Mechanisms, regulation and functions of the unfolded protein response

Signal integration in the endoplasmic reticulum unfolded protein response

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The Unfolded Protein Response: From Stress Pathway to Homeostatic Regulation

Walter, P., & Ron, D. (2011) · Science · doi:10.1126/science.1209038 · Cited by 5,897

Control of inositol 1,4,5-trisphosphate-induced Ca2+ release by cytosolic Ca2+

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XBP1 mRNA Is Induced by ATF6 and Spliced by IRE1 in Response to ER Stress to Produce a Highly Active Transcription Factor

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Proapoptotic BAX and BAK: A Requisite Gateway to Mitochondrial Dysfunction and Death

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Endoplasmic Reticulum Stress Links Obesity, Insulin Action, and Type 2 Diabetes

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Mutation of the mouse klotho gene leads to a syndrome resembling ageing

Kuro-o, M., Matsumura, Y., Aizawa, H., Kawaguchi, H., Suga, T., Utsugi, T., Ohyama, Y., Kurabayashi, M., Kaname, T., Kume, E., et al. (1997) · Nature · doi:10.1038/36285 · Cited by 3,837

An Integrated Stress Response Regulates Amino Acid Metabolism and Resistance to Oxidative Stress

Harding, H. P., Zhang, Y., Zeng, H., Novoa, I., Lu, P. D., Calfon, M. A., Sadri, N., Yun, C., Popko, B., Paules, R. S., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00105-9 · Cited by 3,336

Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase

Harding, H. P., Zhang, Y., & Ron, D. (1999) · Nature · doi:10.1038/16729 · Cited by 3,310

IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA

Calfon, M. A., Zeng, H., Urano, F., Till, J. H., Hubbard, S. R., Harding, H. P., Clark, S. G., & Ron, D. (2002) · Nature · doi:10.1038/415092a · Cited by 2,907

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. (2000) · Nature Cell Biology · doi:10.1038/35014014 · Cited by 2,871

Adapting Proteostasis for Disease Intervention

Balch, W. E., Morimoto, R. I., Dillin, A., & Kelly, J. W. (2008) · Science · doi:10.1126/science.1141448 · Cited by 2,495

Regulation of apoptosis in health and disease: the balancing act of BCL-2 family proteins

Singh, R., Letai, A., & Sarosiek, K. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0089-8 · Cited by 2,111

Mammalian Transcription Factor ATF6 Is Synthesized as a Transmembrane Protein and Activated by Proteolysis in Response to Endoplasmic Reticulum Stress

Haze, K., Yoshida, H., Yanagi, H., Yura, T., & Mori, K. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.11.3787 · Cited by 2,100

CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulumPreprint

Marciniak, S. J., Yun, C. Y., Oyadomari, S., Novoa, I., Zhang, Y., Jungreis, R., Nagata, K., Harding, H. P., & Ron, D. (2004) · Genes & Development · doi:10.1101/gad.1250704 · Cited by 2,066

Gadd153 Sensitizes Cells to Endoplasmic Reticulum Stress by Down-Regulating Bcl2 and Perturbing the Cellular Redox State

McCullough, K. D., Martindale, J. L., Klotz, L., Aw, T. Y., & Holbrook, N. J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.4.1249-1259.2001 · Cited by 1,945

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

Signals from the lysosome: a control centre for cellular clearance and energy metabolism

Settembre, C., Fraldi, A., Medina, D. L., & Ballabio, A. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3565 · Cited by 1,755

Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells

Vattem, K. M., & Wek, R. C. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400541101 · Cited by 1,696

ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death

Han, J., Back, S. H., Hur, J., Lin, Y.-H., Gildersleeve, R., Shan, J., Yuan, C. L., Krokowski, D., Wang, S., Hatzoglou, M., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2738 · Cited by 1,691

The Unfolded Protein Response and Cell Fate Control

Hetz, C. A., & Papa, F. R. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.06.017 · Cited by 1,567

