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Synthetic lethal screening identifies compounds activating iron-dependent, nonapoptotic cell death in oncogenic-RAS-harboring cancer cells.
Open accessAbstract
We screened small molecules to identify two compounds, which we named RSL3 and RSL5, that have increased lethality in the presence of oncogenic RAS. Counter screening with biologically active compounds defined aspects of the mechanism of action for RSL3 and RSL5, such as a nonapoptotic, MEK-dependent, and iron-dependent oxidative cell death. Erastin, a previously reported compound with RAS-selective lethality, showed similar properties. RNA interference experiments targeting voltage-dependent anion channel 3 (VDAC3), a target of erastin, demonstrated that RSL5 is a scaffold that acts through VDACs to activate the observed pathway. RSL3 activated a similar death mechanism but in a VDAC-independent manner. We found that cells transformed with oncogenic RAS have increased iron content relative to their normal cell counterparts through upregulation of transferrin receptor 1 and downregulation of ferritin heavy chain 1 and ferritin light chain.
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In the citing paper
“Under normal circumstances, glutathione peroxidase (GPX) neutralizes lipid peroxide to lipid alcohols, but the depletion of intracellular glutathione (GSH, GPX substrate) reduces GPX functionality (Yang and Stockwell, 2008; Friedmann Angeli et al., 2014).”
From Toxic Concentrations of Glutamate Induce Ferroptosis without Affecting Mitochondrial Respiration in Rodent Brain Slice Cultures (2026) · cites this paper as Yang and Stockwell, 2008
Experimental — accuracy not yet measuredIn the citing paper
“the ferroptosis-inhibiting effect of iron depletion by either chelators [539, 543, 548] or phosphorylase kinase catalytic subunit gamma 2 (PHKG2) knockdown [566]”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [543]
In the citing paper
“The mode of cell death induced by these compounds was surprisingly found to be non-apoptotic, as cells treated with erastin and RSL3 died in the absence of apoptotic hallmarks [11, 12, 13], and in cells where the core apoptosis machinery – caspases, BAX, and BAK was suppressed [14].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [12]
In the citing paper
“The first ferroptosis-inducing compounds, erastin [11] and RSL3 [12], were discovered using high-throughout screening of small molecule libraries [11, 12].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [12]
In the citing paper
“Cell death induced by RSL3 shares common features with erastin-mediated ferroptosis, such as iron, MEK, and ROS dependencies [12].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [12]
In the citing paper
“Moreover, iron chelators were identified as inhibitors of cell death induction, after RSL3 treatment, revealing the requirement of cellular iron [12].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [12]
In the citing paper
“Cells are also desensitized to ferroptosis through genetic silencing of iron uptake (TfR1), metabolism (IRP2 and ISCU) and storage (ferritin) genes [62], [66], [82], or through depletion of transferrin in the extracellular environment [83].”
From Iron accumulation in senescent cells is coupled with impaired ferritinophagy and inhibition of ferroptosis (2018) · cites this paper as [66]
In the citing paper
“Cell death elicited by ferroptosis-inducing compounds (FINs) (e.g. erastin and RSL3) can also be mitigated through various iron chelators (Dfo, 2,2-bipyridile or compound 311) [62], [66], [81].”
From Iron accumulation in senescent cells is coupled with impaired ferritinophagy and inhibition of ferroptosis (2018) · cites this paper as [66]
In the citing paper
“Ferroptosis, a unique cell death pathway distinct from apoptosis [62], [66], [80], is reliant on the availability of iron [62], [66], [81] liberated through ferritinophagy [63].”
From Iron accumulation in senescent cells is coupled with impaired ferritinophagy and inhibition of ferroptosis (2018) · cites this paper as [66]
In the citing paper
“two structurally different inducers of ferroptosis that affect distinct pathways [66].”
