UPR, autophagy, and mitochondria crosstalk underlies the ER stress response

Senft, Daniela; Ronai, Ze’ev A.

doi:10.1016/j.tibs.2015.01.002

Cited by 1,121Endoplasmic Reticulum Stress and DiseaseAutophagy in Disease and TherapyIon Channels and Receptors

UPR, autophagy, and mitochondria crosstalk underlies the ER stress response

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Senft, Daniela, Ronai, Ze’ev A.·2015·Trends in Biochemical Sciences

DOI 10.1016/j.tibs.2015.01.002PMC PMC4340752

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Abstract

Cellular stress, induced by external or internal cues, activates several well-orchestrated processes aimed at either restoring cellular homeostasis or committing to cell death. Those processes include the unfolded protein response (UPR), autophagy, hypoxia, and mitochondrial function, which are part of the global endoplasmic reticulum (ER) stress (ERS) response. When one of the ERS elements is impaired, as often occurs under pathological conditions, overall cellular homeostasis may be perturbed. Further, activation of the UPR could trigger changes in mitochondrial function or autophagy, which could modulate the UPR, exemplifying crosstalk processes. Among the numerous factors that control the magnitude or duration of these processes are ubiquitin ligases, which govern overall cellular stress outcomes. Here we summarize crosstalk among the fundamental processes governing ERS responses.

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C. albicans cells utilize the UPR pathway to mitigate or manage ER stress, and it plays a crucial role in restoring homeostasis and normal ER function.
“To mitigate or manage ER stress, C. albicans cells utilize the UPR pathway, which plays a crucial role in restoring homeostasis and normal ER function [41].”
From Disruption of the UPC2 Gene Enhances Fluconazole Antifungal Activity by Inhibiting HAC1 mRNA Splicing in Candida albicans (2026) · cites this paper as [41]
In “ER stress, an overview” (page not available), the paper says the UPR is part of the cellular response to ER stress and plays a critical role in restoring homeostasis. It does not identify C. albicans as the cells using that pathway, so the species-specific part of the claim is not supported by this copy. (LLM, conf=0.88)
Experimental — accuracy not yet measured
Disruptions in ER homeostasis, such as accumulation of misfolded proteins or disturbances in Ca2+ signaling, activate the UPR pathway, an adaptive signaling pathway aimed at restoring proteostasis.
“Disruptions in ER homeostasis, such as the accumulation of misfolded proteins or disturbances in Ca2+ signaling, activate the UPR pathway, an adaptive signaling pathway aimed at restoring proteostasis [41].”
From Disruption of the UPC2 Gene Enhances Fluconazole Antifungal Activity by Inhibiting HAC1 mRNA Splicing in Candida albicans (2026) · cites this paper as [41]

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The E3 Ligase Smurf1 Regulates Wolfram Syndrome Protein Stability at the Endoplasmic Reticulum
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SUMO modification regulates the transcriptional activity of XBP1
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TRIM13 regulates caspase-8 ubiquitination, translocation to autophagosomes and activation during ER stress induced cell death
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Mitochondrial stress: Balancing friend and foe
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Cellular Inhibitor of Apoptosis Protein-1 (cIAP1) Plays a Critical Role in β-Cell Survival under Endoplasmic Reticulum Stress
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Activation of OASIS family, ER stress transducers, is dependent on its stabilization
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SENP1 deficiency promotes ER stress-induced apoptosis by increasing XBP1 SUMOylation
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A novel RING finger E3 ligase RNF186 regulate ER stress-mediated apoptosis through interaction with BNip1
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Fine Tuning of the UPR by the Ubiquitin Ligases Siah1/2
Scortegagna, M., Kim, H., Li, J.-L., Yao, H., Brill, L., Han, J., Lau, E., Bowtell, D., Haddad, G., Kaufman, R., et al. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004348 · Cited by 41 · see citing works
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Transcriptional cross talk between orphan nuclear receptor ERR and transmembrane transcription factor ATF6 coordinates endoplasmic reticulum stress response
Misra, J., Kim, D.-K., Choi, W., Koo, S., Lee, C.-H., Back, S.-H., Kaufman, R. J., & Choi, H.-S. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt429 · Cited by 38 · see citing works
Cyclophilin B is involved in p300-mediated degradation of CHOP in tumor cell adaptation to hypoxia
Jeong, K., Kim, H., Kim, K., Kim, S.-J., Hahn, B.-S., Jahng, G.-H., Yoon, K.-S., Kim, S. S., Ha, J., Kang, I., et al. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.164 · Cited by 35 · see citing works
ULK1 Regulates Melanin Levels in MNT-1 Cells Independently of mTORC1
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Temporal clustering of gene expression links the metabolic transcription factor HNF4α to the ER stress-dependent gene regulatory network
Arensdorf, A. M., DeZwaan-McCabe, D., Kaufman, R. J., & Rutkowski, D. T. (2013) · Frontiers in Genetics · doi:10.3389/fgene.2013.00188 · Cited by 24 · see citing works

