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

The DOI matches its Crossref record; 90 of the 90 references it cites were found in a registry or an index.

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

Open access

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

DOI 10.1016/j.tibs.2015.01.002PMC PMC4340752

Open this paper in CoChat — free account Open PDF

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.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1016/j.tibs.2015.01.002

Cites

90 of 90 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

1 retracted

RETRACTED: Autoadaptive ER-Associated Degradation Defines a Preemptive Unfolded Protein Response Pathway
Bernasconi, R., Galli, C., Kokame, K., & Molinari, M. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.10.016 · Cited by 21
Retracted
Autophagy: Renovation of Cells and Tissues
Mizushima, N., & Komatsu, M. (2011) · Cell · doi:10.1016/j.cell.2011.10.026 · Cited by 6,615
The unfolded protein response: controlling cell fate decisions under ER stress and beyond
Hetz, C. A. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3270 · Cited by 4,223
XBP1 mRNA Is Induced by ATF6 and Spliced by IRE1 in Response to ER Stress to Produce a Highly Active Transcription Factor
Yoshida, H., Matsui, T., Yamamoto, A., Okada, T., & Mori, K. (2001) · Cell · doi:10.1016/s0092-8674(01)00611-0 · Cited by 4,054
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026
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
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442
ER stress-induced cell death mechanisms
Sano, R., & Reed, J. C. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.06.028 · Cited by 1,988
Autophagosomes form at ER–mitochondria contact sites
Hamasaki, M., Furuta, N., Matsuda, A., Nezu, A., Yamamoto, A., Fujita, N., Oomori, H., Noda, T., Haraguchi, T., Hiraoka, Y., et al. (2013) · Nature · doi:10.1038/nature11910 · Cited by 1,683
Ubiquitin is phosphorylated by PINK1 to activate parkin
Koyano, F., Okatsu, K., Kosako, H., Tamura, Y., Go, E., Kimura, M., Kimura, Y., Tsuchiya, H., Yoshihara, H., Hirokawa, T., et al. (2014) · Nature · doi:10.1038/nature13392 · Cited by 1,477
The autophagosome: origins unknown, biogenesis complex
Lamb, C. A., Yoshimori, T., & Tooze, S. A. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3696 · Cited by 1,371
PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity
Kane, L. A., Lazarou, M., Fogel, A. I., Li, Y., Yamano, K., Sarraf, S. A., Banerjee, S., & Youle, R. J. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201402104 · Cited by 1,298
The eIF2α/ATF4 pathway is essential for stress-induced autophagy gene expression
B’chir, W., Maurin, A.-C., Carraro, V., Averous, J., Jousse, C., Muranishi, Y., Parry, L., Stepien, G., Fafournoux, P., & Bruhat, A. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt563 · Cited by 1,162
An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of parkin
Imai, Y., Soda, M., Inoue, H., Hattori, N., Mizuno, Y., & Takahashi, R. (2001) · Cell · doi:10.1016/s0092-8674(01)00407-x · Cited by 1,050
The eIF2α kinases: their structures and functions
Donnelly, N., Gorman, A. M., Gupta, S., & Samali, A. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1252-6 · Cited by 906
The PINK1/Parkin pathway regulates mitochondrial morphology
Poole, A. C., Thomas, R. E., Andrews, L. A., McBride, H. M., Whitworth, A. J., & Pallanck, L. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709336105 · Cited by 885
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
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
The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