From Iron accumulation in senescent cells is coupled with impaired ferritinophagy and inhibition of ferroptosis (2018) · cites this paper as [66]
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Cites
Specific killing of BRCA2-deficient tumours with inhibitors of poly(ADP-ribose) polymerase
Bryant, H. E., Schultz, N., Thomas, H. D., Parker, K. M., Flower, D., Lopez, E., Kyle, S., Meuth, M., Curtin, N. J., & Helleday, T. (2005) · Nature · doi:10.1038/nature03443 · Cited by 5,198
The ferritins: molecular properties, iron storage function and cellular regulation
Harrison, P. M., & Arosio, P. (1996) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(96)00022-9 · Cited by 2,667
Creation of human tumour cells with defined genetic elements
Hahn, W. C., Counter, C. M., Lundberg, A. S., Beijersbergen, R. L., Brooks, M. W., & Weinberg, R. A. (1999) · Nature · doi:10.1038/22780 · Cited by 2,345
Systematic Genetic Analysis with Ordered Arrays of Yeast Deletion Mutants
Tong, A. H. Y., Evangelista, M., Parsons, A. B., Xu, H., Bader, G. D., Pagé, N., Robinson, M., Raghibizadeh, S., Hogue, C. W. V., Bussey, H., et al. (2001) · Science · doi:10.1126/science.1065810 · Cited by 2,138
A Lentiviral RNAi Library for Human and Mouse Genes Applied to an Arrayed Viral High-Content Screen
Moffat, J., Grueneberg, D. A., Yang, X., Kim, S. Y., Kloepfer, A. M., Hinkle, G., Piqani, B., Eisenhaure, T., Luo, B., Grenier, J. K., et al. (2006) · Cell · doi:10.1016/j.cell.2006.01.040 · Cited by 1,804
Self-citationDiscovery and development of sorafenib: a multikinase inhibitor for treating cancer
Wilhelm, S., Carter, C. A., Lynch, M., Lowinger, T., Dumas, J., Smith, R., Schwartz, B., Simantov, R., & Kelley, S. (2006) · Nature reviews. Drug discovery · doi:10.1038/nrd2130 · Cited by 1,651
RAS–RAF–MEK-dependent oxidative cell death involving voltage-dependent anion channels
Yagoda, N., von Rechenberg, M., Zaganjor, E., Bauer, A. J., Yang, W. S., Fridman, D. J., Wolpaw, A. J., Smukste, I., Peltier, J. M., Boniface, J. J., et al. (2007) · Nature · doi:10.1038/nature05859 · Cited by 1,631
Self-citationDolma, S., Lessnick, S. L., Hahn, W. C., & Stockwell, B. R. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00050-3 · Cited by 1,446
Self-citationEnhanced sensitivity of PTEN-deficient tumors to inhibition of FRAP/mTOR
Neshat, M. S., Mellinghoff, I. K., Tran, C., Stiles, B. L., THOMAS, G. V., Petersen, R., Frost, P., Gibbons, J. J., Wu, H., & Sawyers, C. L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.171076798 · Cited by 971
Paull, K. D., Shoemaker, R. H., Hodes, L., Monks, A. P., Scudiero, D. A., Rubinstein, L., Plowman, J., & Boyd, M. R. (1989) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/81.14.1088 · Cited by 970
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Chakraborty, A., Yang, L., Zhang, C., Li, Y., LeMaire, S. A., & Shen, Y. H. (2021) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2021.09.010 · Cited by 95
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The role of ferroptosis in intervertebral disc degeneration
Fan, C., Chu, G., Yu, Z., Ji, Z., Kong, F., Yao, L., Wang, J., Geng, D., Wu, X., & Mao, H. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1219840 · Cited by 94
Targeting FSP1 triggers ferroptosis in lung cancer
Wu, K., Vaughan, A. J., Bossowski, J. P., Hao, Y., Ziogou, A., Kim, S. M., Kim, T. H., Nakamura, M. N., Pillai, R., Mancini, M. C. S., et al. (2025) · Nature · doi:10.1038/s41586-025-09710-8 · Cited by 102
Wu, Y., Torabi, S.-F., Lake, R. J., Hong, S., Yu, Z., Wu, P., Yang, Z., Nelson, K., Guo, W., Pawel, G. T., et al. (2023) · Science Advances · doi:10.1126/sciadv.ade7622 · Cited by 91
