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XBP-1 Regulates a Subset of Endoplasmic Reticulum Resident Chaperone Genes in the Unfolded Protein Response
Open accessAbstract
The mammalian unfolded protein response (UPR) protects the cell against the stress of misfolded proteins in the endoplasmic reticulum (ER). We have investigated here the contribution of the UPR transcription factors XBP-1, ATF6alpha, and ATF6beta to UPR target gene expression. Gene profiling of cell lines lacking these factors yielded several XBP-1-dependent UPR target genes, all of which appear to act in the ER. These included the DnaJ/Hsp40-like genes, p58(IPK), ERdj4, and HEDJ, as well as EDEM, protein disulfide isomerase-P5, and ribosome-associated membrane protein 4 (RAMP4), whereas expression of BiP was only modestly dependent on XBP-1. Surprisingly, given previous reports that enforced expression of ATF6alpha induced a subset of UPR target genes, cells deficient in ATF6alpha, ATF6beta, or both had minimal defects in upregulating UPR target genes by gene profiling analysis, suggesting the presence of compensatory mechanism(s) for ATF6 in the UPR. Since cells lacking both XBP-1 and ATF6alpha had significantly impaired induction of select UPR target genes and ERSE reporter activation, XBP-1 and ATF6alpha may serve partially redundant functions. No UPR target genes that required ATF6beta were identified, nor, in contrast to XBP-1 and ATF6alpha, did the activity of the UPRE or ERSE promoters require ATF6beta, suggesting a minor role for it during the UPR. Collectively, these results suggest that the IRE1/XBP-1 pathway is required for efficient protein folding, maturation, and degradation in the ER and imply the existence of subsets of UPR target genes as defined by their dependence on XBP-1. Further, our observations suggest the existence of additional, as-yet-unknown, key regulators of the UPR.
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ER Stress Induces Cleavage of Membrane-Bound ATF6 by the Same Proteases that Process SREBPs
Ye, J., Rawson, R. B., Komuro, R., Chen, X., Davé, U. P., Prywes, R., Brown, M. S., & Goldstein, J. L. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00133-7 · Cited by 1,871
Orchestrating the unfolded protein response in health and disease
Kaufman, R. J. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0216886 · Cited by 1,015
Yoshida, H., Okada, T., Haze, K., Yanagi, H., Yura, T., Negishi, M., & Mori, K. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.18.6755-6767.2000 · Cited by 934
Yan, W., Frank, C. L., Korth, M. J., Sopher, B. L., Novoa, I., Ron, D., & Katze, M. G. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252341799 · Cited by 385
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Özcan, U., Cao, Q., Yilmaz, E., Lee, A.-H., Iwakoshi, N. N., Özdelen, E., Tuncman, G., Görgün, C., Glimcher, L. H., & Hotamisligil, G. S. (2004) · Science · doi:10.1126/science.1103160 · Cited by 3,844
Self-citationEndoplasmic reticulum stress and the inflammatory basis of metabolic disease
Hotamisligil, G. S. (2010) · Cell · doi:10.1016/j.cell.2010.02.034 · Cited by 2,802
Mediators of endoplasmic reticulum stress-induced apoptosis
Szegezdi, E., Logue, S. E., Gorman, A. M., & Samali, A. (2006) · The EMBO Reports · doi:10.1038/sj.embor.7400779 · Cited by 2,345
Endoplasmic reticulum stress signals in the tumour and its microenvironment
Chen, X., & Cubillos-Ruiz, J. R. (2021) · Nature Reviews Cancer · doi:10.1038/s41568-020-00312-2 · Cited by 1,356