Meacham, G. C., Patterson, C., Zhang, W., Younger, J. M., & Cyr, D. (2000) · Nature Cell Biology · doi:10.1038/35050509 · Cited by 839
Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65
Kazlauskaite, A., Kondapalli, C., Gourlay, R., Campbell, D. G., Ritorto, M. S., Hofmann, K., Alessi, D. R., Knebel, A., Trost, M., & Muqit, M. M. K. (2014) · Biochemical Journal · doi:10.1042/bj20140334 · Cited by 806
Paneth cells as a site of origin for intestinal inflammation
Adolph, T. E., Tomczak, M. F., Niederreiter, L., Ko, H.-J., Böck, J., Martinez-Naves, E., Glickman, J. N., Tschurtschenthaler, M., Hartwig, J., Hosomi, S., et al. (2013) · Nature · doi:10.1038/nature12599 · Cited by 732
The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila
Deng, H., Dodson, M. W., Huang, H., & Guo, M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803998105 · Cited by 707
Getting RIDD of RNA: IRE1 in cell fate regulation
Maurel, M., Chevet, É., Tavernier, J. H., & Gerlo, S. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2014.02.008 · Cited by 636
ER-associated degradation: Protein quality control and beyond
Ruggiano, A., Foresti, O., & Carvalho, P. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201312042 · Cited by 599
The critical roles of endoplasmic reticulum chaperones and unfolded protein response in tumorigenesis and anticancer therapies
Luo, B., & Lee, A. S. (2012) · Oncogene · doi:10.1038/onc.2012.130 · Cited by 580
CHIP Is Associated with Parkin, a Gene Responsible for Familial Parkinson's Disease, and Enhances Its Ubiquitin Ligase Activity
Imai, Y., Soda, M., Hatakeyama, S., Akagi, T., Hashikawa, T., Nakayama, K. I., & Takahashi, R. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00583-x · Cited by 477
Where the endoplasmic reticulum and the mitochondrion tie the knot: The mitochondria-associated membrane (MAM)
Raturi, A., & Simmen, T. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.04.013 · Cited by 470
Targeting ER stress–induced autophagy overcomes BRAF inhibitor resistance in melanoma
Ma, X.-H., Piao, S.-F., Dey, S., Mcafee, Q., Karakousis, G., Villanueva, J., Hart, L. S., Levi, S., Hu, J., Zhang, G., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci70454 · Cited by 457
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 in health and disease
Zhao, L., & Ackerman, S. L. (2006) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2006.06.005 · Cited by 447
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
Wolfram syndrome 1 gene negatively regulates ER stress signaling in rodent and human cells
Fonseca, S. G., Ishigaki, S., Oslowski, C. M., Lu, S., Lipson, K. L., Ghosh, R., Hayashi, E., Ishihara, H., Oka, Y., Permutt, M. A., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci39678 · Cited by 412
The accumulation of misfolded proteins in the mitochondrial matrix is sensed by PINK1 to induce PARK2/Parkin-mediated mitophagy of polarized mitochondria
Jin, S. M., & Youle, R. J. (2013) · Autophagy · doi:10.4161/auto.26122 · Cited by 411
Parkin, PINK1, and DJ-1 form a ubiquitin E3 ligase complex promoting unfolded protein degradation
Xiong, H., Wang, D., Chen, L., Choo, Y. S., Ma, H., Tang, C., Xia, K., Jiang, W. B., Ronai, Z. A., Zhuang, X., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci37617 · Cited by 406
Self-citation
Siah2 Regulates Stability of Prolyl-Hydroxylases, Controls HIF1α Abundance, and Modulates Physiological Responses to Hypoxia
Nakayama, K., Frew, I. J., Hagensen, M. K., Skals, M., Habelhah, H., Bhoumik, A., Kadoya, T., Erdjument‐Bromage, H., Tempst, P., Frappell, P. B., et al. (2004) · Cell · doi:10.1016/j.cell.2004.06.001 · Cited by 406