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Proteasomal and Autophagic Degradation Systems
Đikić, I. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044908 · Cited by 1,165 · see citing works
Autophagy during viral infection — a double-edged sword
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New insights into the interplay between autophagy, gut microbiota and inflammatory responses in IBD
Larabi, A. B., Barnich, N., & Nguyen, H. T. T. (2019) · Autophagy · doi:10.1080/15548627.2019.1635384 · Cited by 840 · see citing works
Acute Kidney Injury
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Proteostasis control by the unfolded protein response
Hetz, C. A., Chevet, É., & Oakes, S. A. (2015) · Nature Cell Biology · doi:10.1038/ncb3184 · Cited by 754 · see citing works
Quality Control in the Endoplasmic Reticulum: Crosstalk between ERAD and UPR pathways
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Mitochondrial quality control in kidney injury and repair
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Cancer and ER stress: Mutual crosstalk between autophagy, oxidative stress and inflammatory response
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Photoinduced electron transfer (PeT) based fluorescent probes for cellular imaging and disease therapy
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Protein quality control in the secretory pathway
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Mitochondrial quality control mechanisms as molecular targets in cardiac ageing
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Mitofusin 2: from functions to disease
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Repairing mitochondrial dysfunction in disease
Sorrentino, V., Menzies, K. J., & Auwerx, J. (2018) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-104908 · Cited by 337 · see citing works
A Forward Vision for Chemodynamic Therapy: Issues and Opportunities
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Metal-based NanoEnhancers for Future Radiotherapy: Radiosensitizing and Synergistic Effects on Tumor Cells
Liu, Y., Zhang, P., Li, F., Jin, X., Li, J., Chen, W., & Li, Q. (2018) · Theranostics · doi:10.7150/thno.22172 · Cited by 335 · see citing works
ER and Nutrient Stress Promote Assembly of Respiratory Chain Supercomplexes through the PERK-eIF2α Axis
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Pleiotropic Effects of GLP-1 and Analogs on Cell Signaling, Metabolism, and Function
Rowlands, J., Heng, J., Newsholme, P., & Carlessi, R. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00672 · Cited by 302 · see citing works
Targeting autophagy to sensitive glioma to temozolomide treatment
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Regulators of mitochondrial dynamics in cancer
Senft, D., & Ronai, Z. A. (2016) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2016.02.001 · Cited by 295 · see citing works
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Signaling pathways in cancer metabolism: mechanisms and therapeutic targets
You, M., Xie, Z., Zhang, N., Zhang, Y., Xiao, D., Liu, S., Zhuang, W., Li, L., & Tao, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01442-3 · Cited by 297 · see citing works
BCL-2 family: integrating stress responses at the ER to control cell demise
Pihán, P., Carreras-Sureda, A., & Hetz, C. (2017) · Cell Death & Differentiation · doi:10.1038/cdd.2017.82 · Cited by 274 · see citing works
Research Advances in How the cGAS-STING Pathway Controls the Cellular Inflammatory Response
