References
- Acosta-Alvear, D., Zhou, Y., Blais, A., Tsikitis, M., Lents, N.H., Arias, C., Lennon, C.J., Kluger, Y., and Dynlacht, B.D. (2007). XBP1 controls diverse cell type- and condition-specific transcriptional regulatory networks. Mol. Cell 27, 53-66. https://doi.org/10.1016/j.molcel.2007.06.011
- Adachi, Y., Yamamoto, K., Okada, T., Yoshida, H., Harada, A., and Mori, K. (2008). ATF6 is a transcription factor specializing in the regulation of quality control proteins in the endoplasmic reticulum. Cell Struct. Funct. 33, 75-89. https://doi.org/10.1247/csf.07044
- Ansa-Addo, E.A., Thaxton, J., Hong, F., Wu, B.X., Zhang, Y., Fugle, C.W., Metelli, A., Riesenberg, B., Williams, K., Gewirth, D.T., et al. (2016). Clients and oncogenic roles of molecular chaperone gp96/grp94. Curr. Top. Med. Chem. 16, 2765-2778. https://doi.org/10.2174/1568026616666160413141613
- Bertolotti, A., Zhang, Y., Hendershot, L.M., Harding, H.P., and Ron, D. (2000). Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat. Cell Biol. 2, 326-332. https://doi.org/10.1038/35014014
- Bettigole, S.E., and Glimcher, L.H. (2015). Endoplasmic reticulum stress in immunity. Annu. Rev. Immunol. 33, 107-138. https://doi.org/10.1146/annurev-immunol-032414-112116
- Bettigole, S.E., Lis, R., Adoro, S., Lee, A.-H., Spencer, L.A., Weller, P.F., and Glimcher, L.H. (2015). The transcription factor XBP1 is selectively required for eosinophil differentiation. Nat. Immunol. 16, 829-837. https://doi.org/10.1038/ni.3225
- Braakman, I., and Bulleid, N.J. (2011). Protein folding and modification in the mammalian endoplasmic reticulum. Annu. Rev. Biochem. 80, 71-99. https://doi.org/10.1146/annurev-biochem-062209-093836
-
Brucklacher-Waldert, V., Ferreira, C., Stebegg, M., Fesneau, O., Innocentin, S., Marie, J.C., and Veldhoen, M. (2017). Cellular stress in the context of an inflammatory environment supports TGF-
${\beta}$ -independent T helper-17 differentiation. Cell Rep. 19, 2357-2370. https://doi.org/10.1016/j.celrep.2017.05.052 - Byrd, A.E., and Brewer, J.W. (2012). Intricately regulated: a cellular toolbox for fine-tuning XBP1 expression and activity. Cells 1, 738-753. https://doi.org/10.3390/cells1040738
- Calfon, M., Zeng, H., Urano, F., Till, J.H., Hubbard, S.R., Harding, H.P., Clark, S.G., and Ron, D. (2002). IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature 415, 92-96. https://doi.org/10.1038/415092a
- Cao, S.S., Luo, K.L., and Shi, L. (2016). Endoplasmic reticulum stress interacts with inflammation in human diseases. J. Cell. Physiol. 231, 288-294. https://doi.org/10.1002/jcp.25098
- Chen, X., Karnovsky, A., Sans, M.D., Andrews, P.C., and Williams, J.A. (2010). Molecular characterization of the endoplasmic reticulum: insights from proteomic studies. Proteomics 10, 4040-4052. https://doi.org/10.1002/pmic.201000234
- Coelho, D.S., and Domingos, P.M. (2014). Physiological roles of regulated Ire1 dependent decay. Front. Genet. 5, 76.
- Cubillos-Ruiz, J.R., Silberman, P.C., Rutkowski, M.R., Chopra, S., Perales-Puchalt, A., Song, M., Zhang, S., Bettigole, S.E., Gupta, D., Holcomb, K., et al. (2015). ER stress sensor XBP1 controls anti-tumor immunity by disrupting dendritic cell homeostasis. Cell 161, 1527-1538. https://doi.org/10.1016/j.cell.2015.05.025
- Deng, J., Lu, P.D., Zhang, Y., Scheuner, D., Kaufman, R.J., Sonenberg, N., Harding, H.P., and Ron, D. (2004). Translational repression mediates activation of nuclear factor kappa B by phosphorylated translation initiation factor 2. Mol. Cell. Biol. 24, 10161-10168. https://doi.org/10.1128/MCB.24.23.10161-10168.2004
- Endo, M., Oyadomari, S., Suga, M., Mori, M., and Gotoh, T. (2005). The ER stress pathway involving CHOP is activated in the lungs of LPS-treated mice. J. Biochem. 138, 501-507. https://doi.org/10.1093/jb/mvi143
- Fanlei, H., Xiaofei, Y., Hongxia, W., Daming, Z., Chunqing, G., Huanfa, Y., Boaz, T., R., S.J., Xiaoyan, Q., and Xiang-Yang, W. (2011). ER stress and its regulator X-box-binding protein-1 enhance polyICinduced innate immune response in dendritic cells. Eur. J. Immunol. 41, 1086-1097. https://doi.org/10.1002/eji.201040831
- Fawcett, T.W., Martindale, J.L., Guyton, K.Z., Hai, T., and Holbrook, N.J. (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.
