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Volumn 13, Issue 2, 2012, Pages 89-102

The unfolded protein response: Controlling cell fate decisions under ER stress and beyond

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 6; INOSITOL REQUIRING PROTEIN 1ALPHA; MESSENGER RNA; PROTEIN; PROTEIN KINASE; PROTEIN KINASE RNA LIKE ER KINASE; UNCLASSIFIED DRUG;

EID: 84856111924     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm3270     Document Type: Review
Times cited : (3068)

References (130)
  • 1
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • DOI 10.1038/nrm2199, PII NRM2199
    • Ron, D. & Walter, P. Signal integration in the endoplasmic reticulum unfolded protein response. Nature Rev. Mol. Cell Biol. 8, 519-529 (2007). (Pubitemid 46985379)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.7 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 2
    • 0023852783 scopus 로고
    • The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins
    • DOI 10.1038/332462a0
    • Kozutsumi, Y., Segal, M., Normington, K., Gething, M. J. & Sambrook, J. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 332, 462-464 (1988). (Pubitemid 18090252)
    • (1988) Nature , vol.332 , Issue.6163 , pp. 462-464
    • Kozutsumi, Y.1    Segal, M.2    Normington, K.3    Gething, M.-J.4    Sambrook, J.5
  • 3
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • DOI 10.1146/annurev.biochem.73.011303.074134
    • Schroder, M. & Kaufman, R. J. The mammalian unfolded protein response. Annu. Rev. Biochem. 74, 739-789 (2005). (Pubitemid 40995523)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 4
    • 80054722420 scopus 로고    scopus 로고
    • The unfolded protein response: Integrating stress signals through the stress sensor IRE1α
    • Hetz, C., Martinon, F., Rodriguez, D. & Glimcher, L. H. The unfolded protein response: integrating stress signals through the stress sensor IRE1α. Physiol. Rev. 91, 1219-1243 (2011).
    • (2011) Physiol. Rev. , vol.91 , pp. 1219-1243
    • Hetz, C.1    Martinon, F.2    Rodriguez, D.3    Glimcher, L.H.4
  • 5
    • 79958033194 scopus 로고    scopus 로고
    • Modulating stress responses by the UPRosome: A matter of life and death
    • Woehlbier, U. & Hetz, C. Modulating stress responses by the UPRosome: a matter of life and death. Trends Biochem. Sci. 36, 329-337 (2011).
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 329-337
    • Woehlbier, U.1    Hetz, C.2
  • 6
    • 77953153048 scopus 로고    scopus 로고
    • Regulation of basal cellular physiology by the homeostatic unfolded protein response
    • Rutkowski, D. T. & Hegde, R. S. Regulation of basal cellular physiology by the homeostatic unfolded protein response. J. Cell Biol. 189, 783-794 (2010).
    • (2010) J. Cell Biol. , vol.189 , pp. 783-794
    • Rutkowski, D.T.1    Hegde, R.S.2
  • 7
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding, H. P. et al. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol. Cell 6, 1099-1108 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1
  • 8
    • 68049110633 scopus 로고    scopus 로고
    • IRE1α kinase activation modes control alternate endoribonuclease outputs to determine divergent cell fates
    • Han, D. et al. IRE1α kinase activation modes control alternate endoribonuclease outputs to determine divergent cell fates. Cell 138, 562-575 (2009).
    • (2009) Cell , vol.138 , pp. 562-575
    • Han, D.1
  • 9
    • 68549092781 scopus 로고    scopus 로고
    • Regulated Ire1-dependent decay of messenger RNAs in mammalian cells
    • Hollien, J. et al. Regulated Ire1-dependent decay of messenger RNAs in mammalian cells. J. Cell Biol. 186, 323-331 (2009).
    • (2009) J. Cell Biol. , vol.186 , pp. 323-331
    • Hollien, J.1
  • 10
    • 33745893809 scopus 로고    scopus 로고
    • Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response
    • DOI 10.1126/science.1129631
    • Hollien, J. & Weissman, J. S. Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response. Science 313, 104-107 (2006). (Pubitemid 44051264)
    • (2006) Science , vol.313 , Issue.5783 , pp. 104-107
    • Hollien, J.1    Weissman, J.S.2
  • 11
    • 78649338141 scopus 로고    scopus 로고
    • Autophagy and the integrated stress response
    • Kroemer, G., Marino, G. & Levine, B. Autophagy and the integrated stress response. Mol. Cell 40, 280-293 (2010).
    • (2010) Mol. Cell , vol.40 , pp. 280-293
    • Kroemer, G.1    Marino, G.2    Levine, B.3
  • 12
    • 33751333201 scopus 로고    scopus 로고
    • Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway
    • Kang, S. W. et al. Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway. Cell 127, 999-1013 (2006).
    • (2006) Cell , vol.127 , pp. 999-1013
    • Kang, S.W.1
  • 14
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • Walter, P. & Ron, D. The unfolded protein response: from stress pathway to homeostatic regulation. Science 334, 1081-1086 (2011).
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 17
    • 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
    • DOI 10.1016/S0092-8674(01)00611-0
    • Yoshida, H., Matsui, T., Yamamoto, A., Okada, T. & Mori, K. 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). (Pubitemid 34084979)
    • (2001) Cell , vol.107 , Issue.7 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 18
    • 0142059951 scopus 로고    scopus 로고
    • XBP-1 Regulates a Subset of Endoplasmic Reticulum Resident Chaperone Genes in the Unfolded Protein Response
    • DOI 10.1128/MCB.23.21.7448-7459.2003
    • Lee, A. H., Iwakoshi, N. N. & Glimcher, L. H. XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol. Cell. Biol. 23, 7448-7459 (2003). (Pubitemid 37271447)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.21 , pp. 7448-7459
    • Lee, A.-H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 20
    • 79955424672 scopus 로고    scopus 로고
    • The signalling from endoplasmic reticulum-resident bZIP transcription factors involved in diverse cellular physiology
    • Asada, R., Kanemoto, S., Kondo, S., Saito, A. & Imaizumi, K. The signalling from endoplasmic reticulum-resident bZIP transcription factors involved in diverse cellular physiology. J. Biochem. 149, 507-518 (2011).