Wan, D., Jiang, W., & Hao, J. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00615 · Cited by 270 · see citing works
Molecular regulation of autophagy machinery by mTOR‐dependent and ‐independent pathways
Al‐Bari, M. A. A., & Xu, P. (2020) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.14305 · Cited by 265 · see citing works
Role of oxidative stress and antioxidants in daily nutrition and human health
Bjørklund, G., & Chirumbolo, S. (2016) · Nutrition · doi:10.1016/j.nut.2016.07.018 · Cited by 241 · see citing works
Therapeutic strategies of drug repositioning targeting autophagy to induce cancer cell death: from pathophysiology to treatment
Yoshida, G. J. (2017) · Journal of Hematology & Oncology · doi:10.1186/s13045-017-0436-9 · Cited by 237 · see citing works
Mitochondria-derived vesicles deliver antimicrobial reactive oxygen species to control phagosome-localized staphylococcus aureus
Abuaita, B. H., Schultz, T. L., & O’Riordan, M. X. (2018) · Cell Host & Microbe · doi:10.1016/j.chom.2018.10.005 · Cited by 223 · see citing works
FXR Inhibits Endoplasmic Reticulum Stress-Induced NLRP3 Inflammasome in Hepatocytes and Ameliorates Liver Injury
Han, C. Y., Rho, H. S., Kim, A., Kim, T. H., Jang, K., Jun, D. W., Kim, J., Kim, B., & Kim, S. G. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.07.068 · Cited by 233 · see citing works
Lipid Biosynthesis Coordinates a Mitochondrial-to-Cytosolic Stress Response
Kim, H.-E., Grant, A. R., Simic, M., Kohnz, R. A., Nomura, D. K., Durieux, J., Riera, C. E., Sanchez, M., Kapernick, E. A., Wolff, S., et al. (2016) · Cell · doi:10.1016/j.cell.2016.08.027 · Cited by 227 · see citing works
ROS-Scavenging Therapeutic Hydrogels for Modulation of the Inflammatory Response
Kim, Y. E., & Kim, J. (2021) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.1c18261 · Cited by 229 · see citing works
Toxic Effects of Nanoplastics with Different Sizes and Surface Charges on Epithelial-to-Mesenchymal Transition in A549 Cells and the Potential Toxicological Mechanism
Halimu, G., Zhang, Q., Xu, M., Zhang, Z., Wang, X., Gu, W., Li, Y., Dai, Y., Zhang, H., Dai, Y., et al. (2021) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2022.128485 · Cited by 224 · see citing works
Causal roles of mitochondrial dynamics in longevity and healthy aging
Sharma, A., Smith, H. J., Yao, P., & Mair, W. B. (2019) · EMBO Reports · doi:10.15252/embr.201948395 · Cited by 215 · see citing works
Obesity and insulin resistance: Pathophysiology and treatment
Tong, Y. A., Xu, S., Huang, L., & Chen, C. (2021) · Drug Discovery Today · doi:10.1016/j.drudis.2021.11.001 · Cited by 221 · see citing works
Endoplasmic reticulum proteostasis in hepatic steatosis
Baiceanu, A., Mesdom, P., Lagouge, M., & Foufelle, F. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2016.124 · Cited by 212 · see citing works
Gut dysbiosis, defective autophagy and altered immune responses in neurodegenerative diseases: Tales of a vicious cycle
Chidambaram, S. B., Essa, M. M., Rathipriya, A. G., Bishir, M., Ray, B., Mahalakshmi, A. M., Tousif, A. H., Sakharkar, M. K., Kashyap, R. S., Friedland, R. P., et al. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.107988 · Cited by 204 · see citing works
The Autophagy Lysosomal Pathway and Neurodegeneration
Finkbeiner, S. (2020) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033993 · Cited by 196 · see citing works
Epigenetic and post-translational modifications in autophagy: biological functions and therapeutic targets