- Franco, A., Almanza, G., Burns, J.C., Wheeler, M., and Zanetti, M. (2010). Endoplasmic reticulum stress drives a regulatory phenotype in human T-cell clones. Cell. Immunol. 266, 1-6. https://doi.org/10.1016/j.cellimm.2010.09.006
- Garg, A.D., Kaczmarek, A., Krysko, O., Vandenabeele, P., Krysko, D. V, and Agostinis, P. (2012). ER stress-induced inflammation: does it aid or impede disease progression? Trends Mol. Med. 18, 589-598. https://doi.org/10.1016/j.molmed.2012.06.010
- Gass, J.N., Gifford, N.M., and Brewer, J.W. (2002). Activation of an unfolded protein response during differentiation of antibodysecreting B cells. J. Biol. Chem. 277, 49047-49054. https://doi.org/10.1074/jbc.M205011200
- Goodall, J.C., Wu, C., Zhang, Y., McNeill, L., Ellis, L., Saudek, V., and Gaston, J.S.H. (2010). Endoplasmic reticulum stress-induced transcription factor, CHOP, is crucial for dendritic cell IL-23 expression. Proc. Natl. Acad. Sci. USA 107, 17698-17703. https://doi.org/10.1073/pnas.1011736107
-
Han, D., Lerner, A.G., Vande Walle, L., Upton, J.-P., Xu, W., Hagen, A., Backes, B.J., Oakes, S.A., and Papa, F.R. (2009). IRE1
${\alpha}$ kinase activation modes control alternate endoribonuclease outputs to determine divergent cell fates. Cell 138, 562-575. https://doi.org/10.1016/j.cell.2009.07.017 - Harding, H.P., Zeng, H., Zhang, Y., Jungries, R., Chung, P., Plesken, H., Sabatini, D.D., and Ron, D. (2001). Diabetes mellitus and exocrine pancreatic dysfunction in perk-/- mice reveals a role for translational control in secretory cell survival. Mol. Cell 7, 1153-1163. https://doi.org/10.1016/S1097-2765(01)00264-7
-
Harding, H.P., Zhang, Y., Scheuner, D., Chen, J.-J., Kaufman, R.J., and Ron, D. (2009). Ppp1r15 gene knockout reveals an essential role for translation initiation factor 2 alpha (eIF2
${\alpha}$ ) dephosphorylation in mammalian development. Proc. Natl. Acad. Sci. USA 106, 1832-1837. https://doi.org/10.1073/pnas.0809632106 - Heazlewood, C.K., Cook, M.C., Eri, R., Price, G.R., Tauro, S.B., Taupin, D., Thornton, D.J., Png, C.W., Crockford, T.L., Cornall, R.J., et al. (2008). Aberrant mucin assembly in mice causes endoplasmic reticulum stress and spontaneous inflammation resembling ulcerative colitis. PLOS Med. 5, e54. https://doi.org/10.1371/journal.pmed.0050054
- Hetz, C. (2012). The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nat. Rev. Mol. Cell Biol. 13, 89-102. https://doi.org/10.1038/nrm3270
- Hetz, C., Chevet, E., and Harding, H.P. (2013). Targeting the unfolded protein response in disease. Nat. Rev. Drug Discov. 12, 703-719. https://doi.org/10.1038/nrd3976
- Hirayama, D., Iida, T., and Nakase, H. (2018). The phagocytic function of macrophage-enforcing innate immunity and tissue homeostasis. Int. J. Mol. Sci. 19, 92.
