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Volumn 5, Issue APR, 2014, Pages

Physiological roles of regulated Ire1 dependent decay

Author keywords

Endoplasmic reticulum stress; Ire1; RIDD; Unfolded protein response; Xbp1

Indexed keywords

ENZYME; INOSITOL REQUIRING ENZYME 1; MEMBRANE PROTEIN; MESSENGER RNA; STRESS ACTIVATED PROTEIN KINASE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; X BOX BINDING PROTEIN 1;

EID: 84901053043     PISSN: None     EISSN: 16648021     Source Type: Journal    
DOI: 10.3389/fgene.2014.00076     Document Type: Article
Times cited : (94)

References (75)
  • 1
    • 34250794495 scopus 로고    scopus 로고
    • XBP1 controls diverse cell type- and condition-specific transcriptional regulatory networks
    • doi: 10.1016/j.molcel.2007.06.011
    • Acosta-Alvear, D., Zhou, Y., Blais, A., Tsikitis, M., Lents, N. H., Arias, C., et al. (2007). XBP1 controls diverse cell type- and condition-specific transcriptional regulatory networks. Mol. Cell 27, 53-66. doi: 10.1016/j.molcel.2007.06.011.
    • (2007) Mol. Cell , vol.27 , pp. 53-66
    • Acosta-Alvear, D.1    Zhou, Y.2    Blais, A.3    Tsikitis, M.4    Lents, N.H.5    Arias, C.6
  • 2
    • 59649092854 scopus 로고    scopus 로고
    • Messenger RNA targeting to endoplasmic reticulum stress signalling sites
    • doi: 10.1038/nature07641
    • Aragón, T., van Anken, E., Pincus, D., Serafimova, I. M., Korennykh, A. V., Rubio, C. A., et al. (2009). Messenger RNA targeting to endoplasmic reticulum stress signalling sites. Nature 457, 736-740. doi: 10.1038/nature07641.
    • (2009) Nature , vol.457 , pp. 736-740
    • Aragón, T.1    van Anken, E.2    Pincus, D.3    Serafimova, I.M.4    Korennykh, A.V.5    Rubio, C.A.6
  • 3
    • 84896048275 scopus 로고    scopus 로고
    • Regulated IRE1-dependent decay participates in curtailing immunoglobulin secretion from plasma cells
    • doi: 10.1002/eji.201343953
    • Benhamron, S., Hadar, R., Iwawaky, T., So, J.-S., Lee, A.-H., and Tirosh, B. (2014). Regulated IRE1-dependent decay participates in curtailing immunoglobulin secretion from plasma cells. Eur. J. Immunol. 44, 867-876. doi: 10.1002/eji.201343953 .
    • (2014) Eur. J. Immunol. , vol.44 , pp. 867-876
    • Benhamron, S.1    Hadar, R.2    Iwawaky, T.3    So, J.-S.4    Lee, A.-H.5    Tirosh, B.6
  • 4
    • 0037011917 scopus 로고    scopus 로고
    • IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
    • doi: 10.1038/415092a
    • Calfon, M., Zeng, H., Urano, F., Till, J. H., Hubbard, S. R., Harding, H. P., et al. (2002). IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature 415, 92-96. doi: 10.1038/415092a.
    • (2002) Nature , vol.415 , pp. 92-96
    • Calfon, M.1    Zeng, H.2    Urano, F.3    Till, J.H.4    Hubbard, S.R.5    Harding, H.P.6
  • 5
    • 0031282636 scopus 로고    scopus 로고
    • Translational attenuation mediated by an mRNA intron
    • doi: 10.1016/S0960-9822(06)00373-3
    • Chapman, R. E., and Walter, P. (1997). Translational attenuation mediated by an mRNA intron. Curr. Biol. 7, 850-859. doi: 10.1016/S0960-9822(06)00373-3.
    • (1997) Curr. Biol. , vol.7 , pp. 850-859
    • Chapman, R.E.1    Walter, P.2
  • 6
    • 84877870687 scopus 로고    scopus 로고
    • The unfolded protein response element IRE1α senses bacterial proteins invading the ER to activate RIG-I and innate immune signaling
    • doi: 10.1016/j.chom.2013.03.011
    • Cho, J. A., Lee, A.-H., Platzer, B., Cross, B. C. S., Gardner, B. M., De Luca, H., et al. (2013). The unfolded protein response element IRE1α senses bacterial proteins invading the ER to activate RIG-I and innate immune signaling. Cell Host Microbe 13, 558-569. doi: 10.1016/j.chom.2013.03.011.
    • (2013) Cell Host Microbe , vol.13 , pp. 558-569
    • Cho, J.A.1    Lee, A.-H.2    Platzer, B.3    Cross, B.C.S.4    Gardner, B.M.5    De Luca, H.6
  • 7
    • 84855320818 scopus 로고    scopus 로고
    • Protein quality control in the ER: balancing the ubiquitin checkbook
    • doi: 10.1016/j.tcb.2011.09.010
    • Claessen, J. H. L., Kundrat, L., and Ploegh, H. L. (2012). Protein quality control in the ER: balancing the ubiquitin checkbook. Trends Cell Biol. 22, 22-32. doi: 10.1016/j.tcb.2011.09.010.
