The CoQ oxidoreductase FSP1 acts parallel to GPX4 to inhibit ferroptosis.

Animals Apoptosis Regulatory Proteins / genetics Cell Line, Tumor Cell Membrane / metabolism Ferroptosis / genetics Gene Expression Regulation, Enzymologic Heterografts Humans Lipid Peroxides / metabolism Male Mice Mice, SCID Mitochondrial Proteins / genetics Phospholipid Hydroperoxide Glutathione Peroxidase / metabolism Ubiquinone / analogs & derivatives

Journal

Nature
ISSN: 1476-4687
Titre abrégé: Nature
Pays: England
ID NLM: 0410462

Informations de publication

Date de publication:
11 2019
Historique:
received: 25 02 2019
accepted: 01 10 2019
pubmed: 22 10 2019
medline: 14 4 2020
entrez: 22 10 2019
Statut: ppublish

Résumé

Ferroptosis is a form of regulated cell death that is caused by the iron-dependent peroxidation of lipids

Identifiants

DOI: 10.1038/s41586-019-1705-2 PMID: 31634900 PMC: PMC6883167
pubmed: 31634900
doi: 10.1038/s41586-019-1705-2
pii: 10.1038/s41586-019-1705-2
pmc: PMC6883167
mid: NIHMS1540825
doi:

Substances chimiques

ferroptosis suppressor protein 1, human 0
Apoptosis Regulatory Proteins 0
Lipid Peroxides 0
Mitochondrial Proteins 0
Ubiquinone 1339-63-5
Phospholipid Hydroperoxide Glutathione Peroxidase EC 1.11.1.12
coenzyme Q10 EJ27X76M46

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

688-692

Subventions

Organisme : NIGMS NIH HHS
ID : R01 GM122923
Pays : United States
Organisme : NIEHS NIH HHS
ID : P42 ES004705
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM112948
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM127763
Pays : United States
Organisme : NCI NIH HHS
ID : DP2 CA195761
Pays : United States