- Hollien, J., and Weissman, J.S. (2006). Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response. Science 313, 104-107. https://doi.org/10.1126/science.1129631
- 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. https://doi.org/10.1083/jcb.200903014
- Hotamisligil, G.S. (2010). Endoplasmic reticulum stress and atherosclerosis. Nat. Med. 16, 396-399. https://doi.org/10.1038/nm0410-396
-
Hu, P., Han, Z., Couvillon, A.D., Kaufman, R.J., and Exton, J.H. (2006). Autocrine tumor necrosis factor alpha links endoplasmic reticulum stress to the membrane death receptor pathway through IRE1
${\alpha}$ -mediated NF-${\kappa}$ B activation and down-regulation of TRAF2 expression. Mol. Cell. Biol. 26, 3071-3084. https://doi.org/10.1128/MCB.26.8.3071-3084.2006 -
Hur, K.Y., So, J.-S., Ruda, V., Frank-Kamenetsky, M., Fitzgerald, K., Koteliansky, V., Iwawaki, T., Glimcher, L.H., and Lee, A.-H. (2012). IRE1
${\alpha}$ activation protects mice against acetaminophen-induced hepatotoxicity. J. Exp. Med. 209, 307-318. https://doi.org/10.1084/jem.20111298 -
Iqbal, J., Dai, K., Seimon, T., Jungreis, R., Oyadomari, M., Kuriakose, G., Ron, D., Tabas, I., and Hussain, M.M. (2008). IRE1
${\beta}$ inhibits chylomicron production by selectively degrading MTP mRNA. Cell Metab. 7, 445-455. https://doi.org/10.1016/j.cmet.2008.03.005 - Iwakoshi, N.N., Pypaert, M., and Glimcher, L.H. (2007). The transcription factor XBP-1 is essential for the development and survival of dendritic cells. J. Exp. Med. 204, 2267-2275. https://doi.org/10.1084/jem.20070525
- Janssens, S., Pulendran, B., and Lambrecht, B.N. (2014). Emerging functions of the unfolded protein response in immunity. Nat. Immunol. 15, 910-919. https://doi.org/10.1038/ni.2991
- Kamimura, D., and Bevan, M.J. (2008). Endoplasmic reticulum stress regulator XBP-1 contributes to effector CD8+ T cell differentiation during acute infection. J. Immunol. 181, 5433-5441. https://doi.org/10.4049/jimmunol.181.8.5433
- Kaser, A., Lee, A.-H., Franke, A., Glickman, J.N., Zeissig, S., Tilg, H., Nieuwenhuis, E.E.S., Higgins, D.E., Schreiber, S., Glimcher, L.H., et al. (2008). XBP1 links ER stress to intestinal inflammation and confers genetic risk for human inflammatory bowel disease. Cell 134, 743-756. https://doi.org/10.1016/j.cell.2008.07.021
- Kaufman, R.J., Scheuner, D., SchrOder, M., Shen, X., Lee, K., Liu, C.Y., and Arnold, S.M. (2002). The unfolded protein response in nutrient sensing and differentiation. Nat. Rev. Mol. Cell Biol. 3, 411-421.
-
Ko, J.S., Koh, J.M., So, J.-S., Jeon, Y.K., Kim, H.Y., and Chung, D.H. (2017). Palmitate inhibits arthritis by inducing t-bet and gata-3 mRNA degradation in iNKT cells via IRE1
${\alpha}$ -dependent decay. Sci. Rep. 7, 14940. https://doi.org/10.1038/s41598-017-14780-4 - 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. https://doi.org/10.1128/MCB.23.21.7448-7459.2003
- Lee, A., Chu, G.C., Iwakoshi, N.N., and Glimcher, L.H. (2005). XBP-1 is required for biogenesis of cellular secretory machinery of exocrine glands. EMBO J. 24, 4368-4380. https://doi.org/10.1038/sj.emboj.7600903
- Lee, A.-H., Scapa, E.F., Cohen, D.E., and Glimcher, L.H. (2008). Regulation of hepatic lipogenesis by the transcription factor XBP1. Science 320, 1492-1496. https://doi.org/10.1126/science.1158042
-
Lerner, A.G., Upton, J.-P., Praveen, P.V.K., Ghosh, R., Nakagawa, Y., Igbaria, A., Shen, S., Nguyen, V., Backes, B.J., Heiman, M., et al. (2012). IRE1
${\alpha}$ induces thioredoxin-interacting protein to activate the NLRP3 inflammasome and promote programmed cell death during endoplasmic reticulum stress. Cell Metab. 16, 250-264. https://doi.org/10.1016/j.cmet.2012.07.007 - Lipson, K.L., Fonseca, S.G., Ishigaki, S., Nguyen, L.X., Foss, E., Bortell, R., Rossini, A.A., and Urano, F. (2006). Regulation of insulin biosynthesis in pancreatic beta cells by an endoplasmic reticulumresident protein kinase IRE1. Cell Metab. 4, 245-254. https://doi.org/10.1016/j.cmet.2006.07.007
-
Lipson, K.L., Ghosh, R., and Urano, F. (2008). The role of IRE1
${\alpha}$ in the degradation of insulin mRNA in pancreatic${\beta}$ -cells. PLoS One 3, e1648. https://doi.org/10.1371/journal.pone.0001648 - Lu, P.D., Harding, H.P., and Ron, D. (2004). Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response. J. Cell Biol. 167, 27-33. https://doi.org/10.1083/jcb.200408003
- Ma, Y., and Hendershot, L.M. (2003). Delineation of a negative feedback regulatory loop that controls protein translation during endoplasmic reticulum stress. J. Biol. Chem. 278, 34864-34873. https://doi.org/10.1074/jbc.M301107200
- Ma, Y., Brewer, J.W., Alan Diehl, J., and Hendershot, L.M. (2002). Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response. J. Mol. Biol. 318, 1351-1365. https://doi.org/10.1016/S0022-2836(02)00234-6
- Marciniak, S.J., and Ron, D. (2006). Endoplasmic reticulum stress signaling in disease. Physiol. Rev. 86, 1133-1149. https://doi.org/10.1152/physrev.00015.2006
- Marisa, R., Andreia, M., J., A.R., Evelina, G., and Philippe, P. (2018). At the crossway of ER-stress and proinflammatory responses. FEBS J. doi:10.1111/febs.14391. [Epub ahead of print].