    • (2011) J. Biochem. , vol.149 , pp. 507-518
    • Asada, R.1    Kanemoto, S.2    Kondo, S.3    Saito, A.4    Imaizumi, K.5
  • 21
    • 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. 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). (Pubitemid 29534025)
    • (1999) Molecular Biology of the Cell , vol.10 , Issue.11 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 22
    • 34548172495 scopus 로고    scopus 로고
    • Transcriptional Induction of Mammalian ER Quality Control Proteins Is Mediated by Single or Combined Action of ATF6α and XBP1
    • DOI 10.1016/j.devcel.2007.07.018, PII S1534580707003000
    • Yamamoto, K. et al. Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6α and XBP1. Dev. Cell 13, 365-376 (2007). (Pubitemid 47308680)
    • (2007) Developmental Cell , vol.13 , Issue.3 , pp. 365-376
    • Yamamoto, K.1    Sato, T.2    Matsui, T.3    Sato, M.4    Okada, T.5    Yoshida, H.6    Harada, A.7    Mori, K.8
  • 24
    • 79955520100 scopus 로고    scopus 로고
    • A CHOP-regulated microRNA controls rhodopsin expression
    • Behrman, S., Acosta-Alvear, D. & Walter, P. A CHOP-regulated microRNA controls rhodopsin expression. J. Cell Biol. 192, 919-927 (2011).
    • (2011) J. Cell Biol. , vol.192 , pp. 919-927
    • Behrman, S.1    Acosta-Alvear, D.2    Walter, P.3
  • 25
    • 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. Nature Cell Biol. 13, 184-190 (2011).
    • (2011) Nature Cell Biol. , vol.13 , pp. 184-190
    • Tabas, I.1    Ron, D.2
  • 26
    • 77956095537 scopus 로고    scopus 로고
    • Mitochondria and cell death: Outer membrane permeabilization and beyond
    • Tait, S. W. & Green, D. R. Mitochondria and cell death: outer membrane permeabilization and beyond. Nature Rev. Mol. Cell Biol. 11, 621-632 (2010).
    • (2010) Nature Rev. Mol. Cell Biol. , vol.11 , pp. 621-632
    • Tait, S.W.1    Green, D.R.2
  • 27
    • 69749123786 scopus 로고    scopus 로고
    • Fine-tuning of the unfolded protein response: Assembling the IRE1α interactome
    • Hetz, C. & Glimcher, L. H. Fine-tuning of the unfolded protein response: assembling the IRE1α interactome. Mol. Cell 35, 551-561 (2009).
    • (2009) Mol. Cell , vol.35 , pp. 551-561
    • Hetz, C.1    Glimcher, L.H.2
  • 28
    • 0034723235 scopus 로고    scopus 로고
    • Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1
    • DOI 10.1126/science.287.5453.664
    • Urano, F. et al. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 287, 664-666 (2000). (Pubitemid 30070916)
    • (2000) Science , vol.287 , Issue.5453 , pp. 664-666
    • Urano, F.1    Wang, X.2    Bertolotti, A.3    Zhang, Y.4    Chung, P.5    Harding, H.P.6    Ron, D.7
  • 30
    • 78149339310 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis pathogenesis: A journey through the secretory pathway
    • Nassif, M., Matus, S., Castillo, K. & Hetz, C. Amyotrophic lateral sclerosis pathogenesis: a journey through the secretory pathway. Antioxid. Redox Signal. 13, 1955-1989 (2010).
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 1955-1989
    • Nassif, M.1    Matus, S.2    Castillo, K.3    Hetz, C.4
  • 31
    • 79953146630 scopus 로고    scopus 로고
    • Selective abrogation of BiP/GRP78 blunts activation of NF-κB through the ATF6 branch of the UPR: Involvement of C/EBPβ and mTOR-dependent dephosphorylation of Akt
    • Nakajima, S. et al. Selective abrogation of BiP/GRP78 blunts activation of NF-κB through the ATF6 branch of the UPR: involvement of C/EBPβ and mTOR-dependent dephosphorylation of Akt. Mol. Cell. Biol. 31, 1710-1718 (2011).
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 1710-1718
    • Nakajima, S.1
  • 32
    • 79954426601 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-sensing mechanisms in yeast and mammalian cells
    • Kimata, Y. & Kohno, K. Endoplasmic reticulum stress-sensing mechanisms in yeast and mammalian cells. Curr. Opin. Cell Biol. 23, 135-142 (2011).
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 135-142
    • Kimata, Y.1    Kohno, K.2
  • 33
    • 77958016968 scopus 로고    scopus 로고
    • Mammalian endoplasmic reticulum stress sensor IRE1 signals by dynamic clustering
    • Li, H., Korennykh, A. V., Behrman, S. L. & Walter, P. Mammalian endoplasmic reticulum stress sensor IRE1 signals by dynamic clustering. Proc. Natl Acad. Sci. USA 107, 16113-16118 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 16113-16118
    • Li, H.1    Korennykh, A.V.2    Behrman, S.L.3    Walter, P.4
  • 34
    • 59649111087 scopus 로고    scopus 로고
    • The unfolded protein response signals through high-order assembly of Ire1
    • Korennykh, A. V. et al. The unfolded protein response signals through high-order assembly of Ire1. Nature 457, 687-693 (2009).