    • (2012) Trends Cell Biol. , vol.22 , pp. 22-32
    • Claessen, J.H.L.1    Kundrat, L.2    Ploegh, H.L.3
  • 8
    • 84887609926 scopus 로고    scopus 로고
    • Xbp1-independent ire1 signaling is required for photoreceptor differentiation and rhabdomere morphogenesis in Drosophila
    • doi: 10.1016/j.celrep.2013.09.046
    • Coelho, D. S., Cairrão, F., Zeng, X., Pires, E., Coelho, A. V., Ron, D., et al. (2013). Xbp1-independent ire1 signaling is required for photoreceptor differentiation and rhabdomere morphogenesis in Drosophila. Cell Rep. 5, 791-801. doi: 10.1016/j.celrep.2013.09.046.
    • (2013) Cell Rep. , vol.5 , pp. 791-801
    • Coelho, D.S.1    Cairrão, F.2    Zeng, X.3    Pires, E.4    Coelho, A.V.5    Ron, D.6
  • 9
    • 0003779650 scopus 로고    scopus 로고
    • Washington, DC; Sunderland, MA: ASM Press; Sinauer Associates
    • Cooper, G. M. (2000). The Cell: A Molecular Approach. Washington, DC; Sunderland, MA: ASM Press; Sinauer Associates.
    • (2000) The Cell: A Molecular Approach
    • Cooper, G.M.1
  • 10
    • 0027324844 scopus 로고
    • Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase
    • doi: 10.1016/0092-8674(93)90648-A
    • Cox, J. S., Shamu, C. E., and Walter, P. (1993). Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 73, 1197-1206. doi: 10.1016/0092-8674(93)90648-A.
    • (1993) Cell , vol.73 , pp. 1197-1206
    • Cox, J.S.1    Shamu, C.E.2    Walter, P.3
  • 11
    • 0030297537 scopus 로고    scopus 로고
    • A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response
    • doi: 10.1016/S0092-8674(00)81360-4
    • Cox, J. S., and Walter, P. (1996). A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response. Cell 87, 391-404. doi: 10.1016/S0092-8674(00)81360-4.
    • (1996) Cell , vol.87 , pp. 391-404
    • Cox, J.S.1    Walter, P.2
  • 12
    • 84859587957 scopus 로고    scopus 로고
    • The molecular basis for selective inhibition of unconventional mRNA splicing by an IRE1-binding small molecule
    • doi: 10.1073/pnas.1115623109
    • Cross, B. C., Bond, P. J., Sadowski, P. G., Jha, B. K., Zak, J., Goodman, J. M., et al. (2012). The molecular basis for selective inhibition of unconventional mRNA splicing by an IRE1-binding small molecule. Proc. Natl. Acad. Sci. U. S. A. 109, E869-E878. doi: 10.1073/pnas.1115623109.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109
    • Cross, B.C.1    Bond, P.J.2    Sadowski, P.G.3    Jha, B.K.4    Zak, J.5    Goodman, J.M.6
  • 13
    • 84864603834 scopus 로고    scopus 로고
    • Drosophila fatty acid transport protein regulates rhodopsin-1 metabolism and is required for photoreceptor neuron survival
    • doi: 10.1371/journal.pgen.1002833
    • Dourlen, P., Bertin, B., Chatelain, G., Robin, M., Napoletano, F., Roux, M. J., et al. (2012). Drosophila fatty acid transport protein regulates rhodopsin-1 metabolism and is required for photoreceptor neuron survival. PLoS Genet. 8:e1002833. doi: 10.1371/journal.pgen.1002833.
    • (2012) PLoS Genet. , vol.8
    • Dourlen, P.1    Bertin, B.2    Chatelain, G.3    Robin, M.4    Napoletano, F.5    Roux, M.J.6
  • 14
    • 84871911924 scopus 로고    scopus 로고
    • Comparison of mRNA localization and regulation during endoplasmic reticulum stress in Drosophila cells
    • doi: 10.1091/mbc.E12-06-0491
    • Gaddam, D., Stevens, N., and Hollien, J. (2013). Comparison of mRNA localization and regulation during endoplasmic reticulum stress in Drosophila cells. Mol. Biol. Cell 24, 14-20. doi: 10.1091/mbc.E12-06-0491.
    • (2013) Mol. Biol. Cell , vol.24 , pp. 14-20
    • Gaddam, D.1    Stevens, N.2    Hollien, J.3
  • 16
    • 68049110633 scopus 로고    scopus 로고
    • IRE1alpha kinase activation modes control alternate endoribonuclease outputs to determine divergent cell fates
    • doi: 10.1016/j.cell.2009.07.017
    • Han, D., Lerner, A. G., Vande Walle, L., Upton, J.-P., Xu, W., Hagen, A., et al. (2009). IRE1alpha kinase activation modes control alternate endoribonuclease outputs to determine divergent cell fates. Cell 138, 562-575. doi: 10.1016/j.cell.2009.07.017.
    • (2009) Cell , vol.138 , pp. 562-575
    • Han, D.1    Lerner, A.G.2    Vande Walle, L.3    Upton, J.-P.4    Xu, W.5    Hagen, A.6
  • 17
    • 0036437307 scopus 로고    scopus 로고
    • Transcriptional and translational control in the Mammalian unfolded protein response
    • doi: 10.1146/annurev.cellbio.18.011402.160624
    • Harding, H. P., Calfon, M., Urano, F., Novoa, I., and Ron, D. (2002). Transcriptional and translational control in the Mammalian unfolded protein response. Annu. Rev. Cell Dev. Biol. 18, 575-599. doi: 10.1146/annurev.cellbio.18.011402.160624.