- Martinon, F., Chen, X., Lee, A.-H., and Glimcher, L.H. (2010). TLR activation of the transcription factor XBP1 regulates innate immune responses in macrophages. Nat. Immunol. 11, 411-418. https://doi.org/10.1038/ni.1857
- Martins, A.S., Alves, I., Helguero, L., Domingues, M.R., and Neves, B.M. (2016). The unfolded protein response in homeostasis and modulation of mammalian immune cells. Int. Rev. Immunol. 35, 457-476. https://doi.org/10.3109/08830185.2015.1110151
- Moore, K., and Hollien, J. (2015). Ire1-mediated decay in mammalian cells relies on mRNA sequence, structure, and translational status. Mol. Biol. Cell 26, 2873-2884. https://doi.org/10.1091/mbc.e15-02-0074
- Novoa, I., Zhang, Y., Zeng, H., Jungreis, R., Harding, H.P., and Ron, D. (2003). Stress-induced gene expression requires programmed recovery from translational repression. EMBO J. 22, 1180-1187. https://doi.org/10.1093/emboj/cdg112
-
Oikawa, D., Kimata, Y., Kohno, K., and Iwawaki, T. (2009). Activation of mammalian IRE1
${\alpha}$ upon ER stress depends on dissociation of BiP rather than on direct interaction with unfolded proteins. Exp. Cell Res. 315, 2496-2504. https://doi.org/10.1016/j.yexcr.2009.06.009 -
Oikawa, D., Tokuda, M., Hosoda, A., and Iwawaki, T. (2010). Identification of a consensus element recognized and cleaved by IRE1
${\alpha}$ . Nucleic Acids Res. 38, 6265-6273. https://doi.org/10.1093/nar/gkq452 - Oslowski, C.M., and Urano, F. (2011). Measuring ER stress and the unfolded protein response using mammalian tissue culture system. Methods Enzymol. 490, 71-92.
-
Osorio, F., Tavernier, S.J., Hoffmann, E., Saeys, Y., Martens, L., Vetters, J., Delrue, I., De Rycke, R., Parthoens, E., Pouliot, P., et al. (2014). The unfolded-protein-response sensor IRE-1
${\alpha}$ regulates the function of CD8${\alpha}+$ dendritic cells. Nat. Immunol. 15, 248-257. https://doi.org/10.1038/ni.2808 -
Oyadomari, S., Harding, H.P., Zhang, Y., Oyadomari, M., and Ron, D. (2008). Dephosphorylation of translation initiation factor 2
${\alpha}$ enhances glucose tolerance and attenuates hepatosteatosis in mice. Cell Metab. 7, 520-532. https://doi.org/10.1016/j.cmet.2008.04.011 - Ozcan, U., Cao, Q., Yilmaz, E., Lee, A.-H., Iwakoshi, N.N., Ozdelen, E., Tuncman, G., GOrgun, C., Glimcher, L.H., and Hotamisligil, G.S. (2004). Endoplasmic reticulum stress links obesity, insulin action, and type 2 diabetes. Science 306, 457-461. https://doi.org/10.1126/science.1103160
- Puthalakath, H., O'Reilly, L.A., Gunn, P., Lee, L., Kelly, P.N., Huntington, N.D., Hughes, P.D., Michalak, E.M., McKimm-Breschkin, J., Motoyama, N., et al. (2007). ER Stress Triggers Apoptosis by Activating BH3-Only Protein Bim. Cell 129, 1337-1349. https://doi.org/10.1016/j.cell.2007.04.027
- Raffaella, I., and Cristina, M. (2015). Cell death induced by endoplasmic reticulum stress. FEBS J. 283, 2640-2652.
- Rao, J., Yue, S., Fu, Y., Zhu, J., Wang, X., Busuttil, R.W., Kupiec-Weglinski, J.W., Lu, L., and Zhai, Y. (2014). ATF6 mediates a proinflammatory synergy between ER stress and TLR activation in the pathogenesis of liver ischemia reperfusion injury. Am. J. Transplant 14, 1552-1561. https://doi.org/10.1111/ajt.12711
- Reimold, A.M., Etkin, A., Clauss, I., Perkins, A., Friend, D.S., Zhang, J., Horton, H.F., Scott, A., Orkin, S.H., Byrne, M.C., et al. (2000). An essential role in liver development for transcription factor XBP-1. Genes Dev. 14, 152-157.