    • (2009) Nature , vol.457 , pp. 687-693
    • Korennykh, A.V.1
  • 35
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • Bertolotti, A., Zhang, Y., Hendershot, L. M., Harding, H. P. & Ron, D. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nature Cell Biol. 2, 326-332 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 326-332
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5
  • 36
    • 0036069980 scopus 로고    scopus 로고
    • ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of golgi localization signals
    • DOI 10.1016/S1534-5807(02)00203-4
    • Shen, J., Chen, X., Hendershot, L. & Prywes, R. ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev. Cell 3, 99-111 (2002). (Pubitemid 34778399)
    • (2002) Developmental Cell , vol.3 , Issue.1 , pp. 99-111
    • Shen, J.1    Chen, X.2    Hendershot, L.3    Prywes, R.4
  • 37
    • 70449577164 scopus 로고    scopus 로고
    • In vitro reconstitution of ER-stress induced ATF6 transport in COPII vesicles
    • Schindler, A. J. & Schekman, R. In vitro reconstitution of ER-stress induced ATF6 transport in COPII vesicles. Proc. Natl Acad. Sci. USA 106, 17775-17780 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 17775-17780
    • Schindler, A.J.1    Schekman, R.2
  • 39
    • 33846223428 scopus 로고    scopus 로고
    • Role of disulfide bridges formed in the luminal domain of ATF6 in sensing endoplasmic reticulum stress
    • DOI 10.1128/MCB.00408-06
    • Nadanaka, S., Okada, T., Yoshida, H. & Mori, K. Role of disulfide bridges formed in the luminal domain of ATF6 in sensing endoplasmic reticulum stress. Mol. Cell. Biol. 27, 1027-1043 (2007). (Pubitemid 46174565)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.3 , pp. 1027-1043
    • Nadanaka, S.1    Okada, T.2    Yoshida, H.3    Mori, K.4
  • 41
    • 80053369081 scopus 로고    scopus 로고
    • Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response
    • Gardner, B. M. & Walter, P. Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response. Science 333, 1891-1894 (2011).
    • (2011) Science , vol.333 , pp. 1891-1894
    • Gardner, B.M.1    Walter, P.2
  • 42
    • 67651045789 scopus 로고    scopus 로고
    • Activation of mammalian IRE1α upon ER stress depends on dissociation of BiP rather than on direct interaction with unfolded proteins
    • Oikawa, D., Kimata, Y., Kohno, K. & Iwawaki, T. Activation of mammalian IRE1α upon ER stress depends on dissociation of BiP rather than on direct interaction with unfolded proteins. Exp. Cell Res. 315, 2496-2504 (2009).
    • (2009) Exp. Cell Res. , vol.315 , pp. 2496-2504
    • Oikawa, D.1    Kimata, Y.2    Kohno, K.3    Iwawaki, T.4
  • 44
  • 45
    • 33745590436 scopus 로고    scopus 로고
    • Intrinsic capacities of molecular sensors of the unfolded protein response to sense alternate forms of endoplasmic reticulum stress
    • DOI 10.1091/mbc.E06-01-0055
    • DuRose, J. B., Tam, A. B. & Niwa, M. Intrinsic capacities of molecular sensors of the unfolded protein response to sense alternate forms of endoplasmic reticulum stress. Mol. Biol. Cell 17, 3095-3107 (2006). (Pubitemid 43993512)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.7 , pp. 3095-3107
    • DuRose, J.B.1    Tam, A.B.2    Niwa, M.3
  • 46
    • 79956352017 scopus 로고    scopus 로고
    • Selective activation of the transcription factor ATF6 mediates endoplasmic reticulum proliferation triggered by a membrane protein
    • Maiuolo, J., Bulotta, S., Verderio, C., Benfante, R. & Borgese, N. Selective activation of the transcription factor ATF6 mediates endoplasmic reticulum proliferation triggered by a membrane protein. Proc. Natl Acad. Sci. USA 108, 7832-7837 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 7832-7837
    • Maiuolo, J.1    Bulotta, S.2    Verderio, C.3    Benfante, R.4    Borgese, N.5
  • 47
    • 79957773163 scopus 로고    scopus 로고
    • Dual and opposing roles of the unfolded protein response regulated by IRE1α and XBP1 in proinsulin processing and insulin secretion
    • Lee, A. H., Heidtman, K., Hotamisligil, G. S. & Glimcher, L. H. Dual and opposing roles of the unfolded protein response regulated by IRE1α and XBP1 in proinsulin processing and insulin secretion. Proc. Natl Acad. Sci. USA 108, 8885-8890 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 8885-8890
    • Lee, A.H.1    Heidtman, K.2    Hotamisligil, G.S.3    Glimcher, L.H.4
  • 48
    • 45749114525 scopus 로고    scopus 로고
    • The role of IRE1α in the degradation of insulin mRNA in pancreatic β-cells
    • Lipson, K. L., Ghosh, R. & Urano, F. The role of IRE1α in the degradation of insulin mRNA in pancreatic β-cells. PLoS ONE 3, e1648 (2008).
    • (2008) PLoS ONE , vol.3
    • Lipson, K.L.1    Ghosh, R.2    Urano, F.3
  • 50
    • 0034637605 scopus 로고    scopus 로고
    • Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum
    • DOI 10.1074/jbc.M004454200
    • Liu, C. Y., Schroder, M. & Kaufman, R. J. 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). (Pubitemid 30626593)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.32 , pp. 24881-24885
    • Chuan Yin Liu1    Schroder, M.2    Kaufman, R.J.3
  • 52
    • 58449084895 scopus 로고    scopus 로고
    • Divergent effects of PERK and IRE1 signaling on cell viability
    • Lin, J. H., Li, H., Zhang, Y., Ron, D. & Walter, P. Divergent effects of PERK and IRE1 signaling on cell viability. PLoS ONE 4, e4170 (2009).
    • (2009) PLoS ONE , vol.4
    • Lin, J.H.1    Li, H.2    Zhang, Y.3    Ron, D.4    Walter, P.5
  • 53
    • 77955023666 scopus 로고    scopus 로고
    • BiP binding to the ER-stress sensor Ire1 tunes the homeostatic behavior of the unfolded protein response
    • Pincus, D. et al. BiP binding to the ER-stress sensor Ire1 tunes the homeostatic behavior of the unfolded protein response. PLoS Biol. 8, e1000415 (2010).
    • (2010) PLoS Biol. , vol.8
    • Pincus, D.1
  • 54
    • 79955499906 scopus 로고    scopus 로고
    • Homeostatic adaptation to endoplasmic reticulum stress depends on Ire1 kinase activity
    • Rubio, C. et al. Homeostatic adaptation to endoplasmic reticulum stress depends on Ire1 kinase activity. J. Cell Biol. 193, 171-184 (2011).