    • (2002) Annu. Rev. Cell Dev. Biol. , vol.18 , pp. 575-599
    • Harding, H.P.1    Calfon, M.2    Urano, F.3    Novoa, I.4    Ron, D.5
  • 18
    • 84870808965 scopus 로고    scopus 로고
    • Nonmuscle myosin IIB links cytoskeleton to IRE1α signaling during ER stress
    • doi: 10.1016/j.devcel.2012.11.006
    • He, Y., Beatty, A., Han, X., Ji, Y., Ma, X., Adelstein, R. S., et al. (2012). Nonmuscle myosin IIB links cytoskeleton to IRE1α signaling during ER stress. Dev. Cell 23, 1141-1152. doi: 10.1016/j.devcel.2012.11.006.
    • (2012) Dev. Cell , vol.23 , pp. 1141-1152
    • He, Y.1    Beatty, A.2    Han, X.3    Ji, Y.4    Ma, X.5    Adelstein, R.S.6
  • 19
    • 84856111924 scopus 로고    scopus 로고
    • The unfolded protein response: controlling cell fate decisions under ER stress and beyond
    • doi: 10.1038/nrm3270
    • Hetz, C. (2012). The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nat. Rev. Mol. Cell Biol. 13, 89-102. doi: 10.1038/nrm3270.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 89-102
    • Hetz, C.1
  • 20
    • 69749123786 scopus 로고    scopus 로고
    • Fine-tuning of the unfolded protein response: assembling the IRE1alpha interactome
    • doi: 10.1016/j.molcel.2009.08.021
    • Hetz, C., and Glimcher, L. H. (2009). Fine-tuning of the unfolded protein response: assembling the IRE1alpha interactome. Mol. Cell 35, 551-561. doi: 10.1016/j.molcel.2009.08.021.
    • (2009) Mol. Cell , vol.35 , pp. 551-561
    • Hetz, C.1    Glimcher, L.H.2
  • 21
    • 84880641508 scopus 로고    scopus 로고
    • Evolution of the unfolded protein response
    • doi: 10.1016/j.bbamcr.2013.01.016
    • Hollien, J. (2013). Evolution of the unfolded protein response. Biochim. Biophys. Acta 1833, 2458-2463. doi: 10.1016/j.bbamcr.2013.01.016.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 2458-2463
    • Hollien, J.1
  • 22
    • 68549092781 scopus 로고    scopus 로고
    • Regulated Ire1-dependent decay of messenger RNAs in mammalian cells
    • doi: 10.1083/jcb.200903014
    • Hollien, J., Lin, J. H., Li, H., Stevens, N., Walter, P., and Weissman, J. S. (2009). Regulated Ire1-dependent decay of messenger RNAs in mammalian cells. J. Cell Biol. 186, 323-331. doi: 10.1083/jcb.200903014.
    • (2009) J. Cell Biol. , vol.186 , pp. 323-331
    • Hollien, J.1    Lin, J.H.2    Li, H.3    Stevens, N.4    Walter, P.5    Weissman, J.S.6
  • 23
    • 33745893809 scopus 로고    scopus 로고
    • Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response
    • doi: 10.1126/science.1129631
    • Hollien, J., and Weissman, J. S. (2006). Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response. Science 313, 104-107. doi: 10.1126/science.1129631.
    • (2006) Science , vol.313 , pp. 104-107
    • Hollien, J.1    Weissman, J.S.2
  • 24
    • 84856856011 scopus 로고    scopus 로고
    • IRE1α activation protects mice against acetaminophen-induced hepatotoxicity
    • doi: 10.1084/jem.20111298
    • Hur, K. Y., So, J.-S., Ruda, V., Frank-Kamenetsky, M., Fitzgerald, K., Koteliansky, V., et al. (2012). IRE1α activation protects mice against acetaminophen-induced hepatotoxicity. J. Exp. Med. 209, 307-318. doi: 10.1084/jem.20111298.
    • (2012) J. Exp. Med. , vol.209 , pp. 307-318
    • Hur, K.Y.1    So, J.-S.2    Ruda, V.3    Frank-Kamenetsky, M.4    Fitzgerald, K.5    Koteliansky, V.6
  • 25
    • 42649125586 scopus 로고    scopus 로고
    • IRE1β inhibits chylomicron production by selectively degrading MTP mRNA
    • doi: 10.1016/j.cmet.2008.03.005
    • Iqbal, J., Dai, K., Seimon, T., Jungreis, R., Oyadomari, M., Kuriakose, G., et al. (2008). IRE1β inhibits chylomicron production by selectively degrading MTP mRNA. Cell Metab. 7, 445-455. doi: 10.1016/j.cmet.2008.03.005.
    • (2008) Cell Metab. , vol.7 , pp. 445-455
    • Iqbal, J.1    Dai, K.2    Seimon, T.3    Jungreis, R.4    Oyadomari, M.5    Kuriakose, G.6
  • 26
    • 84875857579 scopus 로고    scopus 로고
    • The unfolded protein response in fission yeast modulates stability of select mRNAs to maintain protein homeostasis
    • doi: 10.7554/eLife.00048
    • Kimmig, P., Diaz, M., Zheng, J., Williams, C. C., Lang, A., Aragón, T., et al. (2012). The unfolded protein response in fission yeast modulates stability of select mRNAs to maintain protein homeostasis. Elife 1:e00048. doi: 10.7554/eLife.00048.