- Reimold, A.M., Iwakoshi, N.N., Manis, J., Vallabhajosyula, P., Szomolanyi-Tsuda, E., Gravallese, E.M., Friend, D., Grusby, M.J., Alt, F., and Glimcher, L.H. (2001). Plasma cell differentiation requires the transcription factor XBP-1. Nature 412, 300-307. https://doi.org/10.1038/35085509
- Ron, D., and Walter, P. (2007). Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 8, 519-529. https://doi.org/10.1038/nrm2199
- Rutkowski, D.T., and Hegde, R.S. (2010). Regulation of basal cellular physiology by the homeostatic unfolded protein response. J. Cell Biol. 189, 783-794. https://doi.org/10.1083/jcb.201003138
- Sandrine, B., Rivka, H., Takao, I., Jae-Seon, S., Ann-Hwee, L., and Boaz, T. (2013). Regulated IRE1-dependent decay participates in curtailing immunoglobulin secretion from plasma cells. Eur. J. Immunol. 44, 867-876.
- Scheu, S., Stetson, D.B., Reinhardt, R.L., Leber, J.H., Mohrs, M., and Locksley, R.M. (2006). Activation of the integrated stress response during T helper cell differentiation. Nat. Immunol. 7, 644-651.
- Shaffer, A.L., Shapiro-Shelef, M., Iwakoshi, N.N., Lee, A.-H., Qian, S.-B., Zhao, H., Yu, X., Yang, L., Tan, B.K., Rosenwald, A., 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. https://doi.org/10.1016/j.immuni.2004.06.010
- Shen, J., Chen, X., Hendershot, L., and 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. https://doi.org/10.1016/S1534-5807(02)00203-4
- Shkoda, A., Ruiz, P.A., Daniel, H., Kim, S.C., Rogler, G., Sartor, R.B., and Haller, D. (2007). Interleukin-10 blocked endoplasmic reticulum stress in intestinal epithelial cells: impact on chronic inflammation. Gastroenterology 132, 190-207. https://doi.org/10.1053/j.gastro.2006.10.030
- Smith, J.A. (2018). Regulation of cytokine production by the unfolded protein response; implications for infection and autoimmunity. Front. Immunol. 9, 422. https://doi.org/10.3389/fimmu.2018.00422
-
Smith, J.A., Turner, M.J., DeLay, M.L., Klenk, E.I., Sowders, D.P., and Colbert, R.A. (2008). Endoplasmic reticulum stress and the unfolded protein response are linked to synergistic IFN-
${\beta}$ induction via X-box binding protein 1. Eur. J. Immunol. 38, 1194-1203. https://doi.org/10.1002/eji.200737882 -
So, J.-S., Hur, K.Y., Tarrio, M., Ruda, V., Frank-Kamenetsky, M., Fitzgerald, K., Koteliansky, V., Lichtman, A.H., Iwawaki, T., Glimcher, L.H., et al. (2012). Silencing of lipid metabolism genes through IRE1
${\alpha}$ -mediated mRNA decay lowers plasma lipids in mice. Cell Metab. 16, 487-499. https://doi.org/10.1016/j.cmet.2012.09.004 -
So, J.-S., Cho, S., Min, S.-H., Kimball, S.R., and Lee, A.-H. (2015). IRE1
${\alpha}$ -dependent decay of CReP/Ppp1r15b mRNA increases eukaryotic initiation factor 2${\alpha}$ phosphorylation and suppresses protein synthesis. Mol. Cell. Biol. 35, 2761-2770. https://doi.org/10.1128/MCB.00215-15 - Stadhouders, R., Lubberts, E., and Hendriks, R.W. (2018). A cellular and molecular view of T helper 17 cell plasticity in autoimmunity. J. Autoimmun. 87, 1-15. https://doi.org/10.1016/j.jaut.2017.12.007
- Tang, C.-H.A., Chang, S., Paton, A.W., Paton, J.C., Gabrilovich, D.I., Ploegh, H.L., Del Valle, J.R., and Hu, C.-C.A. (2018). Phosphorylation of IRE1 at S729 regulates RIDD in B cells and antibody production after immunization. J. Cell Biol. 217, 1739-1755. https://doi.org/10.1083/jcb.201709137
- Taubenheim, N., Tarlinton, D.M., Crawford, S., Corcoran, L.M., Hodgkin, P.D., and Nutt, S.L. (2012). High rate of antibody secretion is not integral to plasma cell differentiation as revealed by XBP-1 deficiency. J. Immunol. 189, 3328-3338. https://doi.org/10.4049/jimmunol.1201042
- Tavernier, S.J., Osorio, F., Vandersarren, L., Vetters, J., Vanlangenakker, N., Van Isterdael, G., Vergote, K., De Rycke, R., Parthoens, E., van de Laar, L., et al. (2017). Regulated IRE1-dependent mRNA decay sets the threshold for dendritic cell survival. Nat. Cell Biol. 19, 698-710. https://doi.org/10.1038/ncb3518