    • (2011) J. Cell Biol. , vol.193 , pp. 171-184
    • Rubio, C.1
  • 55
    • 79955508656 scopus 로고    scopus 로고
    • Attenuation of yeast UPR is essential for survival and is mediated by IRE1 kinase
    • Chawla, A., Chakrabarti, S., Ghosh, G. & Niwa, M. Attenuation of yeast UPR is essential for survival and is mediated by IRE1 kinase. J. Cell Biol. 193, 41-50 (2011).
    • (2011) J. Cell Biol. , vol.193 , pp. 41-50
    • Chawla, A.1    Chakrabarti, S.2    Ghosh, G.3    Niwa, M.4
  • 56
    • 33751069967 scopus 로고    scopus 로고
    • Adaptation to ER stress is mediated by differential stabilities of pro-survival and pro-apoptotic mRNAs and proteins
    • Rutkowski, D. T. et al. Adaptation to ER stress is mediated by differential stabilities of pro-survival and pro-apoptotic mRNAs and proteins. PLoS Biol. 4, e374 (2006).
    • (2006) PLoS Biol. , vol.4
    • Rutkowski, D.T.1
  • 57
    • 33646237823 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK modulate the unfolded protein response by a direct interaction with IRE1α
    • Hetz, C. et al. Proapoptotic BAX and BAK modulate the unfolded protein response by a direct interaction with IRE1α. Science 312, 572-576 (2006).
    • (2006) Science , vol.312 , pp. 572-576
    • Hetz, C.1
  • 58
    • 77955044180 scopus 로고    scopus 로고
    • HSP72 protects cells from ER stress-induced apoptosis via enhancement of IRE1α-XBP1 signaling through a physical interaction
    • Gupta, S. et al. HSP72 protects cells from ER stress-induced apoptosis via enhancement of IRE1α-XBP1 signaling through a physical interaction. PLoS Biol. 8, e1000410 (2010).
    • (2010) PLoS Biol. , vol.8
    • Gupta, S.1
  • 59
  • 60
    • 45549103421 scopus 로고    scopus 로고
    • AIP 1 is critical in transducing IRE1-mediated endoplasmic reticulum stress response
    • Luo, D. et al. AIP1 is critical in transducing IRE1-mediated endoplasmic reticulum stress response. J. Biol. Chem. 283, 11905-11912 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 11905-11912
    • Luo, D.1
  • 61
    • 0035957929 scopus 로고    scopus 로고
    • Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress
    • Yoneda, T. et al. Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress. J. Biol. Chem. 276, 13935-13940 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 13935-13940
    • Yoneda, T.1
  • 63
    • 62549129467 scopus 로고    scopus 로고
    • BAX inhibitor-1 is a negative regulator of the ER stress sensor IRE1α
    • Lisbona, F. et al. BAX inhibitor-1 is a negative regulator of the ER stress sensor IRE1α. Mol. Cell 33, 679-691 (2009).
    • (2009) Mol. Cell , vol.33 , pp. 679-691
    • Lisbona, F.1
  • 64
    • 33644515957 scopus 로고    scopus 로고
    • Cytoprotective gene bi-1 is required for intrinsic protection from endoplasmic reticulum stress and ischemia-reperfusion injury
    • Bailly-Maitre, B. et al. Cytoprotective gene bi-1 is required for intrinsic protection from endoplasmic reticulum stress and ischemia-reperfusion injury. Proc. Natl Acad. Sci. USA 103, 2809-2814 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 2809-2814
    • Bailly-Maitre, B.1
  • 65
    • 77949883045 scopus 로고    scopus 로고
    • Hepatic Bax inhibitor-1 inhibits IRE1α and protects from obesity-associated insulin resistance and glucose intolerance
    • Bailly-Maitre, B. et al. Hepatic Bax inhibitor-1 inhibits IRE1α and protects from obesity-associated insulin resistance and glucose intolerance. J. Biol. Chem. 285, 6198-6207 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 6198-6207
    • Bailly-Maitre, B.1
  • 66
    • 78651385207 scopus 로고    scopus 로고
    • BAR, an endoplasmic reticulum-associated E3 ubiquitin ligase, modulates BI-1 protein stability and function in ER stress
    • Rong, J. et al. BAR, an endoplasmic reticulum-associated E3 ubiquitin ligase, modulates BI-1 protein stability and function in ER stress. J. Biol. Chem. 286, 1453-1463 (2010).
    • (2010) J. Biol. Chem. , vol.286 , pp. 1453-1463
    • Rong, J.1
  • 67
    • 84855696465 scopus 로고    scopus 로고
    • MTORC1 serves ER stress-triggered apoptosis via selective activation of the IRE1-JNK pathway
    • 22 Jul doi:10.1038/cdd.2011.98
    • Kato, H. et al. mTORC1 serves ER stress-triggered apoptosis via selective activation of the IRE1-JNK pathway. Cell Death Differ. 22 Jul 2011 (doi:10.1038/cdd.2011.98).
    • (2011) Cell Death Differ.
    • Kato, H.1
  • 68
    • 77950887221 scopus 로고    scopus 로고
    • Flavonol activation defines an unanticipated ligand-binding site in the kinase-RNase domain of IRE1
    • Wiseman, R. L. et al. Flavonol activation defines an unanticipated ligand-binding site in the kinase-RNase domain of IRE1. Mol. Cell 38, 291-304.
    • Mol. Cell , vol.38 , pp. 291-304
    • Wiseman, R.L.1
  • 69
    • 79959902152 scopus 로고    scopus 로고
    • Cofactor-mediated conformational control in the bifunctional kinase/RNase Ire1
    • Korennykh, A. V. et al. Cofactor-mediated conformational control in the bifunctional kinase/RNase Ire1. BMC Biol. 9, 48 (2011).
    • (2011) BMC Biol. , vol.9 , pp. 48
    • Korennykh, A.V.1
  • 70
    • 80052825784 scopus 로고    scopus 로고
    • Membrane aberrancy and unfolded proteins activate the endoplasmic reticulum-stress sensor Ire1 by different manners
    • Ishiwata-Kimata, Y. et al. Membrane aberrancy and unfolded proteins activate the endoplasmic reticulum-stress sensor Ire1 by different manners. Mol. Biol. Cell 22, 3520-3532 (2011).