    • (2012) Elife , vol.1
    • Kimmig, P.1    Diaz, M.2    Zheng, J.3    Williams, C.C.4    Lang, A.5    Aragón, T.6
  • 27
    • 0035197608 scopus 로고    scopus 로고
    • Molecular characterization of two Arabidopsis Ire1 homologs, endoplasmic reticulum-located transmembrane protein kinases
    • doi: 10.1104/pp.010636
    • Koizumi, N., Martinez, I. M., Kimata, Y., Kohno, K., Sano, H., and Chrispeels, M. J. (2001). Molecular characterization of two Arabidopsis Ire1 homologs, endoplasmic reticulum-located transmembrane protein kinases. Plant Physiol. 127, 949-962. doi: 10.1104/pp.010636.
    • (2001) Plant Physiol. , vol.127 , pp. 949-962
    • Koizumi, N.1    Martinez, I.M.2    Kimata, Y.3    Kohno, K.4    Sano, H.5    Chrispeels, M.J.6
  • 28
    • 59649111087 scopus 로고    scopus 로고
    • The unfolded protein response signals through high-order assembly of Ire1
    • doi: 10.1038/nature07661
    • Korennykh, A. V., Egea, P. F., Korostelev, A. A., Finer-Moore, J., Zhang, C., Shokat, K. M., et al. (2009). The unfolded protein response signals through high-order assembly of Ire1. Nature 457, 687-693. doi: 10.1038/nature07661.
    • (2009) Nature , vol.457 , pp. 687-693
    • Korennykh, A.V.1    Egea, P.F.2    Korostelev, A.A.3    Finer-Moore, J.4    Zhang, C.5    Shokat, K.M.6
  • 29
    • 79959902152 scopus 로고    scopus 로고
    • Cofactor-mediated conformational control in the bifunctional kinase/RNase Ire1
    • doi: 10.1186/1741-7007-9-48
    • Korennykh, A. V., Egea, P. F., Korostelev, A. A., Finer-Moore, J., Stroud, R. M., Zhang, C., et al. (2011a). Cofactor-mediated conformational control in the bifunctional kinase/RNase Ire1. BMC Biol. 9:48. doi: 10.1186/1741-7007-9-48.
    • (2011) BMC Biol. , vol.9 , pp. 48
    • Korennykh, A.V.1    Egea, P.F.2    Korostelev, A.A.3    Finer-Moore, J.4    Stroud, R.M.5    Zhang, C.6
  • 31
    • 84870159094 scopus 로고    scopus 로고
    • Structural basis of the unfolded protein response
    • doi: 10.1146/annurev-cellbio-101011-155826
    • Korennykh, A., and Walter, P. (2012). Structural basis of the unfolded protein response. Annu. Rev. Cell Dev. Biol. 28, 251-277. doi: 10.1146/annurev-cellbio-101011-155826.
    • (2012) Annu. Rev. Cell Dev. Biol. , vol.28 , pp. 251-277
    • Korennykh, A.1    Walter, P.2
  • 32
    • 79957773163 scopus 로고    scopus 로고
    • Dual and opposing roles of the unfolded protein response regulated by IRE1 and XBP1 in proinsulin processing and insulin secretion
    • doi: 10.1073/pnas.1105564108
    • Lee, A.-H., Heidtman, K., Hotamisligil, G. S., and Glimcher, L. H. (2011). Dual and opposing roles of the unfolded protein response regulated by IRE1 and XBP1 in proinsulin processing and insulin secretion. Proc. Natl. Acad. Sci. U.S.A. 108, 8885-8890. doi: 10.1073/pnas.1105564108.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 8885-8890
    • Lee, A.-H.1    Heidtman, K.2    Hotamisligil, G.S.3    Glimcher, L.H.4
  • 33
    • 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., and Glimcher, L. H. (2003). XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol. Cell. Biol. 23, 7448-7459. doi: 10.1128/MCB.23.21.7448-7459.2003.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7448-7459
    • Lee, A.-H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 34
    • 37649004940 scopus 로고    scopus 로고
    • Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation in nonconventional RNA splicing
    • doi: 10.1016/j.cell.2007.10.057
    • Lee, K. P. K., Dey, M., Neculai, D., Cao, C., Dever, T. E., and Sicheri, F. (2008). Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation in nonconventional RNA splicing. Cell 132, 89-100. doi: 10.1016/j.cell.2007.10.057.
    • (2008) Cell , vol.132 , pp. 89-100
    • Lee, K.P.K.1    Dey, M.2    Neculai, D.3    Cao, C.4    Dever, T.E.5    Sicheri, F.6
  • 35
    • 45749114525 scopus 로고    scopus 로고
    • The role of IRE1α in the degradation of insulin mRNA in pancreatic β-Cells
    • doi: 10.1371/journal.pone.0001648
    • Lipson, K. L., Ghosh, R., and Urano, F. (2008). The role of IRE1α in the degradation of insulin mRNA in pancreatic β-Cells. PLoS ONE 3:e1648. doi: 10.1371/journal.pone.0001648.
    • (2008) PLoS ONE , vol.3
    • Lipson, K.L.1    Ghosh, R.2    Urano, F.3
  • 36
    • 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., Schröder, M., and Kaufman, R. J. (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. doi: 10.1074/jbc.M004454200.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24881-24885
    • Liu, C.Y.1    Schröder, M.2    Kaufman, R.J.3
  • 37
    • 33749492425 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress signaling in disease
    • doi: 10.1152/physrev.00015.2006
    • Marciniak, S. J., and Ron, D. (2006). Endoplasmic reticulum stress signaling in disease. Physiol. Rev. 86, 1133-1149. doi: 10.1152/physrev.00015.2006.