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Ferritinophagy, a form of autophagic ferroptosis: New insights into cancer treatment
Sun, K., Li, C., Liao, S., Yao, X., Ouyang, Y., Liu, Y., Wang, Z., Li, Z., & Yao, F. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1043344 · Cited by 101
Wang, Z., Li, R., Hou, N., Zhang, J., Wang, T., Fan, P., Ji, C., Zhang, B., Liu, L., Wang, Y., et al. (2023) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2023-006890 · Cited by 92
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Aguirre, A. J., & Hahn, W. C. (2018) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a031518 · Cited by 90
Zeng, Y., Hu, Q., Zhuo, Q., Zhu, Y., Fan, G., Liu, M., Sun, Q., Zhang, Z., Liu, W., Xu, W., et al. (2020) · PubMed Central · Cited by 89
Ferroptosis: Cancer Stem Cells Rely on Iron until “to Die for” It
Cosialls, E., Elhage, R., Santos, L. D., Gong, C., Mehrpour, M., & Hamaï, A. (2021) · Cells · doi:10.3390/cells10112981 · Cited by 94
Ebrahimi, N., Adelian, S., Shakerian, S., Afshinpour, M., Chaleshtori, S. R., Ravari, N. R., Rezaei‐Tazangi, F., Beiranvand, S., Hamblin, M. R., & Aref, A. R. (2022) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2022.01.006 · Cited by 91
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Reed, J. C., & Pellecchia, M. (2012) · Cell · doi:10.1016/j.cell.2012.05.009 · Cited by 87
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Gillen, K. M., Mubarak, M., Nguyen, T. D., & Pitt, D. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00255 · Cited by 88
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Saini, K. K., Chaturvedi, P., Sinha, A., Singh, M. P., Khan, M. A., Verma, A., Nengroo, M. A., Satrusal, S. R., Meena, S., Singh, A., et al. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102833 · Cited by 84
Bruedigam, C., Porter, A. H., Song, A., de Wei, G. V. I., Stoll, T. M., Straube, J., Cooper, L. T., Cheng, G., Kahl, V. F. S., Sobinoff, A. P., et al. (2023) · Nature Cancer · doi:10.1038/s43018-023-00653-5 · Cited by 86
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Cabello, C. M., Lamore, S. D., Bair, W. B., Qiao, S., Azimian, S., Lesson, J. L., & Wondrak, G. T. (2011) · Investigational New Drugs · doi:10.1007/s10637-011-9676-7 · Cited by 81
Zuo, T., Fang, T., Zhang, J., Yang, J., Xu, R., Wang, Z., Deng, H., & Shen, Q. (2021) · Advanced Healthcare Materials · doi:10.1002/adhm.202100683 · Cited by 80
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Liu, Z., Lv, X., Song, E., & Song, Y. (2020) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2020.115241 · Cited by 77
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Yang, W. S., Shimada, K., Delva, D., Patel, M., Ode, E., Skouta, R., & Stockwell, B. R. (2011) · ACS Medicinal Chemistry Letters · doi:10.1021/ml200195s · Cited by 76
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Geng, H., Li, Z., Li, Z., Zhang, Y., Gao, Z., Sun, L., Li, X., Cui, J., Ni, S., & Hao, J. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2220300120 · Cited by 76
Ramkumar, K., Samanta, S., Kyani, A., Yang, S., Tamura, S., Ziemke, E. K., Stuckey, J. A., Li, S., Chinnaswamy, K., Otake, H., et al. (2016) · Nature Communications · doi:10.1038/ncomms13084 · Cited by 75
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Codenotti, S., Poli, M., Asperti, M., Zizioli, D., Marampon, F., & Fanzani, A. (2018) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-018-2699-0 · Cited by 76
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Yang, M., Lu, Z., Li, F., Shi, F., Zhan, F., Zhao, L., Li, Y., Li, J., Lin, L., & Qin, Z. (2020) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2020.09.036 · Cited by 72