Commentaires et corrections

Type : CommentIn
Type : CommentIn
Type : CommentIn

Références

Dixon, S. J. et al. Ferroptosis: an iron-dependent form of nonapoptotic cell death. Cell 149, 1060–1072 (2012).
doi: 10.1016/j.cell.2012.03.042
Stockwell, B. R. et al. Ferroptosis: a regulated cell death nexus linking metabolism, redox biology, and disease. Cell 171, 273–285 (2017).
doi: 10.1016/j.cell.2017.09.021
Yang, W. S. et al. Regulation of ferroptotic cancer cell death by GPX4. Cell 156, 317–331 (2014).
doi: 10.1016/j.cell.2013.12.010
Ingold, I. et al. Selenium utilization by GPX4 is required to prevent hydroperoxide-induced ferroptosis. Cell 172, 409–422.e21 (2018).
doi: 10.1016/j.cell.2017.11.048
Dixon, S. J. & Stockwell, B. R. The hallmarks of ferroptosis. Annu. Rev. Cancer Biol. 3, 35–54 (2019).
doi: 10.1146/annurev-cancerbio-030518-055844
Zou, Y. et al. A GPX4-dependent cancer cell state underlies the clear-cell morphology and confers sensitivity to ferroptosis. Nat. Commun. 10, 1617 (2019).
doi: 10.1038/s41467-019-09277-9
Wu, M., Xu, L.-G., Li, X., Zhai, Z. & Shu, H.-B. AMID, an apoptosis-inducing factor-homologous mitochondrion-associated protein, induces caspase-independent apoptosis. J. Biol. Chem. 277, 25617–25623 (2002).
doi: 10.1074/jbc.M202285200
Ohiro, Y. et al. A novel p53-inducible apoptogenic gene, PRG3, encodes a homologue of the apoptosis-inducing factor (AIF). FEBS Lett. 524, 163–171 (2002).
doi: 10.1016/S0014-5793(02)03049-1
Dixon, S. J. et al. Pharmacological inhibition of cysteine–glutamate exchange induces endoplasmic reticulum stress and ferroptosis. eLife 3, e02523 (2014).
doi: 10.7554/eLife.02523
Bersuker, K. et al. A Proximity labeling strategy provides insights into the composition and dynamics of lipid droplet proteomes. Dev. Cell 44, 97–112.e7 (2018).
doi: 10.1016/j.devcel.2017.11.020
Magtanong, L. et al. Exogenous monounsaturated fatty acids promote a ferroptosis-resistant cell state. Cell Chem. Biol. 26, 420–432.e9 (2019).
doi: 10.1016/j.chembiol.2018.11.016
Yang, W. S. et al. Peroxidation of polyunsaturated fatty acids by lipoxygenases drives ferroptosis. Proc. Natl Acad. Sci. USA 113, E4966–E4975 (2016).
doi: 10.1073/pnas.1603244113
Marshall, K. R. et al. The human apoptosis-inducing protein AMID is an oxidoreductase with a modified flavin cofactor and DNA binding activity. J. Biol. Chem. 280, 30735–30740 (2005).
doi: 10.1074/jbc.M414018200
Shimada, K. et al. Global survey of cell death mechanisms reveals metabolic regulation of ferroptosis. Nat. Chem. Biol. 12, 497–503 (2016).
doi: 10.1038/nchembio.2079
Arroyo, A., Navarro, F., Navas, P. & Villalba, J. M. Ubiquinol regeneration by plasma membrane ubiquinone reductase. Protoplasma 205, 107–113 (1998).
doi: 10.1007/BF01279300
Takahashi, T., Okamoto, T., Mori, K., Sayo, H. & Kishi, T. Distribution of ubiquinone and ubiquinol homologues in rat tissues and subcellular fractions. Lipids 28, 803–809 (1993).
doi: 10.1007/BF02536234
Sun, X. et al. Activation of the p62-Keap1-NRF2 pathway protects against ferroptosis in hepatocellular carcinoma cells. Hepatology 63, 173–184 (2016).
doi: 10.1002/hep.28251
Rees, M. G. et al. Correlating chemical sensitivity and basal gene expression reveals mechanism of action. Nat. Chem. Biol. 12, 109–116 (2016).
doi: 10.1038/nchembio.1986
Hangauer, M. J. et al. Drug-tolerant persister cancer cells are vulnerable to GPX4 inhibition. Nature 551, 247–250 (2017).
doi: 10.1038/nature24297
Viswanathan, V. S. et al. Dependency of a therapy-resistant state of cancer cells on a lipid peroxidase pathway. Nature 547, 453–457 (2017).
doi: 10.1038/nature23007
Zhang, Y. et al. Imidazole ketone erastin induces ferroptosis and slows tumor growth in a mouse lymphoma model. Cell Chem. Biol. 26, 623–633.e9 (2019).
doi: 10.1016/j.chembiol.2019.01.008
Hayano, M., Yang, W. S., Corn, C. K., Pagano, N. C. & Stockwell, B. R. Loss of cysteinyl-tRNA synthetase (CARS) induces the transsulfuration pathway and inhibits ferroptosis induced by cystine deprivation. Cell Death Differ. 23, 270–278 (2016).
doi: 10.1038/cdd.2015.93
Doll, S. et al. FSP1 is a glutathione-independent ferroptosis suppressor. Nature https://doi.org/10.1038/s41586-019-1707-0 (2019).
doi: 10.1038/nmeth763
Nguyen, T. B. et al. DGAT1-dependent lipid droplet biogenesis protects mitochondrial function during starvation-induced autophagy. Dev. Cell 42, 9–21.e5 (2017).
doi: 10.1016/j.devcel.2017.06.003
Tribble, D. L. et al. Oxidative susceptibility of low density lipoprotein subfractions is related to their ubiquinol-10 and α-tocopherol content. Proc. Natl Acad. Sci. USA 91, 1183–1187 (1994).
doi: 10.1073/pnas.91.3.1183
Stocker, R., Bowry, V. W. & Frei, B. Ubiquinol-10 protects human low density lipoprotein more efficiently against lipid peroxidation than does α-tocopherol. Proc. Natl Acad. Sci. USA 88, 1646–1650 (1991).
doi: 10.1073/pnas.88.5.1646
Inoue, T., Heo, W. D., Grimley, J. S., Wandless, T. J. & Meyer, T. An inducible translocation strategy to rapidly activate and inhibit small GTPase signaling pathways. Nat. Methods 2, 415–418 (2005).
doi: 10.1038/nmeth763
Macdonald, J. L. & Pike, L. J. A simplified method for the preparation of detergent-free lipid rafts. J. Lipid Res. 46, 1061–1067 (2005).
doi: 10.1194/jlr.D400041-JLR200
Morgens, D. W. et al. Genome-scale measurement of off-target activity using Cas9 toxicity in high-throughput screens. Nat. Commun. 8, 15178 (2017).
doi: 10.1038/ncomms15178
Tang, P. H., Miles, M. V., DeGrauw, A., Hershey, A. & Pesce, A. HPLC analysis of reduced and oxidized coenzyme Q
pubmed: 11159774

Auteurs

Kirill Bersuker (K)

Department of Nutritional Sciences and Toxicology, University of California, Berkeley, Berkeley, CA, USA.