Shu, F., Han, X., Li, Q.-N., Ren, X., Liu, Z., Hu, B., Wang, H., Wang, H., & Jiang, G. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01300-8 · Cited by 194 · see citing works
The role of oxidative stress in intervertebral disc degeneration: Mechanisms and therapeutic implications
Chen, X., Zhang, A., Zhao, K., Gao, H., Shi, P., Chen, Y., Cheng, Z., Zhou, W., & Zhang, Y. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102323 · Cited by 194 · see citing works
Hypoxia and Selective Autophagy in Cancer Development and Therapy
Daskalaki, I., Gkikas, I., & Tavernarakis, N. (2018) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2018.00104 · Cited by 188 · see citing works
Targeting autophagy, oxidative stress, and ER stress for neurodegenerative disease treatment
Esmaeili, Y., Yarjanli, Z., Paknia, F., Bidram, E., Łoś, M., Eshraghi, M., Klionsky, D. J., Ghavami, S., & Zarrabi, A. (2022) · Journal of Controlled Release · doi:10.1016/j.jconrel.2022.03.001 · Cited by 180 · see citing works
Endoplasmic reticulum stress—a key guardian in cancer
Zhang, W., Shi, Y., Oyang, L., Cui, S., Li, S., Li, J., Liu, L., Li, Y., Peng, M., Tan, S., et al. (2024) · Cell Death Discovery · doi:10.1038/s41420-024-02110-3 · Cited by 184 · see citing works
The N-Degron Pathway Mediates ER-phagy
Ji, C. H., Kim, H. Y., Heo, A. J., Lee, S. H., Lee, M. J., Kim, S., Srinivasrao, G., Mun, S. R., Cha‐Molstad, H., Ciechanover, A. J., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.06.028 · Cited by 162 · see citing works
Activation of immune signals during organ transplantation
Li, Q., & Lan, P. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01377-9 · Cited by 173 · see citing works
Mitochondrial – Endoplasmic reticulum interactions in the trophoblast: Stress and senescence
Burton, G. J., Yung, H. W., & Murray, A. J. (2016) · Placenta · doi:10.1016/j.placenta.2016.04.001 · Cited by 155 · see citing works
Why should neuroscientists worry about iron? The emerging role of ferroptosis in the pathophysiology of neuroprogressive diseases
Morris, G., Berk, M., Carvalho, A. F., Maes, M. H. J., Walker, A. J., & Puri, B. K. (2017) · Behavioural Brain Research · doi:10.1016/j.bbr.2017.12.036 · Cited by 154 · see citing works
Redox dynamics of manganese as a mitochondrial life-death switch
Smith, M. R., Fernandes, J., Go, Y., & Jones, D. P. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.10.126 · Cited by 150 · see citing works
Reactive oxygen species and ovarian diseases: Antioxidant strategies
Liang, J., Gao, Y., Feng, Z., Zhang, B., Na, Z., & Li, D. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102659 · Cited by 149 · see citing works
Triggers, cascades, and endpoints: connecting the dots of coral bleaching mechanisms
Helgoe, J., Davy, S. K., Weis, V. M., & Rodríguez‐Lanetty, M. (2024) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.13042 · Cited by 148 · see citing works
ENDOPLASMIC RETICULUM STRESS IN SEPSIS
Khan, M. M., Yang, W.-L., & Wang, P. (2015) · Shock · doi:10.1097/shk.0000000000000425 · Cited by 142 · see citing works
Adaptations of the human placenta to hypoxia: opportunities for interventions in fetal growth restriction
Colson, A., Sonveaux, P., Debiève, F., & Sferruzzi-Perri, A. N. (2020) · Human Reproduction Update · doi:10.1093/humupd/dmaa053 · Cited by 145 · see citing works
Doxorubicin impairs cardiomyocyte viability by suppressing transcription factor EB expression and disrupting autophagy
Bartlett, J. J., Trivedi, P. C., Yeung, P. K. F., Kienesberger, P. C., & Pulinilkunnil, T. (2016) · Biochemical Journal · doi:10.1042/bcj20160385 · Cited by 137 · see citing works