Adamson, B., Norman, T. M., Jost, M., Cho, M. Y., Nuñez, J. K., Chen, Y., Villalta, J. E., Gilbert, L. A., Horlbeck, M. A., Hein, M. Y., et al. (2016) · Cell · doi:10.1016/j.cell.2016.11.048 · Cited by 1,193
The Role for Endoplasmic Reticulum Stress in Diabetes Mellitus
Eizirik, D. L., Cardozo, A. K., & Cnop, M. (2008) · Endocrine Reviews · doi:10.1210/er.2007-0015 · Cited by 1,173
Yoshida, H. (2007) · The FEBS Journal · doi:10.1111/j.1742-4658.2007.05639.x · Cited by 1,086
Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus
Westermark, P., Andersson, A., & Westermark, G. T. (2011) · Physiological Reviews · doi:10.1152/physrev.00042.2009 · Cited by 1,044
Endoplasmic reticulum stress signalling-from basic mechanisms to clinical applications
Almanza, A., Carlesso, A., Chintha, C., Creedican, S., Doultsinos, D., Leuzzi, B., Luís, A., McCarthy, N., Montibeller, L., More, S., et al. (2019) · The FEBS Journal · doi:10.1111/febs.14608 · Cited by 1,034
ER Stress Sensor XBP1 Controls Anti-tumor Immunity by Disrupting Dendritic Cell Homeostasis
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) · Cell · doi:10.1016/j.cell.2015.05.025 · Cited by 933
Self-citationEndoplasmic reticulum stress contributes to beta cell apoptosis in type 2 diabetes
Laybutt, D. R., Preston, A. M., Åkerfeldt, M. C., Kench, J. G., Busch, A. K., Biankin, A. V., & Biden, T. J. (2007) · Diabetologia · doi:10.1007/s00125-006-0590-z · Cited by 830
Endoplasmic Reticulum Stress Activates Cleavage of CREBH to Induce a Systemic Inflammatory Response
Zhang, K., Shen, X., Wu, J., Sakaki, K., Saunders, T., Rutkowski, D. T., Back, S. H., & Kaufman, R. J. (2006) · Cell · doi:10.1016/j.cell.2005.11.040 · Cited by 716
Sriburi, R., Jackowski, S., Mori, K., & Brewer, J. W. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200406136 · Cited by 653
A Molecular Web: Endoplasmic Reticulum Stress, Inflammation, and Oxidative Stress
Chaudhari, N., Talwar, P., Parimisetty, A., Lefebvre d’Hellencourt, C., & Ravanan, P. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00213 · Cited by 600
Glucose-regulated proteins in cancer: molecular mechanisms and therapeutic potential
Lee, A. S. (2014) · Nature Reviews Cancer · doi:10.1038/nrc3701 · Cited by 587
Self-citationCoordination of ER and oxidative stress signaling: The PERK/Nrf2 signaling pathway
Cullinan, S. B., & Diehl, J. A. (2006) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.09.018 · Cited by 554
Hetz, C., Thielen, P., Matus, S., Nassif, M., Court, F., Kiffin, R., Martinez, G., Cuervo, A. M., Brown, R. H., & Glimcher, L. H. (2009) · Genes & Development · doi:10.1101/gad.1830709 · Cited by 530
Self-citationMimura, N., Fulciniti, M., Gorgun, G., Tai, Y.-T., Cirstea, D., Santo, L., Hu, Y., Fabre, C., Minami, J., Ohguchi, H., et al. (2012) · Blood · doi:10.1182/blood-2011-07-366633 · Cited by 432
Characterization of a novel PERK kinase inhibitor with antitumor and antiangiogenic activity
Atkins, C., Liu, Q., Minthorn, E., Zhang, S.-Y., Figueroa, D. J., Moss, K., Stanley, T. B., Sanders, B., Goetz, A., Gaul, N., et al. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-3109 · Cited by 443
IRE1α–XBP1 controls T cell function in ovarian cancer by regulating mitochondrial activity
Song, M., Sandoval, T. A., Chae, C.-S., Chopra, S., Tan, C., Rutkowski, M. R., Raundhal, M., Chaurio, R. A., Payne, K. K., Konrad, C., et al. (2018) · Nature · doi:10.1038/s41586-018-0597-x · Cited by 413
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Oakes, S. A. (2020) · The American Journal of Pathology · doi:10.1016/j.ajpath.2020.01.010 · Cited by 397