Joseph M Hendricks (JM)

Department of Nutritional Sciences and Toxicology, University of California, Berkeley, Berkeley, CA, USA.

Zhipeng Li (Z)

Department of Nutritional Sciences and Toxicology, University of California, Berkeley, Berkeley, CA, USA.

Leslie Magtanong (L)

Department of Biology, Stanford University, Stanford, CA, USA.

Breanna Ford (B)

Department of Nutritional Sciences and Toxicology, University of California, Berkeley, Berkeley, CA, USA.
Department of Chemistry, University of California, Berkeley, Berkeley, CA, USA.
Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA, USA.

Peter H Tang (PH)

Department of Pathology and Laboratory Medicine, Cincinnati Children's Hospital Medical Center and University of Cincinnati College of Medicine, Cincinnati, OH, USA.

Melissa A Roberts (MA)

Department of Nutritional Sciences and Toxicology, University of California, Berkeley, Berkeley, CA, USA.

Bingqi Tong (B)

Department of Chemistry, University of California, Berkeley, Berkeley, CA, USA.

Thomas J Maimone (TJ)

Department of Chemistry, University of California, Berkeley, Berkeley, CA, USA.

Roberto Zoncu (R)

Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA, USA.

Michael C Bassik (MC)

Department of Genetics and Stanford University Chemistry, Engineering and Medicine for Human Health (ChEM-H), Stanford University School of Medicine, Stanford, CA, USA.

Daniel K Nomura (DK)

Department of Nutritional Sciences and Toxicology, University of California, Berkeley, Berkeley, CA, USA.
Department of Chemistry, University of California, Berkeley, Berkeley, CA, USA.
Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA, USA.

Scott J Dixon (SJ)

Department of Biology, Stanford University, Stanford, CA, USA.

James A Olzmann (JA)

Department of Nutritional Sciences and Toxicology, University of California, Berkeley, Berkeley, CA, USA. olzmann@berkeley.edu.
Chan Zuckerberg Biohub, San Francisco, CA, USA. olzmann@berkeley.edu.

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Classifications MeSH

questionsmedicales.fr › Eucaryotes › Animaux › The CoQ oxidoreductase FSP1 acts parallel to...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protéines régulatrices de l'apoptose › The CoQ oxidoreductase FSP1 acts parallel to...
questionsmedicales.fr › Cellules › Cellules cultivées › Cellules cancéreuses en culture › Lignée cellulaire tumorale › The CoQ oxidoreductase FSP1 acts parallel to...
questionsmedicales.fr › Cellules › Structures cellulaires › Membrane cellulaire › The CoQ oxidoreductase FSP1 acts parallel to...
questionsmedicales.fr › Phénomènes physiologiques cellulaires › Mort cellulaire › Mort cellulaire régulée › Ferroptose › The CoQ oxidoreductase FSP1 acts parallel to...
questionsmedicales.fr › Phénomènes génétiques › Régulation de l'expression des gènes › Régulation de l'expression des gènes codant pour des enzymes › The CoQ oxidoreductase FSP1 acts parallel to...
questionsmedicales.fr › Régions du corps › Transplants › Hétérogreffes › The CoQ oxidoreductase FSP1 acts parallel to...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › The CoQ oxidoreductase FSP1 acts parallel to...
questionsmedicales.fr › Lipides › Peroxydes lipidiques › The CoQ oxidoreductase FSP1 acts parallel to...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Rodentia › Muridae › Murinae › Souris › The CoQ oxidoreductase FSP1 acts parallel to...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Rodentia › Muridae › Murinae › Souris › Souches mutantes de souris › Souris SCID › The CoQ oxidoreductase FSP1 acts parallel to...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines mitochondriales › The CoQ oxidoreductase FSP1 acts parallel to...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Sélénoprotéines › Glutathione peroxidase › Phospholipid hydroperoxide glutathione peroxidase › The CoQ oxidoreductase FSP1 acts parallel to...
questionsmedicales.fr › Enzymes et coenzymes › Coenzymes › Ubiquinones › The CoQ oxidoreductase FSP1 acts parallel to...