    • (2006) Physiol. Rev. , vol.86 , pp. 1133-1149
    • Marciniak, S.J.1    Ron, D.2
  • 38
    • 33646365640 scopus 로고    scopus 로고
    • Central role of the scaffold protein tumor necrosis factor receptor-associated factor 2 in regulating endoplasmic reticulum stress-induced apoptosis
    • doi: 10.1074/jbc.M502181200
    • Mauro, C., Crescenzi, E., De Mattia, R., Pacifico, F., Mellone, S., Salzano, S., et al. (2006). Central role of the scaffold protein tumor necrosis factor receptor-associated factor 2 in regulating endoplasmic reticulum stress-induced apoptosis. J. Biol. Chem. 281, 2631-2638. doi: 10.1074/jbc.M502181200.
    • (2006) J. Biol. Chem. , vol.281 , pp. 2631-2638
    • Mauro, C.1    Crescenzi, E.2    De Mattia, R.3    Pacifico, F.4    Mellone, S.5    Salzano, S.6
  • 39
    • 84870166429 scopus 로고    scopus 로고
    • The unfolded protein response in secretory cell function
    • doi: 10.1146/annurev-genet-110711-155644
    • Moore, K. A., and Hollien, J. (2012). The unfolded protein response in secretory cell function. Annu. Rev. Genet. 46, 165-183. doi: 10.1146/annurev-genet-110711-155644.
    • (2012) Annu. Rev. Genet. , vol.46 , pp. 165-183
    • Moore, K.A.1    Hollien, J.2
  • 40
    • 84884278268 scopus 로고    scopus 로고
    • Regulation of sumo mRNA during endoplasmic reticulum stress
    • doi: 10.1371/journal.pone.0075723
    • Moore, K. A., Plant, J. J., Gaddam, D., Craft, J., and Hollien, J. (2013). Regulation of sumo mRNA during endoplasmic reticulum stress. PLoS ONE 8:e75723. doi: 10.1371/journal.pone.0075723.
    • (2013) PLoS ONE , vol.8
    • Moore, K.A.1    Plant, J.J.2    Gaddam, D.3    Craft, J.4    Hollien, J.5
  • 41
    • 0027305620 scopus 로고
    • A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus
    • doi: 10.1016/0092-8674(93)90521-Q
    • Mori, K., Ma, W., Gething, M. J., and Sambrook, J. (1993). A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus. Cell 74, 743-756. doi: 10.1016/0092-8674(93)90521-Q.
    • (1993) Cell , vol.74 , pp. 743-756
    • Mori, K.1    Ma, W.2    Gething, M.J.3    Sambrook, J.4
  • 42
    • 0030228708 scopus 로고    scopus 로고
    • Signalling from endoplasmic reticulum to nucleus: transcription factor with a basic-leucine zipper motif is required for the unfolded protein-response pathway
    • doi: 10.1046/j.1365-2443.1996.d01-274.x
    • Mori, K., Kawahara, T., Yoshida, H., Yanagi, H., and Yura, T. (1996). Signalling from endoplasmic reticulum to nucleus: transcription factor with a basic-leucine zipper motif is required for the unfolded protein-response pathway. Genes Cells 1, 803-817. doi: 10.1046/j.1365-2443.1996.d01-274.x.
    • (1996) Genes Cells , vol.1 , pp. 803-817
    • Mori, K.1    Kawahara, T.2    Yoshida, H.3    Yanagi, H.4    Yura, T.5
  • 43
    • 0026628290 scopus 로고
    • A 22 bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins
    • Mori, K., Sant, A., Kohno, K., Normington, K., Gething, M. J., and Sambrook, J. F. (1992). A 22 bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins. EMBO J. 11, 2583-2593.
    • (1992) EMBO J. , vol.11 , pp. 2583-2593
    • Mori, K.1    Sant, A.2    Kohno, K.3    Normington, K.4    Gething, M.J.5    Sambrook, J.F.6
  • 44
    • 58949093382 scopus 로고    scopus 로고
    • USP14 inhibits ER-associated degradation via interaction with IRE1alpha
    • doi: 10.1016/j.bbrc.2008.12.182
    • Nagai, A., Kadowaki, H., Maruyama, T., Takeda, K., Nishitoh, H., and Ichijo, H. (2009). USP14 inhibits ER-associated degradation via interaction with IRE1alpha. Biochem. Biophys. Res. Commun. 379, 995-1000. doi: 10.1016/j.bbrc.2008.12.182.
    • (2009) Biochem. Biophys. Res. Commun. , vol.379 , pp. 995-1000
    • Nagai, A.1    Kadowaki, H.2    Maruyama, T.3    Takeda, K.4    Nishitoh, H.5    Ichijo, H.6
  • 45
    • 0029860982 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae IRE2/HAC1 is involved in IRE1-mediated KAR2 expression
    • doi: 10.1093/nar/24.21.4222
    • Nikawa, J., Akiyoshi, M., Hirata, S., and Fukuda, T. (1996). Saccharomyces cerevisiae IRE2/HAC1 is involved in IRE1-mediated KAR2 expression. Nucleic Acids Res. 24, 4222-4226. doi: 10.1093/nar/24.21.4222.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4222-4226
    • Nikawa, J.1    Akiyoshi, M.2    Hirata, S.3    Fukuda, T.4
  • 46
    • 0036606540 scopus 로고    scopus 로고
    • ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
    • doi: 10.1101/gad.992302
    • Nishitoh, H., Matsuzawa, A., Tobiume, K., Saegusa, K., Takeda, K., Inoue, K., et al. (2002). ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev. 16, 1345-1355. doi: 10.1101/gad.992302.