Oncogenic HSP60 regulates mitochondrial oxidative phosphorylation to support Erk1/2 activation during pancreatic cancer cell growth
Chao Hui, Z. H. O. U., Sun, H., Zheng, C., Gao, J., Fu, Q., Hu, N., Shao, X., Zhou, Y., Xiong, J., Nie, K., et al. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0196-z · Cited by 135 · see citing works
Mitochondria Retrograde Signaling and the UPRmt: Where Are We in Mammals?
Arnould, T., Michel, S., & Renard, P. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160818224 · Cited by 134 · see citing works
Potential of natural drug modulation of endoplasmic reticulum stress in the treatment of myocardial injury
Yang, K., Zhang, P., Li, J.-X., Zhang, G.-M., & Chang, X. (2024) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2024.101034 · Cited by 137 · see citing works
Targeting Proteotoxic Stress in Cancer: A Review of the Role that Protein Quality Control Pathways Play in Oncogenesis
Ho, M., Kavanagh, E. L., Dunne, L., Dowling, P., Zhang, L., Lindsay, S., Bazou, D., Goh, C. Y., Hanley, C., Bianchi, G., et al. (2019) · Cancers · doi:10.3390/cancers11010066 · Cited by 131 · see citing works
Shedding light on autophagy coordinating with cell wall integrity signaling to govern pathogenicity of Magnaporthe oryzae
Yin, Z., Feng, W., Chen, C., Xu, J., Li, Y., Yang, L., Wang, J., Liu, X., Wang, W., Gao, C., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1644075 · Cited by 131 · see citing works
Ubiquilins regulate autophagic flux through mTOR signalling and lysosomal acidification
Şentürk, M., Lin, G., Zuo, Z., Mao, D., Watson, E., Mikos, A. G., & Bellen, H. J. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0281-x · Cited by 124 · see citing works
IFN-γ-induced ER stress impairs autophagy and triggers apoptosis in lung cancer cells
Fang, C., Weng, T., Hu, S., Yuan, Z., Xiong, H., Huang, B. Y., Cai, Y., Li, L., & Fu, X. (2021) · OncoImmunology · doi:10.1080/2162402x.2021.1962591 · Cited by 127 · see citing works
Regulation of longevity by FGF21: interaction between energy metabolism and stress responses
Salminen, A., Kaarniranta, K., & Kauppinen, A. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2017.05.004 · Cited by 121 · see citing works
Polystyrene microplastics induced nephrotoxicity associated with oxidative stress, inflammation, and endoplasmic reticulum stress in juvenile rats
Wang, W., Guan, J., Feng, Y., Nie, L., Xu, Y., Xu, H., & Fu, F. (2023) · Frontiers in Nutrition · doi:10.3389/fnut.2022.1059660 · Cited by 121 · see citing works
The Roles of the Ubiquitin–Proteasome System in the Endoplasmic Reticulum Stress Pathway
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The Balance of MFN2 and OPA1 in Mitochondrial Dynamics, Cellular Homeostasis, and Disease
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Molecular Mechanisms of Bipolar Disorder: Progress Made and Future Challenges
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Progerin accelerates atherosclerosis by inducing endoplasmic reticulum stress in vascular smooth muscle cells
Hamczyk, M. R., Villa‐Bellosta, R., Quesada, V., Gonzalo, P., Vidak, S., Nevado, R. M., Andrés‐Manzano, M. J., Misteli, T., López-Otı́n, C., & Andrés, V. (2019) · EMBO Molecular Medicine · doi:10.15252/emmm.201809736 · Cited by 119 · see citing works
Adaptive Stress Responses During Tumor Metastasis and Dormancy
Senft, D., & Ronai, Z. A. (2016) · Trends in cancer · doi:10.1016/j.trecan.2016.06.004 · Cited by 111 · see citing works