- Tellier, J., Shi, W., Minnich, M., Liao, Y., Crawford, S., Smyth, G.K., Kallies, A., Busslinger, M., and Nutt, S.L. (2016). Blimp-1 controls plasma cell function through the regulation of immunoglobulin secretion and the unfolded protein response. Nat. Immunol. 17, 323-330. https://doi.org/10.1038/ni.3348
- Thaxton, J.E., Wallace, C., Riesenberg, B., Zhang, Y., Paulos, C.M., Beeson, C.C., Liu, B., and Li, Z. (2017). Modulation of endoplasmic reticulum stress controls CD4+ T-cell activation and antitumor function. Cancer Immunol. Res. 5, 666-675. https://doi.org/10.1158/2326-6066.CIR-17-0081
- Todd, D.J., McHeyzer-Williams, L.J., Kowal, C., Lee, A.-H., Volpe, B.T., Diamond, B., McHeyzer-Williams, M.G., and Glimcher, L.H. (2009). XBP1 governs late events in plasma cell differentiation and is not required for antigen-specific memory B cell development. J. Exp. Med. 206, 2151-2159. https://doi.org/10.1084/jem.20090738
-
Tsuru, A., Fujimoto, N., Takahashi, S., Saito, M., Nakamura, D., Iwano, M., Iwawaki, T., Kadokura, H., Ron, D., and Kohno, K. (2013). Negative feedback by IRE1
${\beta}$ optimizes mucin production in goblet cells. Proc. Natl. Acad. Sci. USA 110, 2864 LP-2869. -
Upton, J.-P., Wang, L., Han, D., Wang, E.S., Huskey, N.E., Lim, L., Truitt, M., McManus, M.T., Ruggero, D., Goga, A., et al. (2012). IRE1
${\alpha}$ cleaves select microRNAs during ER stress to derepress translation of proapoptotic caspase-2. Science 338, 818-822. https://doi.org/10.1126/science.1226191 - Urano, F., Wang, X., Bertolotti, A., Zhang, Y., Chung, P., Harding, H.P., and Ron, D. (2000). Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 287, 664-666. https://doi.org/10.1126/science.287.5453.664
- Urra, H., Dufey, E., Lisbona, F., Rojas-Rivera, D., and Hetz, C. (2013). When ER stress reaches a dead end. Biochim. Biophys. Acta. Mol. Cell Res. 1833, 3507-3517. https://doi.org/10.1016/j.bbamcr.2013.07.024
- Vattemi, G., Engel, W.K., McFerrin, J., and Askanas, V. (2004). Endoplasmic reticulum stress and unfolded protein response in inclusion body myositis muscle. Am. J. Pathol. 164, 1-7. https://doi.org/10.1016/S0002-9440(10)63089-1
- Volmer, R., and Ron, D. (2015). Lipid-dependent regulation of the unfolded protein response. Curr. Opin. Cell Biol. 33, 67-73. https://doi.org/10.1016/j.ceb.2014.12.002
- Walter, P., and Ron, D. (2011). The unfolded protein response: from stress pathway to homeostatic regulation. Science 334, 1081-1086. https://doi.org/10.1126/science.1209038
- Wang, S., and Kaufman, R.J. (2012). The impact of the unfolded protein response on human disease. J. Cell Biol. 197, 857-867. https://doi.org/10.1083/jcb.201110131
- Wheeler, M.C., Rizzi, M., Sasik, R., Almanza, G., Hardiman, G., and Zanetti, M. (2008). KDEL-retained antigen in B lymphocytes induces a proinflammatory response: a possible role for endoplasmic reticulum stress in adaptive T cell immunity. J. Immunol. 181, 256-264. https://doi.org/10.4049/jimmunol.181.1.256
-
Xue, X., Piao, J.-H., Nakajima, A., Sakon-Komazawa, S., Kojima, Y., Mori, K., Yagita, H., Okumura, K., Harding, H., and Nakano, H. (2005). Tumor necrosis factor
${\alpha}$ (TNF${\alpha}$ ) induces the unfolded protein response (UPR) in a reactive oxygen species (ROS)-dependent fashion, and the UPR counteracts ROS accumulation by TNF${\alpha}$ . J. Biol. Chem. 280, 33917-33925. https://doi.org/10.1074/jbc.M505818200 - Yamaguchi, H., and Wang, H.-G. (2004). CHOP is involved in endoplasmic reticulum stress-induced apoptosis by enhancing DR5 expression in human carcinoma cells. J. Biol. Chem. 279, 45495-45502. https://doi.org/10.1074/jbc.M406933200
- Yamamoto, K., Yoshida, H., Kokame, K., Kaufman, R.J., and Mori, K. (2004). Differential contributions of ATF6 and XBP1 to the activation of endoplasmic reticulum stress-responsive cis-acting elements ERSE, UPRE and ERSE-II. J. Biochem. 136, 343-350. https://doi.org/10.1093/jb/mvh122