    • (2011) Mol. Biol. Cell , vol.22 , pp. 3520-3532
    • Ishiwata-Kimata, Y.1
  • 71
    • 80052668828 scopus 로고    scopus 로고
    • Peptides derived from the bifunctional kinase/RNase enzyme IRE1α modulate IRE1α activity and protect cells from endoplasmic reticulum stress
    • Bouchecareilh, M., Higa, A., Fribourg, S., Moenner, M. & Chevet, E. Peptides derived from the bifunctional kinase/RNase enzyme IRE1α modulate IRE1α activity and protect cells from endoplasmic reticulum stress. FASEB J. 25, 3115-3129 (2011).
    • (2011) FASEB J. , vol.25 , pp. 3115-3129
    • Bouchecareilh, M.1    Higa, A.2    Fribourg, S.3    Moenner, M.4    Chevet, E.5
  • 72
    • 0038182518 scopus 로고    scopus 로고
    • IPK, a novel endoplasmic reticulum stress-inducible protein and potential negative regulator of eIF2α signaling
    • DOI 10.1074/jbc.M212074200
    • van Huizen, R., Martindale, J. L., Gorospe, M. & Holbrook, N. J. P58IPK, a novel endoplasmic reticulum stress-inducible protein and potential negative regulator of eIF2α signaling. J. Biol. Chem. 278, 15558-15564 (2003). (Pubitemid 36799663)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.18 , pp. 15558-15564
    • Van Huizen, R.1    Martindale, J.L.2    Gorospe, M.3    Holbrook, N.J.4
  • 74
    • 69949170481 scopus 로고    scopus 로고
    • Regulation of PERK signaling and leukemic cell survival by a novel cytosolic isoform of the UPR regulator GRP78/BiP
    • Ni, M., Zhou, H., Wey, S., Baumeister, P. & Lee, A. S. Regulation of PERK signaling and leukemic cell survival by a novel cytosolic isoform of the UPR regulator GRP78/BiP. PLoS ONE 4, e6868 (2009).
    • (2009) PLoS ONE , vol.4
    • Ni, M.1    Zhou, H.2    Wey, S.3    Baumeister, P.4    Lee, A.S.5
  • 75
    • 77957758520 scopus 로고    scopus 로고
    • Calcineurin interacts with PERK and dephosphorylates calnexin to relieve ER stress in mammals and frogs
    • Bollo, M. et al. Calcineurin interacts with PERK and dephosphorylates calnexin to relieve ER stress in mammals and frogs. PLoS ONE 5, e11925 (2010).
    • (2010) PLoS ONE , vol.5
    • Bollo, M.1
  • 76
    • 77949751415 scopus 로고    scopus 로고
    • Wolfram syndrome 1 gene negatively regulates ER stress signaling in rodent and human cells
    • Fonseca, S. G. et al. Wolfram syndrome 1 gene negatively regulates ER stress signaling in rodent and human cells. J. Clin. Invest. 120, 744-755 (2010).
    • (2010) J. Clin. Invest. , vol.120 , pp. 744-755
    • Fonseca, S.G.1
  • 77
    • 0033815971 scopus 로고    scopus 로고
    • ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response
    • Yoshida, H. et al. ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response. Mol. Cell. Biol. 20, 6755-6767 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6755-6767
    • Yoshida, H.1
  • 78
    • 50249159442 scopus 로고    scopus 로고
    • CBF/NF-Y controls endoplasmic reticulum stress induced transcription through recruitment of both ATF6(N) and TBP
    • Luo, R., Lu, J. F., Hu, Q. & Maity, S. N. CBF/NF-Y controls endoplasmic reticulum stress induced transcription through recruitment of both ATF6(N) and TBP. J. Cell Biochem. 104, 1708-1723 (2008).
    • (2008) J. Cell Biochem. , vol.104 , pp. 1708-1723
    • Luo, R.1    Lu, J.F.2    Hu, Q.3    Maity, S.N.4
  • 79
    • 0033920261 scopus 로고    scopus 로고
    • ATF6 as a transcription activator of the endoplasmic reticulum stress element: Thapsigargin stress-induced changes and synergistic interactions with NF-Y and YY1
    • DOI 10.1128/MCB.20.14.5096-5106.2000
    • Li, M. et al. ATF6 as a transcription activator of the endoplasmic reticulum stress element: thapsigargin stress-induced changes and synergistic interactions with NF-Y and YY1. Mol. Cell. Biol. 20, 5096-5106 (2000). (Pubitemid 30431563)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.14 , pp. 5096-5106
    • Li, M.1    Baumeister, P.2    Roy, B.3    Phan, T.4    Foti, D.5    Luo, S.6    Lee, A.S.7
  • 80
    • 79953870477 scopus 로고    scopus 로고
    • Luminal domain of ATF6 alone is sufficient for sensing endoplasmic reticulum stress and subsequent transport to the Golgi apparatus
    • Sato, Y., Nadanaka, S., Okada, T., Okawa, K. & Mori, K. Luminal domain of ATF6 alone is sufficient for sensing endoplasmic reticulum stress and subsequent transport to the Golgi apparatus. Cell Struct. Funct. 36, 35-47 (2011).
    • (2011) Cell Struct. Funct. , vol.36 , pp. 35-47
    • Sato, Y.1    Nadanaka, S.2    Okada, T.3    Okawa, K.4    Mori, K.5
  • 81
    • 64749103329 scopus 로고    scopus 로고
    • Cotranslational targeting of XBP1 protein to the membrane promotes cytoplasmic splicing of its own mRNA
    • Yanagitani, K. et al. Cotranslational targeting of XBP1 protein to the membrane promotes cytoplasmic splicing of its own mRNA. Mol. Cell 34, 191-200 (2009).
    • (2009) Mol. Cell , vol.34 , pp. 191-200
    • Yanagitani, K.1
  • 82
    • 79551629027 scopus 로고    scopus 로고
    • Translational pausing ensures membrane targeting and cytoplasmic splicing of XBP1u mRNA
    • Yanagitani, K., Kimata, Y., Kadokura, H. & Kohno, K. Translational pausing ensures membrane targeting and cytoplasmic splicing of XBP1u mRNA. Science 331, 586-589 (2011).