ER Stress Triggers Apoptosis by Activating BH3-Only Protein Bim

Puthalakath, H., O’Reilly, L. A., Gunn, P., Lee, L., Kelly, P. N., Huntington, N. D., Hughes, P., Michalak, E. M., McKimm‐Breschkin, J. L., Motoyama, N., et al. (2007) · Cell · doi:10.1016/j.cell.2007.04.027 · Cited by 1,493

IRE1 Signaling Affects Cell Fate During the Unfolded Protein Response

Lin, J. H., Li, H., Yasumura, D., Cohen, H., Zhang, C., Panning, B., Shokat, K., Lavail, M., & Walter, P. (2007) · Science · doi:10.1126/science.1146361 · Cited by 1,435

Feedback Inhibition of the Unfolded Protein Response by GADD34-Mediated Dephosphorylation of eIF2α

Novoa, I., Zeng, H., Harding, H. P., & Ron, D. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.5.1011 · Cited by 1,434

An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein.

Munro, S., & Pelham, H. (1986) · Cell · doi:10.1016/0092-8674(86)90746-4 · Cited by 1,378

The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins

Kozutsumi, Y., Segal, M. S., Normington, K., Gething, M.-J. H., & Sambrook, J. (1988) · Nature · doi:10.1038/332462a0 · Cited by 1,322

Decay of Endoplasmic Reticulum-Localized mRNAs During the Unfolded Protein Response

Hollien, J., & Weissman, J. S. (2006) · Science · doi:10.1126/science.1129631 · Cited by 1,319

Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase

Cox, J. S., Shamu, C. E., & Walter, P. (1993) · Cell · doi:10.1016/0092-8674(93)90648-a · Cited by 1,240

Identification of the cis-Acting Endoplasmic Reticulum Stress Response Element Responsible for Transcriptional Induction of Mammalian Glucose-regulated Proteins

Yoshida, H., Haze, K., Yanagi, H., Yura, T., & Mori, K. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.50.33741 · Cited by 1,229

Diabetes Mellitus and Exocrine Pancreatic Dysfunction in Perk−/− Mice Reveals a Role for Translational Control in Secretory Cell Survival

Harding, H. P., Zeng, H., Zhang, Y., Jungries, R., Chung, P., Plesken, H., Sabatini, D. D., & Ron, D. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00264-7 · Cited by 1,217

XBP1, Downstream of Blimp-1, Expands the Secretory Apparatus and Other Organelles, and Increases Protein Synthesis in Plasma Cell Differentiation

Shaffer, A. L., Shelef, M. A., Iwakoshi, N. N., Lee, A., Qian, S., Zhao, H., Yu, X., Yang, L., Tan, B. K., Rosenwald, A., et al. (2004) · Immunity · doi:10.1016/j.immuni.2004.06.010 · Cited by 1,060

Aberrant lipid metabolism disrupts calcium homeostasis causing liver endoplasmic reticulum stress in obesity

Fu, S., Yang, L., Li, P., Hofmann, O., Dicker, L. H., Hide, W. A., Lin, X., Watkins, S. M., Ivanov, A. R., & Hotamışlıgil, G. S. (2011) · Nature · doi:10.1038/nature09968 · Cited by 1,045

Fatty Acid Trafficking in Starved Cells: Regulation by Lipid Droplet Lipolysis, Autophagy, and Mitochondrial Fusion Dynamics

Rambold, A. S., Cohen, S., & Lippincott-Schwartz, J. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.01.029 · Cited by 1,038

A Novel Mechanism for Regulating Activity of a Transcription Factor That Controls the Unfolded Protein Response

Cox, J. S., & Walter, P. (1996) · Cell · doi:10.1016/s0092-8674(00)81360-4 · Cited by 1,031

Regulated Ire1-dependent decay of messenger RNAs in mammalian cells

Hollien, J., Lin, J. H., Li, H., Stevens, N. S., Walter, P., & Weissman, J. S. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200903014 · Cited by 1,021

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

Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response

Lu, P. D., Harding, H. P., & Ron, D. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200408003 · Cited by 1,006