Marzec, M., Eletto, D., & Argon, Y. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.10.013 · Cited by 390
Signaling the mitochondrial unfolded protein response
Pellegrino, M. W., Nargund, A. M., & Haynes, C. M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.02.019 · Cited by 359
Somatic mutations and cell identity linked by Genotyping of Transcriptomes
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The ER stress factor XBP1s prevents amyloid-β neurotoxicity
Casas-Tinto, S., Zhang, Y., Sanchez-Garcia, J., Gomez-Velazquez, M., Rincon-Limas, D. E., & Fernandez-Funez, P. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr100 · Cited by 275
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Gerakis, Y., & Hetz, C. (2018) · The FEBS Journal · doi:10.1111/febs.14332 · Cited by 226
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Ye, D., Li, F. Y. L., Lam, K. S. L., Li, H., Jia, W., Wang, Y., Man, K., Lo, C. M., Li, X., & Xu, A. (2012) · Gut · doi:10.1136/gutjnl-2011-300269 · Cited by 206
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Bravo, R., Gutierrez, T., Paredes, F., Gatica, D., Rodriguez, A. E., Pedrozo, Z., Chiong, M., Parra, V., Quest, A. F. G., Rothermel, B. A., et al. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.10.012 · Cited by 191
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Denks, K., Vogt, A., Sachelaru, I., Petriman, N.-A., Kudva, R., & Koch, H.-G. (2014) · Molecular Membrane Biology · doi:10.3109/09687688.2014.907455 · Cited by 170
Smith, J. A. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00422 · Cited by 168
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Self-citationProtein Folding in the Endoplasmic Reticulum and the Unfolded Protein Response
Zhang, K., & Kaufman, R. J. (2005) · Handbook of Experimental Pharmacology · doi:10.1007/3-540-29717-0_3 · Cited by 152
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Lee, H., Lee, Y.-S., Harenda, Q., Pietrzak, S., Oktay, H. Z., Schreiber, S., Liao, Y., Sonthalia, S., Ciecko, A. E., Chen, Y.-G., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.03.002 · Cited by 152
Causes and cures for endoplasmic reticulum stress in lipotoxic β ‐cell dysfunction
Cnop, M., Ladrière, L., Igoillo‐Esteve, M., Moura, R. F., & Cunha, D. A. (2010) · Diabetes, Obesity and Metabolism · doi:10.1111/j.1463-1326.2010.01279.x · Cited by 150
Ling, S. C. W., Lau, E. K. K., Al-Shabeeb, A., Nikolic, A., Catalano, A., Iland, H., Horvath, N., Ho, P. J., Harrison, S., Fleming, S., et al. (2012) · Haematologica · doi:10.3324/haematol.2011.043331 · Cited by 130
Mechanism of Endoplasmic Reticulum Stress in Cerebral Ischemia
Han, Y., Yuan, M., Guo, Y.-S., Shen, X.-Y., Gao, Z.-K., & Bi, X. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.704334 · Cited by 105
Ishihara, K., Yamazaki, T., Ishida, Y., Suzuki, T., Oda, K., Nagao, M., Yamaguchi-Iwai, Y., & Kambe, T. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602470200 · Cited by 104
Gutiérrez, T., & Simmen, T. (2018) · Cell Calcium · doi:10.1016/j.ceca.2017.05.015 · Cited by 104
Stimulation of an Unfolded Protein Response Impairs MHC Class I Expression
de Almeida, S. F., Fleming, J. V., Azevedo, J. E., Carmo-Fonseca, M., & de Sousa, M. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.6.3612 · Cited by 94
Ohya, T., Hayashi, T., Kiyama, E., Nishii, H., Miki, H., Kobayashi, K., Honda, K., Omasa, T., & Ohtake, H. (2008) · Biotechnology and Bioengineering · doi:10.1002/bit.21758 · Cited by 96
The unfolded protein response and cancer: A brighter future unfolding?