    • (2011) Science , vol.331 , pp. 586-589
    • Yanagitani, K.1    Kimata, Y.2    Kadokura, H.3    Kohno, K.4
  • 83
    • 77950523710 scopus 로고    scopus 로고
    • The regulatory subunits of PI3K, p85α and p85β, interact with XBP-1 and increase its nuclear translocation
    • Park, S. W. et al. The regulatory subunits of PI3K, p85α and p85β, interact with XBP-1 and increase its nuclear translocation. Nature Med. 16, 429-437 (2010).
    • (2010) Nature Med. , vol.16 , pp. 429-437
    • Park, S.W.1
  • 84
    • 77950537400 scopus 로고    scopus 로고
    • A regulatory subunit of phosphoinositide 3-kinase increases the nuclear accumulation of X-box-binding protein-1 to modulate the unfolded protein response
    • Winnay, J. N., Boucher, J., Mori, M. A., Ueki, K. & Kahn, C. R. A regulatory subunit of phosphoinositide 3-kinase increases the nuclear accumulation of X-box-binding protein-1 to modulate the unfolded protein response. Nature Med. 16, 438-445 (2010).
    • (2010) Nature Med. , vol.16 , pp. 438-445
    • Winnay, J.N.1    Boucher, J.2    Mori, M.A.3    Ueki, K.4    Kahn, C.R.5
  • 85
    • 80053985758 scopus 로고    scopus 로고
    • P38 MAPK-mediated regulation of Xbp1s is crucial for glucose homeostasis
    • Lee, J. et al. p38 MAPK-mediated regulation of Xbp1s is crucial for glucose homeostasis. Nature Med. 17, 1251-1260 (2011).
    • (2011) Nature Med. , vol.17 , pp. 1251-1260
    • Lee, J.1
  • 86
    • 79551474362 scopus 로고    scopus 로고
    • Regulation of unfolded protein response modulator XBP1s by acetylation and deacetylation
    • Wang, F. M. & Ouyang, H. J. Regulation of unfolded protein response modulator XBP1s by acetylation and deacetylation. Biochem. J. 433, 245-252 (2010).
    • (2010) Biochem. J. , vol.433 , pp. 245-252
    • Wang, F.M.1    Ouyang, H.J.2
  • 87
    • 77954525706 scopus 로고    scopus 로고
    • SUMO modification regulates the transcriptional activity of XBP1
    • Chen, H. & Qi, L. SUMO modification regulates the transcriptional activity of XBP1. Biochem. J. 429, 95-102 (2010).
    • (2010) Biochem. J. , vol.429 , pp. 95-102
    • Chen, H.1    Qi, L.2
  • 88
    • 32644432826 scopus 로고    scopus 로고
    • PXBP1(U) encoded in XBP1 pre-mRNA negatively regulates unfolded protein response activator pXBP1(S) in mammalian ER stress response
    • DOI 10.1083/jcb.200508145
    • Yoshida, H., Oku, M., Suzuki, M. & Mori, K. pXBP1(U) encoded in XBP1 pre-mRNA negatively regulates unfolded protein response activator pXBP1(S) in mammalian ER stress response. J. Cell Biol. 172, 565-575 (2006). (Pubitemid 43243877)
    • (2006) Journal of Cell Biology , vol.172 , Issue.4 , pp. 565-575
    • Yoshida, H.1    Oku, M.2    Suzuki, M.3    Mori, K.4
  • 89
    • 0035947778 scopus 로고    scopus 로고
    • Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2α
    • Novoa, I., Zeng, H., Harding, H. P. & Ron, D. Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2α. J. Cell Biol. 153, 1011-1022 (2001).
    • (2001) J. Cell Biol. , vol.153 , pp. 1011-1022
    • Novoa, I.1    Zeng, H.2    Harding, H.P.3    Ron, D.4
  • 91
    • 79953288480 scopus 로고    scopus 로고
    • Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis
    • Tsaytler, P., Harding, H. P., Ron, D. & Bertolotti, A. Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis. Science 332, 91-94 (2011).
    • (2011) Science , vol.332 , pp. 91-94
    • Tsaytler, P.1    Harding, H.P.2    Ron, D.3    Bertolotti, A.4
  • 92
    • 81755184374 scopus 로고    scopus 로고
    • The eIF2 kinase PERK and the integrated stress response facilitate activation of ATF6 during endoplasmic reticulum stress
    • Teske, B. F. et al. The eIF2 kinase PERK and the integrated stress response facilitate activation of ATF6 during endoplasmic reticulum stress. Mol. Biol. Cell 22, 4390-4405 (2011).
    • (2011) Mol. Biol. Cell , vol.22 , pp. 4390-4405
    • Teske, B.F.1
  • 93
    • 79951676940 scopus 로고    scopus 로고
    • Regulation of innate immunity by signaling pathways emerging from the endoplasmic reticulum
    • Martinon, F. & Glimcher, L. H. Regulation of innate immunity by signaling pathways emerging from the endoplasmic reticulum. Curr. Opin. Immunol. 23, 35-40 (2011).
    • (2011) Curr. Opin. Immunol. , vol.23 , pp. 35-40
    • Martinon, F.1    Glimcher, L.H.2
  • 94
    • 77951290227 scopus 로고    scopus 로고
    • TLR activation of the transcription factor XBP1 regulates innate immune responses in macrophages
    • Martinon, F., Chen, X., Lee, A.-H. & Glimcher, L. H. TLR activation of the transcription factor XBP1 regulates innate immune responses in macrophages. Nature Immunol. 11, 411-418 (2010).
    • (2010) Nature Immunol. , vol.11 , pp. 411-418
    • Martinon, F.1    Chen, X.2    Lee, A.-H.3    Glimcher, L.H.4
  • 95
    • 73349141743 scopus 로고    scopus 로고
    • Adaptive suppression of the ATF4-CHOP branch of the unfolded protein response by toll-like receptor signalling
    • Woo, C. W. et al. Adaptive suppression of the ATF4-CHOP branch of the unfolded protein response by toll-like receptor signalling. Nature Cell Biol. 11, 1473-1480 (2009).