ER stress and the unfolded protein response in neurodegeneration

Hetz, C. A., & Saxena, S. (2017) · Nature Reviews Neurology · doi:10.1038/nrneurol.2017.99 · Cited by 1,006

TLR activation of the transcription factor XBP1 regulates innate immune responses in macrophages

Martinon, F., Chen, X., Lee, A.-H., & Glimcher, L. H. (2010) · Nature Immunology · doi:10.1038/ni.1857 · Cited by 996

A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cellsPreprint

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Structure and function of ER membrane contact sites with other organelles

Phillips, M. J., & Voeltz, G. K. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2015.8 · Cited by 933

Plasma cell differentiation and the unfolded protein response intersect at the transcription factor XBP-1

Iwakoshi, N. N., Lee, A.-H., Vallabhajosyula, P., Otipoby, K. L., Rajewsky, K., & Glimcher, L. H. (2003) · Nature Immunology · doi:10.1038/ni907 · Cited by 880

Mutations in filamin 1 Prevent Migration of Cerebral Cortical Neurons in Human Periventricular Heterotopia

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IRE1α Induces Thioredoxin-Interacting Protein to Activate the NLRP3 Inflammasome and Promote Programmed Cell Death under Irremediable ER Stress

Lerner, A. G., Upton, J.-P., Praveen, P. V. K., Ghosh, R., Nakagawa, Y., Igbaria, A., Shen, S., Nguyen, V. Q., Backes, B. J., Heiman, M., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.07.007 · Cited by 873

PERK is required at the ER-mitochondrial contact sites to convey apoptosis after ROS-based ER stress

Verfaillie, T., Rubio, N., Garg, A. D., Bultynck, G., Rizzuto, R., Decuypere, J.-P., Piette, J. G., Linehan, C., Gupta, S., Samali, A., et al. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.74 · Cited by 865

GRP78 Induction in Cancer: Therapeutic and Prognostic Implications

Lee, A. S. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-0325 · Cited by 856

Immunoglobulin heavy chain binding protein

Haas, I. G., & Wabl, M. R. (1983) · Nature · doi:10.1038/306387a0 · Cited by 852

IRE1α Kinase Activation Modes Control Alternate Endoribonuclease Outputs to Determine Divergent Cell Fates

Han, D., Lerner, A. G., Walle, L. V., Upton, J.-P., Xu, W., Hagen, A., Backes, B. J., Oakes, S. A., & Papa, F. R. (2009) · Journal of End-to-End-testing · doi:10.1016/j.cell.2009.07.017 · Cited by 848

XBP1 promotes triple-negative breast cancer by controlling the HIF1α pathway

Chen, X., Iliopoulos, D., Zhang, Q. H., Tang, Q., Greenblatt, M. B., Hatziapostolou, M., Lim, E., Tam, W. L., Ni, M., Chen, Y., et al. (2014) · Nature · doi:10.1038/nature13119 · Cited by 840

A transmembrane protein with a cdc2+CDC28-related kinase activity is required for signaling from the ER to the nucleus

Morl, K., Ma, W., Gething, M.-J. H., & Sambrook, J. (1993) · Cell · doi:10.1016/0092-8674(93)90521-q · Cited by 834

Adaptation to ER Stress Is Mediated by Differential Stabilities of Pro-Survival and Pro-Apoptotic mRNAs and Proteins

Rutkowski, D. T., Arnold, S. M., Miller, C. N., Wu, J., Li, J., Gunnison, K. M., Mori, K., Akha, A. A. S., Raden, D. L., & Kaufman, R. J. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040374 · Cited by 833

EIF2AK3, encoding translation initiation factor 2-α kinase 3, is mutated in patients with Wolcott-Rallison syndrome

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Cloning of mammalian Ire1 reveals diversity in the ER stress responses

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Noise Propagation in Gene Networks

Pedraza, J. M., & van Oudenaarden, A. (2005) · Science · doi:10.1126/science.1109090 · Cited by 796

Phosphorylation of initiation factor 2α by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast

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Identification and Characterization of Pancreatic Eukaryotic Initiation Factor 2 α-Subunit Kinase, PEK, Involved in Translational Control

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ER stress‐regulated translation increases tolerance to extreme hypoxia and promotes tumor growth

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Pharmacological brake-release of mRNA translation enhances cognitive memory

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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

Complementary Signaling Pathways Regulate the Unfolded Protein Response and Are Required for C. elegans Development

Shen, X., Ellis, R. E., Lee, K., Liu, C.-Y., Yang, K., Solomon, A., Yoshida, H., Morimoto, R., Kurnit, D. M., Mori, K., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00612-2 · Cited by 713

Unfolded Proteins Are Ire1-Activating Ligands That Directly Induce the Unfolded Protein Response

Gardner, B. M., & Walter, P. (2011) · Science · doi:10.1126/science.1209126 · Cited by 711

In and Out of the ER: Protein Folding, Quality Control, Degradation, and Related Human Diseases

Hebert, D. N., & Molinari, M. (2007) · Physiological Reviews · doi:10.1152/physrev.00050.2006 · Cited by 704

Thioredoxin-Interacting Protein Mediates ER Stress-Induced β Cell Death through Initiation of the Inflammasome

Oslowski, C. M., Hara, T., O’Sullivan-Murphy, B., Kanekura, K., Lu, S., Hara, M., Ishigaki, S., Zhu, L. J., Hayashi, E., Hui, S. T. Y., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.07.005 · Cited by 699

Chop deletion reduces oxidative stress, improves β cell function, and promotes cell survival in multiple mouse models of diabetes

Song, B., Scheuner, D., Ron, D., Pennathur, S., & Kaufman, R. J. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34587 · Cited by 698

Mammalian Genes Coordinately Regulated by Growth Arrest Signals and DNA-Damaging Agents

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Here, there, and everywhere: The importance of ER membrane contact sites

Wu, H., Carvalho, P., & Voeltz, G. K. (2018) · Science · doi:10.1126/science.aan5835 · Cited by 689

ATF6α Optimizes Long-Term Endoplasmic Reticulum Function to Protect Cells from Chronic Stress

Wu, J., Rutkowski, D. T., Dubois, M., Swathirajan, J., Saunders, T. L., Wang, J., Song, B., Yau, G. D.-Y., & Kaufman, R. J. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.07.005 · Cited by 680

Membrane lipid saturation activates endoplasmic reticulum unfolded protein response transducers through their transmembrane domains

Volmer, R., van der Ploeg, K., & Ron, D. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1217611110 · Cited by 668

Translational Repression Mediates Activation of Nuclear Factor Kappa B by Phosphorylated Translation Initiation Factor 2

Deng, J., Lu, P. D., Zhang, Y., Scheuner, D., Kaufman, R. J., Sonenberg, N., Harding, H. P., & Ron, D. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.23.10161-10168.2004 · Cited by 665

The unfolded protein response signals through high-order assembly of Ire1

Korennykh, A. V., Egea, P. F., Korostelev, A. A., Finer-Moore, J., Zhang, C., Shokat, K. M., Stroud, R. M., & Walter, P. (2009) · Nature · doi:10.1038/nature07661 · Cited by 656

XBP1

Sriburi, R., Jackowski, S., Mori, K., & Brewer, J. W. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200406136 · Cited by 653

IRE1α Cleaves Select microRNAs During ER Stress to Derepress Translation of Proapoptotic Caspase-2

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) · Science · doi:10.1126/science.1226191 · Cited by 640

Endoplasmic Reticulum Stress and the Hallmarks of Cancer

Urra, H., Dufey, E., Avril, T., Chevet, É., & Hetz, C. A. (2016) · Trends in cancer · doi:10.1016/j.trecan.2016.03.007 · Cited by 630

Sustained translational repression by eIF2α-P mediates prion neurodegeneration

Moreno, J. A., Radford, H. E., Peretti, D., Steinert, J. R., Verity, N., Martin, M. G., Halliday, M., Morgan, J., Dinsdale, D. D., Ortori, C. A., et al. (2012) · Nature · doi:10.1038/nature11058 · Cited by 616