    • (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
  • 47
    • 33845459165 scopus 로고    scopus 로고
    • Autophagy is activated for cell survival after endoplasmic reticulum stress
    • doi: 10.1128/MCB.01453-06
    • Ogata, M., Hino, S., Saito, A., Morikawa, K., Kondo, S., Kanemoto, S., et al. (2006). Autophagy is activated for cell survival after endoplasmic reticulum stress. Mol. Cell. Biol. 26, 9220-9231. doi: 10.1128/MCB.01453-06.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 9220-9231
    • Ogata, M.1    Hino, S.2    Saito, A.3    Morikawa, K.4    Kondo, S.5    Kanemoto, S.6
  • 48
    • 77956016131 scopus 로고    scopus 로고
    • Identification of a consensus element recognized and cleaved by IRE1
    • doi: 10.1093/nar/gkq452
    • Oikawa, D., Tokuda, M., Hosoda, A., and Iwawaki, T. (2010). Identification of a consensus element recognized and cleaved by IRE1. Nucleic Acids Res. 38, 6265-6273. doi: 10.1093/nar/gkq452.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 6265-6273
    • Oikawa, D.1    Tokuda, M.2    Hosoda, A.3    Iwawaki, T.4
  • 50
    • 0344395603 scopus 로고    scopus 로고
    • Bypassing a kinase activity with an ATP-competitive drug
    • doi: 10.1126/science.1090031
    • Papa, F. R., Zhang, C., Shokat, K., and Walter, P. (2003). Bypassing a kinase activity with an ATP-competitive drug. Science 302, 1533-1537. doi: 10.1126/science.1090031.
    • (2003) Science , vol.302 , pp. 1533-1537
    • Papa, F.R.1    Zhang, C.2    Shokat, K.3    Walter, P.4
  • 51
    • 59149090850 scopus 로고    scopus 로고
    • Role of JNK1-dependent Bcl-2 phosphorylation in ceramide-induced macroautophagy
    • doi: 10.1074/jbc.M805920200
    • Pattingre, S., Bauvy, C., Carpentier, S., Levade, T., Levine, B., and Codogno, P. (2009). Role of JNK1-dependent Bcl-2 phosphorylation in ceramide-induced macroautophagy. J. Biol. Chem. 284, 2719-2728. doi: 10.1074/jbc.M805920200.
    • (2009) J. Biol. Chem. , vol.284 , pp. 2719-2728
    • Pattingre, S.1    Bauvy, C.2    Carpentier, S.3    Levade, T.4    Levine, B.5    Codogno, P.6
  • 52
    • 65249141717 scopus 로고    scopus 로고
    • Rhabdomere biogenesis in Drosophila photoreceptors is acutely sensitive to phosphatidic acid levels
    • doi: 10.1083/jcb.200807027
    • Raghu, P., Coessens, E., Manifava, M., Georgiev, P., Pettitt, T., Wood, E., et al. (2009). Rhabdomere biogenesis in Drosophila photoreceptors is acutely sensitive to phosphatidic acid levels. J. Cell Biol. 185, 129-145. doi: 10.1083/jcb.200807027.
    • (2009) J. Cell Biol. , vol.185 , pp. 129-145
    • Raghu, P.1    Coessens, E.2    Manifava, M.3    Georgiev, P.4    Pettitt, T.5    Wood, E.6
  • 53
    • 68149136657 scopus 로고    scopus 로고
    • Cellular responses to endoplasmic reticulum stress and apoptosis
    • doi: 10.1007/s10495-009-0341-y
    • Rasheva, V. I., and Domingos, P. M. (2009). Cellular responses to endoplasmic reticulum stress and apoptosis. Apoptosis 14, 996-1007. doi: 10.1007/s10495-009-0341-y.
    • (2009) Apoptosis , vol.14 , pp. 996-1007
    • Rasheva, V.I.1    Domingos, P.M.2
  • 54
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • doi: 10.1038/nrm2199
    • Ron, D., and Walter, P. (2007). Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 8, 519-529. doi: 10.1038/nrm2199.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 55
    • 0035812716 scopus 로고    scopus 로고
    • Block of HAC1 mRNA translation by long-range base pairing is released by cytoplasmic splicing upon induction of the unfolded protein response
    • doi: 10.1016/S0092-8674(01)00505-0
    • Rüegsegger, U., Leber, J. H., and Walter, P. (2001). Block of HAC1 mRNA translation by long-range base pairing is released by cytoplasmic splicing upon induction of the unfolded protein response. Cell 107, 103-114. doi: 10.1016/S0092-8674(01)00505-0.
    • (2001) Cell , vol.107 , pp. 103-114
    • Rüegsegger, U.1    Leber, J.H.2    Walter, P.3
  • 56
    • 3142658576 scopus 로고    scopus 로고
    • XBP1, downstream of Blimp-1, expands the secretory apparatus and other organelles, and increases protein synthesis in plasma cell differentiation
    • doi: 10.1016/j.immuni.2004.06.010
    • Shaffer, A. L., Shapiro-Shelef, M., Iwakoshi, N. N., Lee, A.-H., Qian, S.-B., Zhao, H., et al. (2004). XBP1, downstream of Blimp-1, expands the secretory apparatus and other organelles, and increases protein synthesis in plasma cell differentiation. Immunity 21, 81-93. doi: 10.1016/j.immuni.2004.06.010.