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XBP1-mediated activation of the STING signalling pathway in macrophages contributes to liver fibrosis progression
Wang, Q., Bu, Q.-F., Liu, M., Zhang, R., Gu, J., Li, L., Zhou, J.-R., Liang, Y., Su, W., Liu, Z., et al. (2022) · JHEP Reports · doi:10.1016/j.jhepr.2022.100555 · Cited by 122 · see citing works
Curcumin induces ER stress-mediated apoptosis through selective generation of reactive oxygen species in cervical cancer cells
Kim, B., Kim, H. S., Jung, E., Lee, J., Tsang, B. K., Lim, J. M., & Song, Y. S. (2015) · Molecular Carcinogenesis · doi:10.1002/mc.22332 · Cited by 111 · see citing works
A Cold Stress Inducible PERK/OGT Axis Controls TOM70-Assisted Mitochondrial Protein Import and Cristae Formation
Latorre-Muro, P., O’Malley, K., Bennett, C., Perry, E. A., Balsa, E., Tavares, C. D. J., Jedrychowski, M. P., Gygi, S., & Puigserver, P. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2021.01.013 · Cited by 109 · see citing works
Noncanonical mitochondrial unfolded protein response impairs placental oxidative phosphorylation in early-onset preeclampsia
Yung, H. W., Colleoni, F., Dommett, E., Cindrová‐Davies, T., Kingdom, J. C., Murray, A. J., & Burton, G. J. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1907548116 · Cited by 110 · see citing works
Dehydrin MtCAS31 promotes autophagic degradation under drought stress
Li, X., Liu, Q., Feng, H., Deng, J., Zhang, R., Wen, J., Dong, J., & Wang, T. (2019) · Autophagy · doi:10.1080/15548627.2019.1643656 · Cited by 110 · see citing works
Vascular calcification: Molecular mechanisms and therapeutic interventions
Pan, W. D., Jie, W., & Huang, H. (2023) · MedComm · doi:10.1002/mco2.200 · Cited by 115 · see citing works
Intracellular APOL1 Risk Variants Cause Cytotoxicity Accompanied by Energy Depletion
Granado, D., Müller, D., Krausel, V., Kruzel-Davila, E., Schuberth, C. E., Eschborn, M., Wedlich‐Söldner, R., Skorecki, K. L., Pavenstädt, H. J., Michgehl, U., et al. (2017) · Journal of the American Society of Nephrology · doi:10.1681/asn.2016111220 · Cited by 107 · see citing works
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Authors: Senft, D., & Ronai, Z. A.
Affiliations: Sanford Burnham Prebys Medical Discovery Institute (US)
Corresponding author: Senft, Daniela
Ronai, Ze’ev A.
ORCID: Senft, Daniela
Ronai, Ze’ev A.
Venue: Trends in Biochemical Sciences
Publisher: Elsevier BV
Published: 2015-03
Volume: 40
Issue: 3
Pages: 141-148
ISSN: 0968-0004 (ISSN-L)
DOI: 10.1016/j.tibs.2015.01.002
PMC: PMC4340752
OpenAlex: W2019263782
Cited by: 1,121
References: 90
Citations by year: 2026: 84 · 2025: 116 · 2024: 113 · 2023: 148 · 2022: 130 · 2021: 107 · 2020: 105 · 2019: 95 · 2018: 72 · 2017: 70 · 2016: 61 · 2015: 20
FWCI: 7.45
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Trends in Biochemical Sciences (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Cancer Institute (P01CA128814, CA-128814, P30CA030199)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
Keywords: unfolded protein response, autophagy, mitochondrial function, endoplasmic reticulum stress, ubiquitin ligase, cellular stress response, cell death, cellular homeostasis
MeSH terms: Animals, Autophagy, Cell Physiological Phenomena, Humans, Mitochondria, Stress, Physiological, Unfolded Protein Response, Endoplasmic Reticulum Stress

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UPR, autophagy, and mitochondria crosstalk underlies the ER stress response

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