    • (2009) Nature Cell Biol. , vol.11 , pp. 1473-1480
    • Woo, C.W.1
  • 96
    • 77950343252 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the inflammatory basis of metabolic disease
    • Hotamisligil, G. S. Endoplasmic reticulum stress and the inflammatory basis of metabolic disease. Cell 140, 900-917 (2010).
    • (2010) Cell , vol.140 , pp. 900-917
    • Hotamisligil, G.S.1
  • 97
    • 33747849846 scopus 로고    scopus 로고
    • Regulation of insulin biosynthesis in pancreatic beta cells by an endoplasmic reticulum-resident protein kinase IRE1
    • DOI 10.1016/j.cmet.2006.07.007, PII S1550413106002701
    • Lipson, K. L. et al. Regulation of insulin biosynthesis in pancreatic β cells by an endoplasmic reticulum-resident protein kinase IRE1. Cell Metab. 4, 245-254 (2006). (Pubitemid 44283955)
    • (2006) Cell Metabolism , vol.4 , Issue.3 , pp. 245-254
    • Lipson, K.L.1    Fonseca, S.G.2    Ishigaki, S.3    Nguyen, L.X.4    Foss, E.5    Bortell, R.6    Rossini, A.A.7    Urano, F.8
  • 98
    • 77951645463 scopus 로고    scopus 로고
    • A crucial role for RACK1 in the regulation of glucose-stimulated IRE1α activation in pancreatic β cells
    • Qiu, Y. et al. A crucial role for RACK1 in the regulation of glucose-stimulated IRE1α activation in pancreatic β cells. Sci. Signal. 3, ra7 (2010).
    • (2010) Sci. Signal. , vol.3
    • Qiu, Y.1
  • 100
    • 79957605136 scopus 로고    scopus 로고
    • Aberrant lipid metabolism disrupts calcium homeostasis causing liver endoplasmic reticulum stress in obesity
    • Fu, S. et al. Aberrant lipid metabolism disrupts calcium homeostasis causing liver endoplasmic reticulum stress in obesity. Nature 473, 528-531 (2011).
    • (2011) Nature , vol.473 , pp. 528-531
    • Fu, S.1
  • 103
    • 29244448729 scopus 로고    scopus 로고
    • XBP-1 is required for biogenesis of cellular secretory machinery of exocrine glands
    • DOI 10.1038/sj.emboj.7600903
    • Lee, A. H., Chu, G. C., Iwakoshi, N. N. & Glimcher, L. H. XBP-1 is required for biogenesis of cellular secretory machinery of exocrine glands. EMBO J. 24, 4368-4380 (2005). (Pubitemid 41828911)
    • (2005) EMBO Journal , vol.24 , Issue.24 , pp. 4368-4380
    • Lee, A.-H.1    Chu, G.C.2    Iwakoshi, N.N.3    Glimcher, L.H.4
  • 104
    • 77958590030 scopus 로고    scopus 로고
    • Disruption causes histological abnormality of exocrine tissues, increase of blood glucose level, and decrease of serum immunoglobulin level
    • Iwawaki, T., Akai, R. & Kohno, K. IRE1α disruption causes histological abnormality of exocrine tissues, increase of blood glucose level, and decrease of serum immunoglobulin level. PLoS ONE 5, e13052 (2010).
    • (2010) PLoS ONE , vol.5
    • Iwawaki, T.1    Akai, R.2    Ire, K.K.3
  • 105
    • 78649688693 scopus 로고    scopus 로고
    • XBP1 controls maturation of gastric zymogenic cells by induction of MIST1 and expansion of the rough endoplasmic reticulum
    • Huh, W. J. et al. XBP1 controls maturation of gastric zymogenic cells by induction of MIST1 and expansion of the rough endoplasmic reticulum. Gastroenterology 139, 2038-2049 (2010).
    • (2010) Gastroenterology , vol.139 , pp. 2038-2049
    • Huh, W.J.1
  • 106
    • 0034968330 scopus 로고    scopus 로고
    • Diabetes mellitus and exocrine pancreatic dysfunction in Perk-/- mice reveals a role for translational control in secretory cell survival
    • DOI 10.1016/S1097-2765(01)00264-7
    • Harding, H. P. et al. Diabetes mellitus and exocrine pancreatic dysfunction in perk-/-mice reveals a role for translational control in secretory cell survival. Mol. Cell 7, 1153-1163 (2001). (Pubitemid 32607350)
    • (2001) Molecular Cell , vol.7 , Issue.6 , pp. 1153-1163
    • Harding, H.P.1    Zeng, H.2    Zhang, Y.3    Jungries, R.4    Chung, P.5    Plesken, H.6    Sabatini, D.D.7    Ron, D.8
  • 107
    • 67349176043 scopus 로고    scopus 로고
    • XBP-1 regulates signal transduction, transcription factors and bone marrow colonization in B cells
    • Hu, C., Dougan, S., McGehee, A., Love, J. & Ploegh, H. XBP-1 regulates signal transduction, transcription factors and bone marrow colonization in B cells. EMBO J. (2009).
    • (2009) EMBO J.
    • Hu, C.1    Dougan, S.2    McGehee, A.3    Love, J.4    Ploegh, H.5
  • 109
    • 33947274572 scopus 로고    scopus 로고
    • Surviving endoplasmic reticulum stress is coupled to altered chondrocyte differentiation and function
    • Tsang, K. Y. et al. Surviving endoplasmic reticulum stress is coupled to altered chondrocyte differentiation and function. PLoS Biol. 5, e44 (2007).
    • (2007) PLoS Biol. , vol.5
    • Tsang, K.Y.1
  • 110
    • 45849137877 scopus 로고    scopus 로고
    • Regulation of hepatic lipogenesis by the transcription factor XBP1
    • DOI 10.1126/science.1158042
    • Lee, A.-H., Scapa, E., Cohen, D. & Glimcher, L. Regulation of hepatic lipogenesis by the transcription factor XBP1. Science 320, 1492-1496 (2008). (Pubitemid 351929428)
    • (2008) Science , vol.320 , Issue.5882 , pp. 1492-1496
    • Lee, A.-H.1    Scapa, E.F.2    Cohen, D.E.3    Glimcher, L.H.4
  • 111
    • 77956232915 scopus 로고    scopus 로고
    • Induction of liver steatosis and lipid droplet formation in ATF6α-knockout mice burdened with pharmacological endoplasmic reticulum stress
    • Yamamoto, K. et al. Induction of liver steatosis and lipid droplet formation in ATF6α-knockout mice burdened with pharmacological endoplasmic reticulum stress. Mol. Biol. Cell 21, 2975-2986 (2010).