Self-citation
Cleaning up in the endoplasmic reticulum: ubiquitin in charge
Christianson, J. C., & Ye, Y. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2793 · Cited by 400
Regulation of basal cellular physiology by the homeostatic unfolded protein response
Rutkowski, D. T., & Hegde, R. S. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201003138 · Cited by 382
New functions of mitochondria associated membranes in cellular signaling
van Vliet, A. R., Verfaillie, T., & Agostinis, P. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.03.009 · Cited by 353
Parkin is transcriptionally regulated by ATF4: evidence for an interconnection between mitochondrial stress and ER stress
Bouman, L., Schlierf, A., Lutz, A. K., Shan, J., Deinlein, A., Kast, J., Galehdar, Z., Palmisano, V., Patenge, N., Berg, D., et al. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.142 · Cited by 347
The Unfolded Protein Response Mediates Adaptation to Exercise in Skeletal Muscle through a PGC-1α/ATF6α Complex
Wu, J., Ruas, J. L., Estall, J. L., Rasbach, K. A., Choi, J. H., Ye, L., Boström, P., Tyra, H. M., Crawford, R. W., Campbell, K. P., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.01.003 · Cited by 312
Regulation of glucose homeostasis through a XBP-1–FoxO1 interaction
Zhou, Y., Lee, J., Reno, C. M., Sun, C., Park, S. W., Chung, J., Lee, J., Fisher, S. J., White, M. F., Biddinger, S. B., et al. (2011) · Nature Medicine · doi:10.1038/nm.2293 · Cited by 306
MITOL Regulates Endoplasmic Reticulum-Mitochondria Contacts via Mitofusin2
Sugiura, A., Nagashima, S., Tokuyama, T., Amo, T., Matsuki, Y., Ishido, S., Kudo, Y., McBride, H. M., Fukuda, T., Matsushita, N., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.04.023 · Cited by 303
The endoribonuclease activity of mammalian IRE1 autoregulates its mRNA and is required for the unfolded protein responsePreprint
Tirasophon, W., Lee, K., Callaghan, B. C., Welihinda, A. A., & Kaufman, R. J. (2000) · Genes & Development · doi:10.1101/gad.839400 · Cited by 288
Targeting the UPR transcription factor XBP1 protects against Huntington's disease through the regulation of FoxO1 and autophagy
Vidal, R. L., Figueroa, A., Court, F. A., Thielen, P., Molina, C., Wirth, C., Caballero, B., Kiffin, R., Segura‐Aguilar, J., Cuervo, A. M., et al. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds040 · Cited by 286
Stress-induced self-cannibalism: on the regulation of autophagy by endoplasmic reticulum stress
Deegan, S., Saveljeva, S., Gorman, A. M., & Samali, A. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1173-4 · Cited by 280
Transcriptional Regulation of VEGF-A by the Unfolded Protein Response Pathway
Ghosh, R., Lipson, K. L., Sargent, K. E., Mercurio, A. M., Hunt, J. S., Ron, D., & Urano, F. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009575 · Cited by 276
Retention of mutant α 1 -antitrypsin Z in endoplasmic reticulum is associated with an autophagic response
Teckman, J. H., & Perlmutter, D. H. (2000) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.2000.279.5.g961 · Cited by 275
Endoplasmic reticulum stress induced by tunicamycin and thapsigargin protects against transient ischemic brain injury
Zhang, X., Yuan, Y., Jiang, L., Zhang, J., Gao, J., Shen, Z., Zheng, Y., Deng, T., Yan, H., Li, W., et al. (2014) · Autophagy · doi:10.4161/auto.32136 · Cited by 259
Fine-Tuning of Drp1/Fis1 Availability by AKAP121/Siah2 Regulates Mitochondrial Adaptation to Hypoxia
Kim, H., Scimia, M. C., Wilkinson, D., Díaz-Trelles, R., Wood, M. R., Bowtell, D. D. L., Dillin, A. G., Mercola, M. A., & Ronai, Z. A. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.045 · Cited by 247
