The DOI matches its Crossref record; 50 of the 51 references it cites were found in a registry or an index.
Sigma-1 receptor chaperone at the ER-mitochondrion interface mediates the mitochondrion-ER-nucleus signaling for cellular survival.
Open accessAbstract
The membrane of the endoplasmic reticulum (ER) of a cell forms contacts directly with mitochondria whereby the contact is referred to as the mitochondrion-associated ER membrane or the MAM. Here we found that the MAM regulates cellular survival via an MAM-residing ER chaperone the sigma-1 receptor (Sig-1R) in that the Sig-1R chaperones the ER stress sensor IRE1 to facilitate inter-organelle signaling for survival. IRE1 is found in this study to be enriched at the MAM in CHO cells. We found that IRE1 is stabilized at the MAM by Sig-1Rs when cells are under ER stress. Sig-1Rs stabilize IRE1 and thus allow for conformationally correct IRE1 to dimerize into the long-lasting, activated endonuclease. The IRE1 at the MAM also responds to reactive oxygen species derived from mitochondria. Therefore, the ER-mitochondrion interface serves as an important subcellular entity in the regulation of cellular survival by enhancing the stress-responding signaling between mitochondria, ER, and nucleus.
Overview
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
Cites
Statistics
Verification
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?
In the citing paper
“Inside the cell Sig-1R is located mainly at the ER–mitochondrion interface—referred to as the MAM—and regulates cellular bioenergetics, particularly under stressful conditions (Su et al., 2010; Mori et al., 2013; Hayashi, 2015).”
From The therapeutic potentials of Ayahuasca: possible effects against various diseases of civilization (2016) · cites this paper as Mori et al., 2013
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
1 retracted
Proapoptotic BAX and BAK Modulate the Unfolded Protein Response by a Direct Interaction with IRE1α
Hetz, C. A., Bernasconi, P., Fisher, J. K., Lee, A., Bassik, M. C., Antonsson, B. E., Brandt, G. S., Iwakoshi, N. N., Schinzel, A. C., Glimcher, L. H., et al. (2006) · Science · doi:10.1126/science.1123480 · Cited by 688
RetractedControl of inositol 1,4,5-trisphosphate-induced Ca2+ release by cytosolic Ca2+
Bootman, M. D., Missiaen, L., Parys, J. B., SMEDT, H. D., & Casteels, R. (1995) · Biochemical Journal · doi:10.1042/bj3060445 · Cited by 5,131
Yoshida, H., Matsui, T., Yamamoto, A., Okada, T., & Mori, K. (2001) · Cell · doi:10.1016/s0092-8674(01)00611-0 · Cited by 4,054
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
THE MAMMALIAN UNFOLDED PROTEIN RESPONSE
Schröder, M., & Kaufman, R. J. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074134 · Cited by 3,099
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
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442
Close Contacts with the Endoplasmic Reticulum as Determinants of Mitochondrial Ca 2+ Responses
Rizzuto, R., Pinton, P., Carrington, W., Fay, F. S., Fogarty, K. E., Lifshitz, L. M., Tuft, R. A., & Pozzan, T. (1998) · Science · doi:10.1126/science.280.5370.1763 · Cited by 2,257
Hayashi, T., & Su, T.-P. (2007) · Cell · doi:10.1016/j.cell.2007.08.036 · Cited by 1,826
Self-citationIRE1 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
Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels
Szabadkai, G., Bianchi, K., Várnai, P., De Stefani, D., Wieckowski, M. R., Cavagna, D., Nagy, A. I., Balla, T., & Rizzuto, R. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200608073 · Cited by 1,413
Csordás, G., Renken, C. W., Várnai, P., Walter, L., Weaver, D., BUTTLE, K. F., Balla, T., Mannella, C. A., & Hajnóczky, G. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200604016 · Cited by 1,377
Oxidative protein folding in eukaryotes
Tu, B. P., & Weissman, J. S. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200311055 · Cited by 1,041
Cárdenas, C., Miller, R. A., Smith, I., Bui, T., Molgó, J., Müller, M., Vais, H., Cheung, K.-H., Yang, J., Parker, I., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.007 · Cited by 1,026
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
ER stress and neurodegenerative diseases
Lindholm, D., Wootz, H., & Korhonen, L. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401778 · Cited by 882
Patil, C., & Walter, P. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00219-2 · Cited by 779
Koppers, A. J., Iuliis, G. N. D., Finnie, J. M., McLaughlin, E. A., & Aitken, R. J. (2008) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2007-2616 · Cited by 699
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
The pharmacology of sigma-1 receptors.