- Yamamoto, K., Suzuki, N., Wada, T., Okada, T., Yoshida, H., Kaufman, R.J., and Mori, K. (2008). Human HRD1 promoter carries a functional unfolded protein response element to which XBP1 but not ATF6 directly binds. J. Biochem. 144, 477-486. https://doi.org/10.1093/jb/mvn091
- Ye, J., Rawson, R.B., Komuro, R., Chen, X., Davé, U.P., Prywes, R., Brown, M.S., and Goldstein, J.L. (2000). ER Stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs. Mol. Cell 6, 1355-1364. https://doi.org/10.1016/S1097-2765(00)00133-7
- 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. https://doi.org/10.1016/S0092-8674(01)00611-0
- Zhang, K., and Kaufman, R.J. (2008). From endoplasmic-reticulum stress to the inflammatory response. Nature 454, 455-462. https://doi.org/10.1038/nature07203
- Zhang, K., Shen, X., Wu, J., Sakaki, K., Saunders, T., Rutkowski, D.T., Back, S.H., and Kaufman, R.J. (2006). Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response. Cell 124, 587-599. https://doi.org/10.1016/j.cell.2005.11.040
- Zinszner, H., Kuroda, M., Wang, X., Batchvarova, N., Lightfoot, R.T., Remotti, H., Stevens, J.L., and Ron, D. (1998). CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum. Genes Dev. 12, 982-995. https://doi.org/10.1101/gad.12.7.982
Cited by
- Endoplasmic Reticulum Stress Signaling Pathways: Activation and Diseases vol.20, pp.9, 2019, https://doi.org/10.2174/1389203720666190621103145
- Insights into the role of endoplasmic reticulum stress in skin function and associated diseases vol.286, pp.2, 2018, https://doi.org/10.1111/febs.14739
- The Emerging Roles of Endoplasmic Reticulum Stress in Balancing Immunity and Tolerance in Health and Diseases: Mechanisms and Opportunities vol.10, pp.None, 2019, https://doi.org/10.3389/fimmu.2019.03154
- G-Protein-Coupled Receptor 120 Mediates DHA-Induced Apoptosis by Regulating IP3R, ROS and, ER Stress Levels in Cisplatin-Resistant Cancer Cells vol.42, pp.3, 2019, https://doi.org/10.14348/molcells.2019.2440
- Impacts of GFP-FoxP3+ regulatory T cells on lupus hallmarks differ by genetic background and type of GFP knock-in vol.52, pp.5, 2019, https://doi.org/10.1080/08916934.2019.1657098
- The Role of Mitochondrial and Endoplasmic Reticulum Reactive Oxygen Species Production in Models of Perinatal Brain Injury vol.31, pp.9, 2018, https://doi.org/10.1089/ars.2019.7779
- Distinct Subcellular Compartments of Dendritic Cells Used for Cross-Presentation vol.20, pp.22, 2019, https://doi.org/10.3390/ijms20225606
- EPHB4 inhibition activates ER stress to promote immunogenic cell death of prostate cancer cells vol.10, pp.11, 2018, https://doi.org/10.1038/s41419-019-2042-y
- Reprogramming the unfolded protein response for replication by porcine reproductive and respiratory syndrome virus vol.15, pp.11, 2018, https://doi.org/10.1371/journal.ppat.1008169
- Wolfram syndrome, a rare neurodegenerative disease: from pathogenesis to future treatment perspectives vol.17, pp.1, 2018, https://doi.org/10.1186/s12967-019-1993-1
- Characterization of the Proteomic Response of A549 Cells Following Sequential Exposure to Aspergillus fumigatus and Pseudomonas aeruginosa vol.19, pp.1, 2018, https://doi.org/10.1021/acs.jproteome.9b00520
- Metabolic Routes in Inflammation: The Citrate Pathway and its Potential as Therapeutic Target vol.26, pp.40, 2018, https://doi.org/10.2174/0929867325666180510124558
- Endoplasmic Reticulum Stress and Intestinal Inflammation: A Perilous Union vol.11, pp.None, 2018, https://doi.org/10.3389/fimmu.2020.543022
- Fibroblast Growth Factor 2 Attenuates Renal Ischemia-Reperfusion Injury via Inhibition of Endoplasmic Reticulum Stress vol.8, pp.None, 2020, https://doi.org/10.3389/fcell.2020.00147
- Fibrillary Glomerulopathy with a High Level of Myeloperoxidase-ANCA: A Case Report vol.2020, pp.None, 2018, https://doi.org/10.1155/2020/6343521
- The active nuclear form of SREBP1 amplifies ER stress and autophagy via regulation of PERK vol.287, pp.11, 2018, https://doi.org/10.1111/febs.15144
- ADAR1-Dependent RNA Editing Promotes MET and iPSC Reprogramming by Alleviating ER Stress vol.27, pp.2, 2018, https://doi.org/10.1016/j.stem.2020.04.016