On the mechanism of sensing unfolded protein in the endoplasmic reticulum

Credle, J. J., Finer-Moore, J. S., Papa, F. R., Stroud, R. M., & Walter, P. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509487102 · Cited by 606

Proteasome inhibitors disrupt the unfolded protein response in myeloma cells

Lee, A., Iwakoshi, N. N., Anderson, K. C., & Glimcher, L. H. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1334037100 · Cited by 606

XBP-1 Is a Cell-Nonautonomous Regulator of Stress Resistance and Longevity

Taylor, R. C., & Dillin, A. G. (2013) · Cell · doi:10.1016/j.cell.2013.05.042 · Cited by 585

UPR Pathways Combine to Prevent Hepatic Steatosis Caused by ER Stress-Mediated Suppression of Transcriptional Master Regulators

Rutkowski, D. T., Wu, J., Back, S.-H., Callaghan, M. U., Ferris, S. P., Iqbal, J., Clark, R. L., Miao, H. Z., Hassler, J. R., Fornek, J. L., et al. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.10.015 · Cited by 580

Opposing unfolded-protein-response signals converge on death receptor 5 to control apoptosis

Lu, M., Lawrence, D. A., Marsters, S. A., Acosta‐Alvear, D., Kimmig, P., Mendez, A. S., Paton, A. W., Paton, J. C., Walter, P., & Ashkenazi, A. (2014) · Science · doi:10.1126/science.1254312 · Cited by 579

Stress-Independent Activation of XBP1s and/or ATF6 Reveals Three Functionally Diverse ER Proteostasis Environments

Shoulders, M. D., Ryno, L. M., Genereux, J. C., Moresco, J. J., Tu, P. G., Wu, C., Yates, J. R., Su, A. I., Kelly, J. W., & Wiseman, R. L. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.03.024 · Cited by 558

XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy

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

Endoplasmic Reticulum Stress in Immunity

Bettigole, S. E., & Glimcher, L. H. (2014) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032414-112116 · Cited by 523

XBP‐1 is required for biogenesis of cellular secretory machinery of exocrine glands

Lee, A., Chu, G. C., Iwakoshi, N. N., & Glimcher, L. H. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600903 · Cited by 453

Mfn2 modulates the UPR and mitochondrial function via repression of PERK

Muñoz, J. P., Ivanova, S., Sánchez‐Wandelmer, J., Martínez‐Cristóbal, P., Noguera, E., Sancho, A., Díaz‐Ramos, A., Hernández‐Alvarez, M. I., Sebastián, D., Mauvezin, C., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.168 · Cited by 451

Endoplasmic Reticulum Stress Activates the Inflammasome via NLRP3- and Caspase-2-Driven Mitochondrial Damage

Bronner, D. N., Abuaita, B. H., Chen, X., Fitzgerald, K. A., Núñez, G., He, Y. O., Yin, X., & O’Riordan, M. X. (2015) · Immunity · doi:10.1016/j.immuni.2015.08.008 · Cited by 447

Regulation of insulin biosynthesis in pancreatic beta cells by an endoplasmic reticulum-resident protein kinase IRE1

Lipson, K. L., Fonseca, S. G., Ishigaki, S., Nguyen, L. X., Foss, E., Bortell, R., Rossini, A. A., & Urano, F. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.07.007 · Cited by 439

Fine-Tuning of the Unfolded Protein Response: Assembling the IRE1α Interactome

Hetz, C. A., & Glimcher, L. H. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.08.021 · Cited by 425

BiP Binding to the ER-Stress Sensor Ire1 Tunes the Homeostatic Behavior of the Unfolded Protein Response

Pincus, D., Chevalier, M. W., Aragón, T., van Anken, E., Vidal, S. E., El‐Samad, H., & Walter, P. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000415 · Cited by 419

UPR proteins IRE1 and PERK switch BiP from chaperone to ER stress sensor

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