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2975-2986
    • Yamamoto, K.1
  • 112
    • 79953794116 scopus 로고    scopus 로고
    • The unfolded protein response transducer IRE1α prevents ER stress-induced hepatic steatosis
    • Zhang, K. et al. The unfolded protein response transducer IRE1α prevents ER stress-induced hepatic steatosis. EMBO J. 30, 1357-1375 (2011).
    • (2011) EMBO J. , vol.30 , pp. 1357-1375
    • Zhang, K.1
  • 113
    • 68949220321 scopus 로고    scopus 로고
    • ER stress controls iron metabolism through induction of hepcidin
    • Vecchi, C. et al. ER stress controls iron metabolism through induction of hepcidin. Science 325, 877-880 (2009).
    • (2009) Science , vol.325 , pp. 877-880
    • Vecchi, C.1
  • 114
    • 79952381078 scopus 로고    scopus 로고
    • Regulation of glucose homeostasis through a XBP-1-FoxO1 interaction
    • Zhou, Y. et al. Regulation of glucose homeostasis through a XBP-1-FoxO1 interaction. Nature Med. 17, 356-365 (2011).
    • (2011) Nature Med. , vol.17 , pp. 356-365
    • Zhou, Y.1
  • 115
    • 77953091249 scopus 로고    scopus 로고
    • Insulin/IGF-1 signaling mutants reprogram ER stress response regulators to promote longevity
    • Henis-Korenblit, S. et al. Insulin/IGF-1 signaling mutants reprogram ER stress response regulators to promote longevity. Proc. Natl Acad. Sci. USA 107, 9730-9735 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 9730-9735
    • Henis-Korenblit, S.1
  • 116
    • 67749135249 scopus 로고    scopus 로고
    • The CREB coactivator CRTC2 links hepatic ER stress and fasting gluconeogenesis
    • Wang, Y., Vera, L., Fischer, W. H. & Montminy, M. The CREB coactivator CRTC2 links hepatic ER stress and fasting gluconeogenesis. Nature 460, 534-537 (2009).
    • (2009) Nature , vol.460 , pp. 534-537
    • Wang, Y.1    Vera, L.2    Fischer, W.H.3    Montminy, M.4
  • 118
    • 79951629888 scopus 로고    scopus 로고
    • Animal models in the study of the unfolded protein response
    • Bommiasamy, H. & Popko, B. Animal models in the study of the unfolded protein response. Meth. Enzymol. 491, 91-109 (2011).
    • (2011) Meth. Enzymol. , vol.491 , pp. 91-109
    • Bommiasamy, H.1    Popko, B.2
  • 119
    • 79954416866 scopus 로고    scopus 로고
    • Protein homeostasis networks in physiology and disease
    • Hetz, C. & Glimcher, L. H. Protein homeostasis networks in physiology and disease. Curr. Opin. Cell Biol. 23, 123-125 (2011).
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 123-125
    • Hetz, C.1    Glimcher, L.H.2
  • 121
    • 70349756962 scopus 로고    scopus 로고
    • Function of IRE1α in the placenta is essential for placental development and embryonic viability
    • Iwawaki, T., Akai, R., Yamanaka, S. & Kohno, K. Function of IRE1α in the placenta is essential for placental development and embryonic viability. Proc. Natl Acad. Sci. USA 106, 16657-16662 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 16657-16662
    • Iwawaki, T.1    Akai, R.2    Yamanaka, S.3    Kohno, K.4
  • 122
    • 35548935675 scopus 로고    scopus 로고
    • The unfolded protein response of B-lymphocytes: PERK-independent development of antibody-secreting cells
    • DOI 10.1016/j.molimm.2007.07.029, PII S0161589007006554
    • Gass, J. N., Jiang, H. Y., Wek, R. C. & Brewer, J. W. The unfolded protein response of B-lymphocytes: PERK-independent development of antibody-secreting cells. Mol. Immunol. 45, 1035-1043 (2008). (Pubitemid 350016334)
    • (2008) Molecular Immunology , vol.45 , Issue.4 , pp. 1035-1043
    • Gass, J.N.1    Jiang, H.-Y.2    Wek, R.C.3    Brewer, J.W.4
  • 125
    • 79954425809 scopus 로고    scopus 로고
    • Protein folding stress in neurodegenerative diseases: A glimpse into the ER
    • Matus, S., Glimcher, L. H. & Hetz, C. Protein folding stress in neurodegenerative diseases: a glimpse into the ER. Curr. Opin. Cell Biol. 23, 239-252 (2011).
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 239-252
    • Matus, S.1    Glimcher, L.H.2    Hetz, C.3
  • 126
    • 67349164383 scopus 로고    scopus 로고
    • A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice
    • Saxena, S., Cabuy, E. & Caroni, P. A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice. Nature Neurosci. 12, 627-636 (2009).
    • (2009) Nature Neurosci. , vol.12 , pp. 627-636
    • Saxena, S.1    Cabuy, E.2    Caroni, P.3
  • 127
    • 79551584057 scopus 로고    scopus 로고
    • The unfolded protein response in familial amyotrophic lateral sclerosis
    • Wang, L., Popko, B. & Roos, R. P. The unfolded protein response in familial amyotrophic lateral sclerosis. Hum. Mol. Genet. 20, 1008-1015 (2011).
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 1008-1015
    • Wang, L.1    Popko, B.2    Roos, R.P.3
  • 128
    • 70349627027 scopus 로고    scopus 로고
    • XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy
    • Hetz, C. et al. XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy. Genes Dev. 23, 2294-2306 (2009).
    • (2009) Genes Dev. , vol.23 , pp. 2294-2306
    • Hetz, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.