Scriven, P., Brown, N. J., Pockley, A. G., & Wyld, L. (2007) · Journal of Molecular Medicine · doi:10.1007/s00109-006-0150-5 · Cited by 67
Targeting the unfolded protein response for disease intervention.
Rivas, A., Vidal, R. L., & Hetz, C. (2015) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2015.1053869 · Cited by 62
Mitochondria, Oxytocin, and Vasopressin: Unfolding the Inflammatory Protein Response
Bordt, E. A., Smith, C. J., Demarest, T. G., Bilbo, S. D., & Kingsbury, M. A. (2019) · Neurotoxicity Research · doi:10.1007/s12640-018-9962-7 · Cited by 58
Sigma-1 receptor: a potential therapeutic target for traumatic brain injury
Shi, M., Chen, F., Chen, Z., Yang, W., Yue, S., Zhang, J., & Chen, X. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.685201 · Cited by 58
Membrane biogenesis and the unfolded protein response
Ron, D., & Hampton, R. Y. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200408117 · Cited by 45
Inhibition of NF-κB by MG132 through ER stress-mediated induction of LAP and LIP
Nakajima, S., Kato, H., Takahashi, S., Johno, H., & Kitamura, M. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.05.047 · Cited by 46
Bartoszewska, S., Cabaj, A., Dąbrowski, M., Collawn, J. F., & Bartoszewski, R. (2019) · The FASEB Journal · doi:10.1096/fj.201900600rr · Cited by 45
Ben Othmène, Y., Monceaux, K., Belhadef, A., Karoui, A., Ben Salem, I., Boussabbeh, M., Abid-Essefi, S., & Lemaire, C. (2022) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2022.103919 · Cited by 43
Transcription factor MIST1 in terminal differentiation of mouse and human plasma cells
Capoccia, B. J., Lennerz, J. K. M., Bredemeyer, A. J., Klco, J. M., Frater, J. L., & Mills, J. C. (2011) · Physiological Genomics · doi:10.1152/physiolgenomics.00084.2010 · Cited by 33
Cao, Y., Knöchel, S., Oswald, F., Donow, C., Zhao, H., & Knöchel, W. (2006) · Mechanisms of Development · doi:10.1016/j.mod.2005.09.003 · Cited by 30
Okoro, E. U., Zhao, Y., Guo, Z., Zhou, L., Lin, X., & Yang, H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0044430 · Cited by 25
Metabolic injury of hepatocytes promotes progression of NAFLD and AALD
Carvalho-Gontijo, R., Han, C., Zhang, L., Zhang, V., Hosseini, M., Mekeel, K., Schnabl, B., Loomba, R., Karin, M., Brenner, D. A., et al. (2022) · Seminars in Liver Disease · doi:10.1055/s-0042-1755316 · Cited by 23
Inflammatory ER stress responses dictate the immunopathogenic progression of systemic candidiasis
Awasthi, D., Chopra, S., Cho, B. A., Emmanuelli, A., Sandoval, T. A., Hwang, S.-M., Chae, C.-S., Salvagno, C., Tan, C., Vasquez-Urbina, L., et al. (2023) · Journal of Clinical Investigation · doi:10.1172/jci167359 · Cited by 24
Villani, G. R. D., Chierchia, A., Di Napoli, D., & Di Natale, P. (2012) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-011-9403-8 · Cited by 15
Dabsan, S., Zur, G., Abu-Freha, N., Sofer, S., Grossman-Haham, I., Gilad, A., & Igbaria, A. (2025) · eLife · doi:10.7554/elife.102658 · Cited by 10
Ranjan, K. (2020) · Gastrointestinal Disorders · doi:10.3390/gidisord2030024 · Cited by 6
Metadata
- Authors
- Lee, A.-H., Iwakoshi, N. N., & Glimcher, L. H.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2003-11-01
- Volume
- 23
- Issue
- 21
- Pages
- 7448-7459
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- OpenAlex
- W2127906377
- Cited by
- 2,037
- References
- 4
- FWCI
- 14.29
- Type
- journal article
- Language
- en
- Open access
- green
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