rev Mol Cell Biol 4: 181-191.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 63
    • 27944464985 scopus 로고    scopus 로고
    • Persistent glycoprotein misfolding activates the glucosidase II/UGT1-driven calnexin cycle to delay aggregation and loss of folding competence
    • Molinari M, Galli C, Vanoni O, Arnold SM, Kaufman RJ (2005) Persistent glycoprotein misfolding activates the glucosidase II/UGT1-driven calnexin cycle to delay aggregation and loss of folding competence. Mol Cell 20: 503-512.
    • (2005) Mol Cell , vol.20 , pp. 503-512
    • Molinari, M.1    Galli, C.2    Vanoni, O.3    Arnold, S.M.4    Kaufman, R.J.5
  • 64
    • 7444240833 scopus 로고    scopus 로고
    • The ER chaperone BiP is a master regulator of ER function
    • Hendershot LM (2004) The ER chaperone BiP is a master regulator of ER function. Mt Sinai J Med 71: 289-297.
    • (2004) Mt Sinai J Med , vol.71 , pp. 289-297
    • Hendershot, L.M.1
  • 65
    • 0031054643 scopus 로고    scopus 로고
    • Immunoglobulin binding protein (BiP) function is required to protect cells from endoplasmic reticulum stress but is not required for the secretion of selective proteins
    • Morris JA, Dorner AJ, Edwards CA, Hendershot L, Kaufman RJ (1997) Immunoglobulin binding protein (BiP) function is required to protect cells from endoplasmic reticulum stress but is not required for the secretion of selective proteins. J Biol Chem 272: 4327-4334.
    • (1997) J Biol Chem , vol.272 , pp. 4327-4334
    • Morris, J.A.1    Dorner, A.J.2    Edwards, C.A.3    Hendershot, L.4    Kaufman, R.J.5
  • 66
    • 0038182518 scopus 로고    scopus 로고
    • P58IPK, a novel endoplasmic reticulum stress-inducible protein and potential negative regulator of eIF2alpha signaling
    • van Huizen R, Martindale JL, Gorospe M, Holbrook NJ (2003) P58IPK, a novel endoplasmic reticulum stress-inducible protein and potential negative regulator of eIF2alpha signaling. J Biol Chem 278: 15558-15564.
    • (2003) J Biol Chem , vol.278 , pp. 15558-15564
    • Van Huizen, R.1    Martindale, J.L.2    Gorospe, M.3    Holbrook, N.J.4
  • 67
    • 0037058574 scopus 로고    scopus 로고
    • Control of PERK eIF2alpha kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK
    • Yan W, Frank CL, Korth MJ, Sopher BL, Novoa I, et al. (2002) Control of PERK eIF2alpha kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK. Proc Natl Acad Sci U S A 99: 15920-15925.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 15920-15925
    • Yan, W.1    Frank, C.L.2    Korth, M.J.3    Sopher, B.L.4    Novoa, I.5
  • 68
    • 1642442467 scopus 로고    scopus 로고
    • Underglycosylation of ATF6 as a novel sensing mechanism for activation of the unfolded protein response
    • Hong M, Luo S, Baumeister P, Huang JM, Gogia RK, et al. (2004) Underglycosylation of ATF6 as a novel sensing mechanism for activation of the unfolded protein response. J Biol Chem 279: 11354-11363.
    • (2004) J Biol Chem , vol.279 , pp. 11354-11363
    • Hong, M.1    Luo, S.2    Baumeister, P.3    Huang, J.M.4    Gogia, R.K.5
  • 69
    • 16644375815 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress triggers an acute proteasome-dependent degradation of ATF6
    • Hong M, Li M, Mao C, Lee AS (2004) Endoplasmic reticulum stress triggers an acute proteasome-dependent degradation of ATF6. J Cell Biochem 92: 723-732.
    • (2004) J Cell Biochem , vol.92 , pp. 723-732
    • Hong, M.1    Li, M.2    Mao, C.3    Lee, A.S.4
  • 70
    • 1842426663 scopus 로고    scopus 로고
    • Discordance of UPR signaling by ATF6 and Ire1p-XBP1 with levels of target transcripts
    • Shang J, Lehrman MA (2004) Discordance of UPR signaling by ATF6 and Ire1p-XBP1 with levels of target transcripts. Biochem Biophys Res Commun 317: 390-396.
    • (2004) Biochem Biophys Res Commun , vol.317 , pp. 390-396
    • Shang, J.1    Lehrman, M.A.2
  • 71
    • 0041853778 scopus 로고    scopus 로고
    • Protection of renal epithelial cells against oxidative injury by endoplasmic reticulum stress preconditioning is mediated by ERK1/2 activation
    • Hung CC, Ichimura T, Stevens JL, Bonventre JV (2003) Protection of renal epithelial cells against oxidative injury by endoplasmic reticulum stress preconditioning is mediated by ERK1/2 activation. J Biol Chem 278: 29317-29326.
    • (2003) J Biol Chem , vol.278 , pp. 29317-29326
    • Hung, C.C.1    Ichimura, T.2    Stevens, J.L.3    Bonventre, J.V.4
  • 72
    • 0041568574 scopus 로고    scopus 로고
    • Induction of GRP78 by ischemic preconditioning reduces endoplasmic reticulum stress and prevents delayed neuronal cell death
    • Hayashi T, Saito A, Okuno S, Ferrand-Drake M, Chan PH (2003) Induction of GRP78 by ischemic preconditioning reduces endoplasmic reticulum stress and prevents delayed neuronal cell death. J Cereb Blood Flow Metab 23: 949-961.
    • (2003) J Cereb Blood Flow Metab , vol.23 , pp. 949-961
    • Hayashi, T.1    Saito, A.2    Okuno, S.3    Ferrand-Drake, M.4    Chan, P.H.5
  • 73
    • 0032496358 scopus 로고    scopus 로고
    • The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes
    • Ferrell JE Jr, Machleder EM (1998) The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes. Science 280: 895-898.
    • (1998) Science , vol.280 , pp. 895-898
    • Ferrell Jr., J.E.1    Machleder, E.M.2
  • 74
    • 15544388848 scopus 로고    scopus 로고
    • Noise propagation in gene networks
    • Pedraza JM, van Oudenaarden A (2005) Noise propagation in gene networks. Science 307: 1965-1969.
    • (2005) Science , vol.307 , pp. 1965-1969
    • Pedraza, J.M.1    Van Oudenaarden, A.2
  • 75
    • 0036111831 scopus 로고    scopus 로고
    • Attenuation of noise in ultrasensitive signaling cascades
    • Thattai M, van Oudenaarden A (2002) Attenuation of noise in ultrasensitive signaling cascades. Biophys J 82: 2943-2950.
    • (2002) Biophys J , vol.82 , pp. 2943-2950
    • Thattai, M.1    Van Oudenaarden, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.