    • (2004) Immunity , vol.21 , pp. 81-93
    • Shaffer, A.L.1    Shapiro-Shelef, M.2    Iwakoshi, N.N.3    Lee, A.-H.4    Qian, S.-B.5    Zhao, H.6
  • 57
    • 0029903049 scopus 로고    scopus 로고
    • Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus
    • Shamu, C. E., and Walter, P. (1996). Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus. EMBO J. 15, 3028-3039.
    • (1996) EMBO J. , vol.15 , pp. 3028-3039
    • Shamu, C.E.1    Walter, P.2
  • 58
    • 18244405070 scopus 로고    scopus 로고
    • Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development
    • doi: 10.1016/S0092-8674(01)00612-2
    • Shen, X., Ellis, R. E., Lee, K., Liu, C. Y., Yang, K., Solomon, A., et al. (2001). Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development. Cell 107, 893-903. doi: 10.1016/S0092-8674(01)00612-2.
    • (2001) Cell , vol.107 , pp. 893-903
    • Shen, X.1    Ellis, R.E.2    Lee, K.3    Liu, C.Y.4    Yang, K.5    Solomon, A.6
  • 59
    • 33745606008 scopus 로고    scopus 로고
    • Genetic interactions due to constitutive and inducible gene regulation mediated by the unfolded protein response in C. elegans
    • doi: 10.1371/journal.pgen.0010037
    • Shen, X., Ellis, R. E., Sakaki, K., and Kaufman, R. J. (2005). Genetic interactions due to constitutive and inducible gene regulation mediated by the unfolded protein response in C. elegans. PLoS Genet. 1:e37. doi: 10.1371/journal.pgen.0010037.
    • (2005) PLoS Genet. , vol.1
    • Shen, X.1    Ellis, R.E.2    Sakaki, K.3    Kaufman, R.J.4
  • 60
    • 84876991539 scopus 로고    scopus 로고
    • Stress-independent activation of XBP1s and/or ATF6 reveals three functionally diverse ER proteostasis environments
    • doi: 10.1016/j.celrep.2013.03.024
    • Shoulders, M. D., Ryno, L. M., Genereux, J. C., Moresco, J. J., Tu, P. G., Wu, C., et al. (2013). Stress-independent activation of XBP1s and/or ATF6 reveals three functionally diverse ER proteostasis environments. Cell Rep. 3, 1279-1292. doi: 10.1016/j.celrep.2013.03.024.
    • (2013) Cell Rep. , vol.3 , pp. 1279-1292
    • Shoulders, M.D.1    Ryno, L.M.2    Genereux, J.C.3    Moresco, J.J.4    Tu, P.G.5    Wu, C.6
  • 61
    • 0030297538 scopus 로고    scopus 로고
    • tRNA ligase is required for regulated mRNA splicing in the unfolded protein response
    • doi: 10.1016/S0092-8674(00)81361-6
    • Sidrauski, C., Cox, J. S., and Walter, P. (1996). tRNA ligase is required for regulated mRNA splicing in the unfolded protein response. Cell 87, 405-413. doi: 10.1016/S0092-8674(00)81361-6.
    • (1996) Cell , vol.87 , pp. 405-413
    • Sidrauski, C.1    Cox, J.S.2    Walter, P.3
  • 62
    • 0030954870 scopus 로고    scopus 로고
    • The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response
    • doi: 10.1016/S0092-8674(00)80369-4
    • Sidrauski, C., and Walter, P. (1997). The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response. Cell 90, 1031-1039. doi: 10.1016/S0092-8674(00)80369-4.
    • (1997) Cell , vol.90 , pp. 1031-1039
    • Sidrauski, C.1    Walter, P.2
  • 63
    • 82255161944 scopus 로고    scopus 로고
    • Road to ruin: targeting proteins for degradation in the endoplasmic reticulum
    • doi: 10.1126/science.1209235
    • Smith, M. H., Ploegh, H. L., and Weissman, J. S. (2011). Road to ruin: targeting proteins for degradation in the endoplasmic reticulum. Science 334, 1086-1090. doi: 10.1126/science.1209235.
    • (2011) Science , vol.334 , pp. 1086-1090
    • Smith, M.H.1    Ploegh, H.L.2    Weissman, J.S.3
  • 64
    • 84867038186 scopus 로고    scopus 로고
    • Silencing of lipid metabolism genes through IRE1α-mediated mRNA decay lowers plasma lipids in mice
    • doi: 10.1016/j.cmet.2012.09.004
    • So, J.-S., Hur, K. Y., Tarrio, M., Ruda, V., Frank-Kamenetsky, M., Fitzgerald, K., et al. (2012). Silencing of lipid metabolism genes through IRE1α-mediated mRNA decay lowers plasma lipids in mice. Cell Metab. 16, 487-499. doi: 10.1016/j.cmet.2012.09.004.
    • (2012) Cell Metab. , vol.16 , pp. 487-499
    • So, J.-S.1    Hur, K.Y.2    Tarrio, M.3    Ruda, V.4    Frank-Kamenetsky, M.5    Fitzgerald, K.6
  • 65
    • 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
    • doi: 10.1101/gad.12.12.1812
    • Tirasophon, W., Welihinda, A. A., and Kaufman, R. J. (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. doi: 10.1101/gad.12.12.1812.