Self-citation
Enhanced parkin levels favor ER-mitochondria crosstalk and guarantee Ca2+ transfer to sustain cell bioenergetics
Calí, T., Ottolini, D., Negro, A., & Brini, M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.01.004 · Cited by 231
SENP3‐mediated deSUMOylation of dynamin‐related protein 1 promotes cell death following ischaemia
Guo, C., Hildick, K. L., Luo, J., Dearden, L., Wilkinson, K. A., & Henley, J. M. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.65 · Cited by 229
Gp78 Cooperates with RMA1 in Endoplasmic Reticulum-associated Degradation of CFTRΔF508
Morito, D., Hirao, K., Oda, Y., Hosokawa, N., Tokunaga, F., Cyr, D., Tanaka, K., Iwaï, K., & Nagata, K. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-06-0601 · Cited by 224
VEGF Signals through ATF6 and PERK to Promote Endothelial Cell Survival and Angiogenesis in the Absence of ER Stress
Karali, E., Bellou, S., Stellas, D., Klinakis, A., Murphy, C., & Fotsis, T. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.022 · Cited by 214
The signalling from endoplasmic reticulum-resident bZIP transcription factors involved in diverse cellular physiology
Asada, R., Kanemoto, S., Kondo, S., Saito, A., & Imaizumi, K. (2011) · The Journal of Biochemistry · doi:10.1093/jb/mvr041 · Cited by 203
Oxidized lipids activate autophagy in a JNK-dependent manner by stimulating the endoplasmic reticulum stress response
Haberzettl, P., & Hill, B. G. (2013) · Redox Biology · doi:10.1016/j.redox.2012.10.003 · Cited by 200
Stress-responsive regulation of mitochondria through the ER unfolded protein response
Rainbolt, T. K., Saunders, J. M., & Wiseman, R. L. (2014) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2014.06.007 · Cited by 188
Quality Control Autophagy Degrades Soluble ERAD-Resistant Conformers of the Misfolded Membrane Protein GnRHR
Houck, S. A., Ren, H. Y., Madden, V. J., Bonner, J. N., Conlin, M. P., Janovick, J. A., Conn, P. M., & Cyr, D. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.02.025 · Cited by 155
Vemurafenib Potently Induces Endoplasmic Reticulum Stress–Mediated Apoptosis in BRAFV600E Melanoma Cells
Beck, D., Niessner, H., Smalley, K. S. M., Flaherty, K. T., Paraiso, K. H. T., Busch, C., Sinnberg, T. W., Vasseur, S., Iovanna, J., Drießen, S., et al. (2013) · Science Signaling · doi:10.1126/scisignal.2003057 · Cited by 153
The TRC8 E3 ligase ubiquitinates MHC class I molecules before dislocation from the ER
Stagg, H. R., Thomas, M., van den Boomen, D. J. H., Wiertz, E. J. H. J., Drabkin, H. A., Gemmill, R. M., & Lehner, P. J. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200906110 · Cited by 152
Endoplasmic reticulum stress triggers autophagy in malignant glioma cells undergoing cyclosporine A-induced cell death
Ciechomska, I. A., Gabrusiewicz, K. R., Szczepankiewicz, A. A., & Kaminska, B. (2012) · Oncogene · doi:10.1038/onc.2012.174 · Cited by 144
Endoplasmic reticulum stress activates autophagy but not the proteasome in neuronal cells: implications for Alzheimer's disease
Nijholt, D. A. T., de Graaf, T. R., van Haastert, E. S., Oliveira, A. O., Berkers, C. R., Zwart, R., Ovaa, H., Baas, F., Hoozemans, J. J. M., & Scheper, W. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2010.176 · Cited by 139
Emerging roles of E3 ubiquitin ligases in autophagy
Kuang, E., Qi, J., & Ronai, Z. A. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.06.008 · Cited by 125
Self-citation
A high-coverage shRNA screen identifies TMEM129 as an E3 ligase involved in ER-associated protein degradation
van de Weijer, M. L., Bassik, M. C., Luteijn, R. D., Voorburg, C. M., Lohuis, M. A. M., Kremmer, E., Hoeben, R. C., LeProust, E. M., Chen, S., Hoelen, H., et al. (2014) · Nature Communications · doi:10.1038/ncomms4832 · Cited by 123