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Saini, S., & Gurung, P. (2024) · Immunological Reviews · doi:10.1111/imr.13409 · Cited by 84
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Zeng, T., Deng, G., Zhong, W., Gao, Z., Ma, S., Mo, C., Li, Y., Huang, S., Zhou, C., Lai, Y., et al. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.01.009 · Cited by 71
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Hu, Y., Guo, N., Yang, T., Yan, J., Wang, W., & Li, X. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/1458143 · Cited by 73
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Gu, R., Xia, Y., Li, P., Zou, D., Lu, K., Ren, L., Zhang, H., & Sun, Z. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.860344 · Cited by 75
Chen, Y., Xu, W., Liu, Y., Zhang, J., Yang, Y., Wang, Z.-W., Sun, D., Li, H., Liu, B., & Chen, L.-X. (2023) · International Journal of Biological Sciences · doi:10.7150/ijbs.82120 · Cited by 72
Wei, Y., Lv, H., Shaikh, A. B., Han, W., Hou, H., Zhang, Z., Wang, S., & Shang, P. (2020) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2020.129539 · Cited by 72
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Eaton, J. K., Furst, L., Cai, L. L., Viswanathan, V. S., & Schreiber, S. L. (2020) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2020.127538 · Cited by 72
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Kolbrink, B., von Samson‐Himmelstjerna, F. A., Messtorff, M. L., Riebeling, T., Nische, R., Schmitz, J., Bräsen, J. H., Kunzendorf, U., & Krautwald, S. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04416-w · Cited by 70
Namgaladze, D., Fuhrmann, D. C., & Brüne, B. (2022) · Cell Death Discovery · doi:10.1038/s41420-022-01117-y · Cited by 70
Kim, J. W., Kim, M.-J., Han, T.-H., Lee, J.-Y., Kim, S., Kim, H., Oh, K., Kim, W. K., Han, B., Bae, K., et al. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-06070-x · Cited by 76
Li, S., Lei, Z., Yang, X., Zhao, M. L., Hou, Y., Wang, D., Tang, S., Li, J., & Yu, J. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.841410 · Cited by 72
Metadata
- Authors
- Yang, W. S., & Stockwell, B. R.
- Affiliations
- Columbia University (US)
- Corresponding author
- Stockwell, Brent R.
- Venue
- Chemistry & Biology
- Publisher
- Elsevier BV
- Published
- 2008-03
- Volume
- 15
- Issue
- 3
- Pages
- 234-245
- ISSN
- 1074-5521 (ISSN-L)
- PMC
- PMC2683762
- OpenAlex
- W2114138419
- Cited by
- 1,876
- References
- 35
- Citations by year
- 2026: 138 · 2025: 231 · 2024: 319 · 2023: 312 · 2022: 271 · 2021: 202 · 2020: 135 · 2019: 66 · 2018: 58 · 2017: 38 · 2016: 35 · 2015: 19 · 2014: 11 · 2013: 7 · 2012: 10
- FWCI
- 3.16
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Chemistry & Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (R01CA097061)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Ferroptosis and cancer prognosis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- synthetic lethality, oncogenic Ras, RSL3, erastin, non-apoptotic cell death, iron-dependent cell death, oxidative cell death, VDAC3, voltage-dependent anion channel, transferrin receptor 1, ferritin, iron metabolism, small molecule screening, cancer cell death
- MeSH terms
- Drug Evaluation, Preclinical, Humans, Iron, Mutation, Neoplasms, Piperazines, Substrate Specificity, Gene Expression Regulation, Neoplastic, Proto-Oncogene Proteins p21(ras), Cell Death, Apoptosis, Cell Line, Tumor, Voltage-Dependent Anion Channels, Small Molecule Libraries
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