- FOXO1 promotes HIV Latency by suppressing ER stress in T cells vol.5, pp.9, 2018, https://doi.org/10.1038/s41564-020-0742-9
- Thapsigargin at Non-Cytotoxic Levels Induces a Potent Host Antiviral Response that Blocks Influenza A Virus Replication vol.12, pp.10, 2020, https://doi.org/10.3390/v12101093
- Nrf2-interacting nutrients and COVID-19: time for research to develop adaptation strategies vol.10, pp.1, 2020, https://doi.org/10.1186/s13601-020-00362-7
- Protein disulfide isomerase A1 regulates breast cancer cell immunorecognition in a manner dependent on redox state vol.44, pp.6, 2020, https://doi.org/10.3892/or.2020.7816
- Spices to Control COVID-19 Symptoms: Yes, but Not Only… vol.182, pp.6, 2018, https://doi.org/10.1159/000513538
- Chinese Herbal Medicine Alleviates Myocardial Ischemia/Reperfusion Injury by Regulating Endoplasmic Reticulum Stress vol.2021, pp.None, 2018, https://doi.org/10.1155/2021/4963346
- A Weak Response to Endoplasmic Reticulum Stress Is Associated With Postoperative Organ Failure in Patients Undergoing Cardiac Surgery With Cardiopulmonary Bypass vol.7, pp.None, 2018, https://doi.org/10.3389/fmed.2020.613518
- XBP-1s Promotes B Cell Pathogenicity in Chronic GVHD by Restraining the Activity of Regulated IRE-1α-Dependent Decay vol.12, pp.None, 2018, https://doi.org/10.3389/fimmu.2021.705484
- Immune-Related Long Non-coding RNA Signature and Clinical Nomogram to Evaluate Survival of Patients Suffering Esophageal Squamous Cell Carcinoma vol.9, pp.None, 2018, https://doi.org/10.3389/fcell.2021.641960
- The Role of the Signaling Pathways Involved in the Effects of Hydrogen Sulfide on Endoplasmic Reticulum Stress vol.9, pp.None, 2021, https://doi.org/10.3389/fcell.2021.646723
- Metformin prevents brain injury after cardiopulmonary resuscitation by inhibiting the endoplasmic reticulum stress response and activating AMPK-mediated autophagy vol.66, pp.1, 2018, https://doi.org/10.1177/0036933020961543
- Endoplasmic reticulum stress in intestinal inflammation: implications of bile acids vol.87, pp.2, 2018, https://doi.org/10.1007/s43538-021-00031-8
- Relationship of endoplasmic reticulum stress with the etiopathogenesis of chronic tonsillitis and tonsillar hypertrophy in pediatric patients: a prospective, parallel-group study vol.48, pp.7, 2018, https://doi.org/10.1007/s11033-021-06579-4
- Roles of XBP1s in Transcriptional Regulation of Target Genes vol.9, pp.7, 2021, https://doi.org/10.3390/biomedicines9070791
- ER stress and its PERK branch enhance TCR-induced activation in regulatory T cells vol.563, pp.None, 2018, https://doi.org/10.1016/j.bbrc.2021.05.061
- Targeting the integrated stress response in ophthalmology vol.46, pp.8, 2018, https://doi.org/10.1080/02713683.2020.1867748
- The Crucial Role of NLRP3 Inflammasome in Viral Infection-Associated Fibrosing Interstitial Lung Diseases vol.22, pp.19, 2018, https://doi.org/10.3390/ijms221910447
- Recombinant human growth hormone improves the immune status of rats with septic encephalopathy: The role of VEGFR2 in the prevalence of endoplasmic reticulum stress repair module vol.101, pp.no.pb, 2018, https://doi.org/10.1016/j.intimp.2021.108370
- Clinical and molecular characteristics of COVID-19 patients with persistent SARS-CoV-2 infection vol.12, pp.1, 2021, https://doi.org/10.1038/s41467-021-23621-y
- Chronic lung diseases are associated with gene expression programs favoring SARS-CoV-2 entry and severity vol.12, pp.1, 2018, https://doi.org/10.1038/s41467-021-24467-0
- Absence of ERAP1 in B Cells Increases Susceptibility to Central Nervous System Autoimmunity, Alters B Cell Biology, and Mechanistically Explains Genetic Associations between ERAP1 and Multiple Scleros vol.207, pp.12, 2018, https://doi.org/10.4049/jimmunol.2100813
- The impaired unfolded protein‐premelanosome protein and transient receptor potential channels‐autophagy axes in apoptotic melanocytes in vitiligo vol.35, pp.1, 2022, https://doi.org/10.1111/pcmr.13006