Maurice, T., & Su, T.-P. (2009) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2009.07.001 · Cited by 654
Self-citationThe Hallucinogen N,N -Dimethyltryptamine (DMT) Is an Endogenous Sigma-1 Receptor Regulator
Fontanilla, D., Johannessen, M., Hajipour, A. R., Cozzi, N. V., Jackson, M. B., & Ruoho, A. E. (2009) · Science · doi:10.1126/science.1166127 · Cited by 535
Mitochondria Are a Major Source of Paraquat-induced Reactive Oxygen Species Production in the Brain
Castello, P. R., Drechsel, D. A., & Patel, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700827200 · Cited by 477
Rusiñol, A. E., Cui, Z., Chen, M. H., & Vance, J. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47012-3 · Cited by 476
A transgenic mouse model for monitoring endoplasmic reticulum stress
Iwawaki, T., Akai, R., Kohno, K., & Miura, M. (2003) · Nature Medicine · doi:10.1038/nm970 · Cited by 472
The sigma-1 receptor chaperone as an inter-organelle signaling modulator
Su, T., Hayashi, T., Maurice, T., Buch, S. J., & Ruoho, A. E. (2010) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2010.08.007 · Cited by 466
Self-citationA mutation in sigma‐1 receptor causes juvenile amyotrophic lateral sclerosis
Al-Saif, A. M., Al-Mohanna, F. A., & Bohlega, S. (2011) · Annals of Neurology · doi:10.1002/ana.22534 · Cited by 430
The Sigma Receptor as a Ligand-Regulated Auxiliary Potassium Channel Subunit
Aydar, E., Palmer, C. P., Klyachko, V. A., & Jackson, M. B. (2002) · Neuron · doi:10.1016/s0896-6273(02)00677-3 · Cited by 400
Zhou, J., Liu, C. Y., Back, S. H., Clark, R. L., Peisach, D., Xu, Z., & Kaufman, R. J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606480103 · Cited by 390
Flirting in Little Space: The ER/Mitochondria Ca 2+ Liaison
Rizzuto, R., Duchen, M. R., & Pozzan, T. (2004) · Science s STKE · doi:10.1126/stke.2152004re1 · Cited by 319
Induction of neuronal death by ER stress in Alzheimer’s disease
Katayama, T., Imaizumi, K., Manabe, T., Hitomi, J., Kudo, T., & Tohyama, M. (2004) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2003.12.004 · Cited by 292
IRE1 and efferent signaling from the endoplasmic reticulum
Urano, F., Bertolotti, A., & Ron, D. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.21.3697 · Cited by 270
Heat Shock Protein 90 Modulates the Unfolded Protein Response by Stabilizing IRE1α
Marcu, M. G., Doyle, M., Bertolotti, A., Ron, D., Hendershot, L. M., & Neckers, L. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.24.8506-8513.2002 · Cited by 236
Neuroprotective and anti-amnesic potentials of sigma (σ) receptor ligands
Maurice, T., & Lockhart, B. P. (1997) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/s0278-5846(96)00160-1 · Cited by 211
Kourrich, S., Hayashi, T., Chuang, J., Tsai, S., Su, T., & Bonci, A. (2013) · Cell · doi:10.1016/j.cell.2012.12.004 · Cited by 204
Self-citationThe sigma-1 receptor enhances brain plasticity and functional recovery after experimental stroke
Ruscher, K., Shamloo, M., Rickhag, M., Ladunga, I., Soriano, L., Gisselsson, L., Toresson, H., Ruslim-Litrus, L., Oksenberg, D., Urfer, R., et al. (2011) · Brain · doi:10.1093/brain/awq367 · Cited by 183
Tsai, S., Hayashi, T., Harvey, B. K., Wang, Y., Wu, W. W., Shen, R., Zhang, Y., Becker, K. G., Hoffer, B. J., & Su, T. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909089106 · Cited by 160
Self-citationYung, H. W., Korolchuk, S., Tolkovsky, A. M., Jones, D. S., & Burton, G. J. (2006) · The FASEB Journal · doi:10.1096/fj.06-6054com · Cited by 126
Liu, C. Y., Wong, H. N., Schauerte, J. A., & Kaufman, R. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112454200 · Cited by 122
Structure and Intermolecular Interactions of the Luminal Dimerization Domain of Human IRE1α
Liu, C. Y., Xu, Z., & Kaufman, R. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300418200 · Cited by 118
Ajmo, C. T., Vernon, D. O. L., Collier, L. A., Pennypacker, K. R., & Cuevas, J. (2006) · Current Neurovascular Research · doi:10.2174/156720206776875849 · Cited by 116