De-Differentiation Confers Multidrug Resistance Via Noncanonical PERK-Nrf2 Signaling
Fitz, C. D. V., Feng, Y., Sokol, E. S., Tillman, E. J., Sanduja, S., Reinhardt, F., & Gupta, P. B. (2014) · PLoS Biology · doi:10.1371/journal.pbio.1001945 · Cited by 121
Synoviolin promotes IRE1 ubiquitination and degradation in synovial fibroblasts from mice with collagen‐induced arthritis
Gao, B., Lee, S., Chen, A., Zhang, J., Zhang, D. D., Kannan, K., Ortmann, R., & Fang, D. (2008) · EMBO Reports · doi:10.1038/embor.2008.37 · Cited by 116
Signal peptide peptidase functions in ERAD to cleave the unfolded protein response regulator XBP1u
Chen, C., Malchus, N. S., Hehn, B., Stelzer, W., Avci, D., Langosch, D., & Lemberg, M. K. (2014) · The EMBO Journal · doi:10.15252/embj.201488208 · Cited by 115
XBP-1u suppresses autophagy by promoting the degradation of FoxO1 in cancer cells
Zhao, Y., Li, X., Cai, M.-Y., Ma, K., Yang, J. H., Zhou, J., Fu, W., Wei, F.-Z., Wang, L., Xie, D., et al. (2013) · Cell Research · doi:10.1038/cr.2013.2 · Cited by 114
TMEM129 is a Derlin-1 associated ERAD E3 ligase essential for virus-induced degradation of MHC-I
van den Boomen, D. J. H., Timms, R. T., Grice, G. L., Stagg, H. R., Skjødt, K., Dougan, G., Nathan, J. A., & Lehner, P. J. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1409099111 · Cited by 109
The RBCC GeneRFP2(Leu5) Encodes a Novel Transmembrane E3 Ubiquitin Ligase Involved in ERAD
Lerner, M., Corcoran, M., Cepeda, D., Nielsen, M. L., Zubarev, R. A., Pontén, F., Uhlén, M., Hober, S., Grandér, D., & Sangfelt, O. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-03-0248 · Cited by 109
RNF185 Is a Novel E3 Ligase of Endoplasmic Reticulum-associated Degradation (ERAD) That Targets Cystic Fibrosis Transmembrane Conductance Regulator (CFTR)
Khouri, E. E., Pavec, G. L., Tolédano, M. B., & Delaunay, A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.470500 · Cited by 106
TRIM13 regulates ER stress induced autophagy and clonogenic ability of the cells
Tomar, D., Singh, R. K., Singh, A. K., Pandya, C. D., & Singh, R. K. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.11.015 · Cited by 102
ER-stress-associated functional link between Parkin and DJ-1 via a transcriptional cascade involving the tumor suppressor p53 and the spliced X-box binding protein XBP-1
Duplan, E., Giaime, E., Viotti, J., Sévalle, J., Corti, O., Brice, A., Ariga, H., Qi, L., Checler, F., & da Costa, C. A. (2013) · Journal of Cell Science · doi:10.1242/jcs.127340 · Cited by 91
Yessotoxin induces ER-stress followed by autophagic cell death in glioma cells mediated by mTOR and BNIP3
Rubiolo, J. A., López‐Alonso, H., Martínez, P., Millán, A., Cagide, E., Vieytes, M. R., Vega, F. V., & Botana, L. M. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.10.004 · Cited by 90
Xbp1-Independent Ire1 Signaling Is Required for Photoreceptor Differentiation and Rhabdomere Morphogenesis in Drosophila
Coelho, D. S., Cairrão, F., Zeng, X., Pires, E., Coelho, A. V., Ron, D., Ryoo, H. D., & Domingos, P. M. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.09.046 · Cited by 85
The E3 Ligase Smurf1 Regulates Wolfram Syndrome Protein Stability at the Endoplasmic Reticulum
Guo, X. L., Shen, S., Song, S., He, S., Cui, Y., Xing, G., Wang, J., Yin, Y., Fan, L., He, F., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.225615 · Cited by 76
Vascular endothelial growth factor–induced elimination of the type 1 interferon receptor is required for efficient angiogenesis