    • (1998) Genes Dev. , vol.12 , pp. 1812-1824
    • Tirasophon, W.1    Welihinda, A.A.2    Kaufman, R.J.3
  • 66
    • 84874251933 scopus 로고    scopus 로고
    • Negative feedback by IRE1 optimizes mucin production in goblet cells
    • doi: 10.1073/pnas.1212484110
    • Tsuru, A., Fujimoto, N., Takahashi, S., Saito, M., Nakamura, D., Iwano, M., et al. (2013). Negative feedback by IRE1 optimizes mucin production in goblet cells. Proc. Natl. Acad. Sci. U.S.A. 110, 2864-2869. doi: 10.1073/pnas.1212484110.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 2864-2869
    • Tsuru, A.1    Fujimoto, N.2    Takahashi, S.3    Saito, M.4    Nakamura, D.5    Iwano, M.6
  • 67
    • 84868525253 scopus 로고    scopus 로고
    • IRE1α cleaves select microRNAs during ER stress to derepress translation of proapoptotic Caspase-2
    • doi: 10.1126/science.1226191
    • Upton, J.-P., Wang, L., Han, D., Wang, E. S., Huskey, N. E., Lim, L., et al. (2012). IRE1α cleaves select microRNAs during ER stress to derepress translation of proapoptotic Caspase-2. Science 338, 818-822. doi: 10.1126/science.1226191.
    • (2012) Science , vol.338 , pp. 818-822
    • Upton, J.-P.1    Wang, L.2    Han, D.3    Wang, E.S.4    Huskey, N.E.5    Lim, L.6
  • 68
    • 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., Wang, X., Bertolotti, A., Zhang, Y., Chung, P., Harding, H. P., et al. (2000). Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 287, 664-666. doi: 10.1126/science.287.5453.664.
    • (2000) Science , vol.287 , pp. 664-666
    • Urano, F.1    Wang, X.2    Bertolotti, A.3    Zhang, Y.4    Chung, P.5    Harding, H.P.6
  • 69
    • 84863740827 scopus 로고    scopus 로고
    • The impact of the unfolded protein response on human disease
    • doi: 10.1083/jcb.201110131
    • Wang, S., and Kaufman, R. J. (2012). The impact of the unfolded protein response on human disease. J. Cell Biol. 197, 857-867. doi: 10.1083/jcb.201110131.
    • (2012) J. Cell Biol. , vol.197 , pp. 857-867
    • Wang, S.1    Kaufman, R.J.2
  • 70
    • 0032190546 scopus 로고    scopus 로고
    • Cloning of mammalian Ire1 reveals diversity in the ER stress responses
    • doi: 10.1093/emboj/17.19.5708
    • Wang, X. Z., Harding, H. P., Zhang, Y., Jolicoeur, E. M., Kuroda, M., and Ron, D. (1998). Cloning of mammalian Ire1 reveals diversity in the ER stress responses. EMBO J. 17, 5708-5717. doi: 10.1093/emboj/17.19.5708.
    • (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    Ron, D.6
  • 71
    • 0029892851 scopus 로고    scopus 로고
    • The unfolded protein response pathway in Saccharomyces cerevisiae. Oligomerization and trans-phosphorylation of Ire1p (Ern1p) are required for kinase activation
    • doi: 10.1074/jbc.271.30.18181
    • Welihinda, A. A., and Kaufman, R. J. (1996). The unfolded protein response pathway in Saccharomyces cerevisiae. Oligomerization and trans-phosphorylation of Ire1p (Ern1p) are required for kinase activation. J. Biol. Chem. 271, 18181-18187. doi: 10.1074/jbc.271.30.18181.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18181-18187
    • Welihinda, A.A.1    Kaufman, R.J.2
  • 72
    • 64749103329 scopus 로고    scopus 로고
    • Cotranslational targeting of XBP1 protein to the membrane promotes cytoplasmic splicing of its own mRNA
    • doi: 10.1016/j.molcel.2009.02.033
    • Yanagitani, K., Imagawa, Y., Iwawaki, T., Hosoda, A., Saito, M., Kimata, Y., et al. (2009). Cotranslational targeting of XBP1 protein to the membrane promotes cytoplasmic splicing of its own mRNA. Mol. Cell 34, 191-200. doi: 10.1016/j.molcel.2009.02.033.
    • (2009) Mol. Cell , vol.34 , pp. 191-200
    • Yanagitani, K.1    Imagawa, Y.2    Iwawaki, T.3    Hosoda, A.4    Saito, M.5    Kimata, Y.6
  • 73
    • 79551629027 scopus 로고    scopus 로고
    • Translational pausing ensures membrane targeting and cytoplasmic splicing of XBP1u mRNA
    • doi: 10.1126/science.1197142
    • Yanagitani, K., Kimata, Y., Kadokura, H., and Kohno, K. (2011). Translational pausing ensures membrane targeting and cytoplasmic splicing of XBP1u mRNA. Science 331, 586-589. doi: 10.1126/science.1197142.
    • (2011) Science , vol.331 , pp. 586-589
    • Yanagitani, K.1    Kimata, Y.2    Kadokura, H.3    Kohno, K.4
  • 74
    • 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., and 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. doi: 10.1016/S0092-8674(01)00611-0.
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 75
    • 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., and Mori, K. (2006). 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. doi: 10.1083/jcb.200508145.
    • (2006) J. Cell Biol. , vol.172 , pp. 565-575
    • Yoshida, H.1    Oku, M.2    Suzuki, M.3    Mori, K.4


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