Ji, Y., Wang, H., Zhao, X., Wang, Q., Zhang, C., Zhang, Y., Zhao, M., Chen, Y., Meng, X., & Xu, D. (2011) · Toxicological Sciences · doi:10.1093/toxsci/kfr232 · Cited by 93
Sørensen, S., Ranheim, T., Bakken, K. S., Leren, T. P., & Kulseth, M. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507071200 · Cited by 89
Słodziński, H., Moran, L. B., Michael, G. J., Wang, B., Novoselov, S. S., Cheetham, M. E., Pearce, R. K. B., & Graeber, M. B. (2009) · PubMed · Cited by 75
Kakiuchi, C., Ishiwata, M., Hayashi, A., & Kato, T. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03772.x · Cited by 75
Mitochondrial Longevity Pathways
Hajnóczky, G., & Hoek, J. B. (2007) · Science · doi:10.1126/science.1138825 · Cited by 49
An Atypical Unfolded Protein Response in Heat Shocked Cells
Heldens, L., Hensen, S. M. M., Onnekink, C., van Genesen, S. T., Dirks, R. P., & Lubsen, N. H. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023512 · Cited by 39
FAD-linked presenilin-1 mutants impede translation regulation under ER stress
Yasuda, Y., Kudo, T., Katayama, T., Imaizumi, K., Yatera, M., Okochi, M., Yamamori, H., Matsumoto, N., Kida, T., Fukumori, A., et al. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00859-8 · Cited by 31
Ulfig, N., Steinbrecher, A., Stoltenburg, G., & Rezaie, P. (2007) · Neuropathology · doi:10.1111/j.1440-1789.2007.00856.x · Cited by 5
Flagged first, then by citations
1 of the 51 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Endoplasmic reticulum stress: molecular mechanism and therapeutic targets
Chen, X., Shi, C., He, M., Xiong, S., & Xia, X. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01570-w · Cited by 1,102
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
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
Mitochondria-associated membranes (MAMs) and inflammation
Missiroli, S., Patergnani, S., Caroccia, N., Pedriali, G., Perrone, M., Previati, M., Wieckowski, M. R., & Giorgi, C. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0027-2 · Cited by 398
The Sigma-1 Receptor as a Pluripotent Modulator in Living Systems
Su, T., Su, T., Nakamura, Y., & Tsai, S. (2016) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2016.01.003 · Cited by 324
Self-citation
Metadata
- Authors
- Mori, T., Hayashi, T., Hayashi, E., & Su, T.-P.
- Affiliations
- United States Department of Health and Human Services (US)
- Corresponding author
- Su, Tsung-Ping
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2013-10-18
- Volume
- 8
- Issue
- 10
- Pages
- e76941
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3799859
- OpenAlex
- W1994289493
- Cited by
- 317
- References
- 51
- Citations by year
- 2026: 22 · 2025: 24 · 2024: 20 · 2023: 29 · 2022: 26 · 2021: 38 · 2020: 33 · 2019: 34 · 2018: 18 · 2017: 29 · 2016: 16 · 2015: 10 · 2014: 17
- FWCI
- 8.51
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- PLoS ONE (publishedVersion, public-domain)
- Europe PMC (PubMed Central) (publishedVersion, public-domain)
- PubMed Central (publishedVersion, public-domain)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Funders
- U.S. Department of Health and Human Services
- National Institutes of Health
- National Institute on Drug Abuse
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacological Receptor Mechanisms and Effects
- Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
- Keywords
- sigma-1 receptor, mitochondria-associated membranes, endoplasmic reticulum, IRE1, endoplasmic reticulum stress, mitochondrial reactive oxygen species, molecular chaperones, protein stabilization, endonuclease activation, cell survival
- MeSH terms
- Sigma-1 Receptor, Animals, Cell Nucleus, Cell Survival, Cricetulus, Endoplasmic Reticulum, Endoribonucleases, Cricetinae, HeLa Cells, Humans, Immunohistochemistry, Intracellular Membranes, Mitochondria, Mutation, Protein Binding, Blotting, Western, Signal Transduction, CHO Cells, Protein Serine-Threonine Kinases, Reactive Oxygen Species, Receptors, sigma, Microscopy, Confocal, Molecular Chaperones, RNA Interference, Cell Line, Tumor, Mice
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