Zheng, H., Qian, J., Carbone, C. J., Leu, N. A., Baker, D. P., & Fuchs, S. Y. (2011) · Blood · doi:10.1182/blood-2011-06-359745 · Cited by 74
SUMO modification regulates the transcriptional activity of XBP1
Chen, H., & Qi, L. (2010) · Biochemical Journal · doi:10.1042/bj20100193 · Cited by 74
TRIM13 regulates caspase-8 ubiquitination, translocation to autophagosomes and activation during ER stress induced cell death
Tomar, D., Prajapati, P., Sripada, L., Singh, K., Singh, R. K., Singh, A. K., & Singh, R. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.08.021 · Cited by 70
Anti-tumorigenic effects of Type 1 interferon are subdued by integrated stress responses
Bhattacharya, S., HuangFu, W.-C., Dong, G., Qian, J., Baker, D. P., Karar, J., Koumenis, C., Diehl, J. A., & Fuchs, S. Y. (2012) · Oncogene · doi:10.1038/onc.2012.439 · Cited by 68
Regulation of Endoplasmic Reticulum-associated Degradation by RNF5-dependent Ubiquitination of JNK-associated Membrane Protein (JAMP)
Tcherpakov, M., Delaunay, A., Toth, J. I., Kadoya, T., Petroski, M. D., & Ronai, Z. A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808222200 · Cited by 67
Self-citation
Mitochondrial stress: Balancing friend and foe
Runkel, E. D., Baumeister, R., & Schulze, E. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2014.02.013 · Cited by 59
Cellular Inhibitor of Apoptosis Protein-1 (cIAP1) Plays a Critical Role in β-Cell Survival under Endoplasmic Reticulum Stress
Qi, Y., & Xia, P. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.362160 · Cited by 51
Activation of OASIS family, ER stress transducers, is dependent on its stabilization
Kondo, S., Hino, S.-I., Saito, A., Kanemoto, S., Kawasaki, N., Asada, R., Izumi, S., Iwamoto, H., Oki, M., Miyagi, H., et al. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.77 · Cited by 49
Fine Tuning of the UPR by the Ubiquitin Ligases Siah1/2
Scortegagna, M., Kim, H., Li, J., Yao, H., Brill, L. M., Han, J., Lau, E. K., Bowtell, D. D. L., Haddad, G., Kaufman, R. J., et al. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004348 · Cited by 43
Self-citation
SENP1 deficiency promotes ER stress-induced apoptosis by increasing XBP1 SUMOylation
Jiang, Z., Fan, Q., Zhang, Z., Zou, Y., Cai, R., Wang, Q., Zuo, Y., & Cheng, J. (2012) · Cell Cycle · doi:10.4161/cc.11.6.19529 · Cited by 42
A novel RING finger E3 ligase RNF186 regulate ER stress-mediated apoptosis through interaction with BNip1
Wang, P., Wu, Y., Li, Y., Zheng, J., & Tang, J. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.07.016 · Cited by 42
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 39
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
ULK1 Regulates Melanin Levels in MNT-1 Cells Independently of mTORC1
Kalie, E., Razi, M., & Tooze, S. A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075313 · Cited by 34
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

Sorted by citations

Proteasomal and Autophagic Degradation Systems
Đikić, I. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044908 · Cited by 1,217
Autophagy during viral infection — a double-edged sword
Choi, Y., Bowman, J. W., & Jung, J. U. (2018) · Nature Reviews Microbiology · doi:10.1038/s41579-018-0003-6 · Cited by 838
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 860
Acute Kidney Injury
Żuk, A., & Bonventre, J. V. (2016) · Annual Review of Medicine · doi:10.1146/annurev-med-050214-013407 · Cited by 776
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 790

See all 1,121

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
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › 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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks