Loss of ferritin in developing wing cells: Apoptosis and ferroptosis coincide
Autoři:
Anna Karen Hernández-Gallardo aff001; Fanis Missirlis aff001
Působiště autorů:
Departamento de Fisiología, Biofísica y Neurociencias, Cinvestav, CDMX, México
aff001
Vyšlo v časopise:
Loss of ferritin in developing wing cells: Apoptosis and ferroptosis coincide. PLoS Genet 16(1): e32767. doi:10.1371/journal.pgen.1008503
Kategorie:
Perspective
prolekare.web.journal.doi_sk:
https://doi.org/10.1371/journal.pgen.1008503
Zdroje
1. Mumbauer S, Pascual J, Kolotuev I, Hamaratoglu F. Ferritin heavy chain protects the developing wing from reactive oxygen species and ferroptosis. PLoS Genet. 2019; 15: e1008396. doi: 10.1371/journal.pgen.1008396 31568497
2. Dixon SJ, Lemberg KM, Lamprecht MR, Skouta R, Zaitsev EM, Gleason CE, et al. Ferroptosis: an iron-dependent form of nonapoptotic cell death. Cell. 2012; 149: 1060–1072. doi: 10.1016/j.cell.2012.03.042 22632970
3. Wu J, Minikes AM, Gao M, Bian H, Li Y, Stockwell BR, et al. Intercellular interaction dictates cancer cell ferroptosis via NF2-YAP signalling. Nature. 2019; 572: 402–406. doi: 10.1038/s41586-019-1426-6 31341276
4. Yang WH, Ding CC, Sun T, Rupprecht G, Lin CC, Hsu D, et al. The Hippo Pathway Effector TAZ Regulates Ferroptosis in Renal Cell Carcinoma. Cell Rep. 2019; 28: 2501–2508.e4. doi: 10.1016/j.celrep.2019.07.107 31484063
5. Marelja Z, Leimkühler S, Missirlis F. Iron Sulfur and Molybdenum Cofactor Enzymes Regulate the Drosophila Life Cycle by Controlling Cell Metabolism. Front Physiol. 2018; 9: 50. doi: 10.3389/fphys.2018.00050 29491838
6. Missirlis F, Kosmidis S, Brody T, Mavrakis M, Holmberg S, Odenwald WF, et al. Homeostatic mechanisms for iron storage revealed by genetic manipulations and live imaging of Drosophila ferritin. Genetics. 2007; 177: 89–100. doi: 10.1534/genetics.107.075150 17603097
7. Tang X, Zhou B. Ferritin is the key to dietary iron absorption and tissue iron detoxification in Drosophila melanogaster. FASEB J. 2013; 27: 288–298. doi: 10.1096/fj.12-213595 23064556
8. González-Morales N, Mendoza-Ortíz MÁ, Blowes LM, Missirlis F, Riesgo-Escovar JR. Ferritin Is Required in Multiple Tissues during Drosophila melanogaster Development. PLoS ONE. 2015; 10: e0133499. doi: 10.1371/journal.pone.0133499 26192321
9. Zheng Y, Pan D. The Hippo Signaling Pathway in Development and Disease. Dev Cell. 2019; 50: 264–282. doi: 10.1016/j.devcel.2019.06.003 31386861
10. Hamaratoglu F, Willecke M, Kango-Singh M, Nolo R, Hyun E, Tao C, et al. The tumour-suppressor genes NF2/Merlin and Expanded act through Hippo signalling to regulate cell proliferation and apoptosis. Nat Cell Biol. 2006; 8: 27–36. doi: 10.1038/ncb1339 16341207
11. Willecke M, Hamaratoglu F, Kango-Singh M, Udan R, Chen CL, Tao C, et al. The fat cadherin acts through the hippo tumor-suppressor pathway to regulate tissue size. Curr Biol. 2006; 16: 2090–2100. doi: 10.1016/j.cub.2006.09.005 16996265
12. Pascual J, Jacobs J, Sansores-Garcia L, Natarajan M, Zeitlinger J, Aerts S, et al. Hippo Reprograms the Transcriptional Response to Ras Signaling. Dev Cell. 2017; 42: 667–680.e4. doi: 10.1016/j.devcel.2017.08.013 28950103
13. Atkins M, Potier D, Romanelli L, Jacobs J, Mach J, Hamaratoglu F, et al. An Ectopic Network of Transcription Factors Regulated by Hippo Signaling Drives Growth and Invasion of a Malignant Tumor Model. Curr Biol. 2016; 26: 2101–2113. doi: 10.1016/j.cub.2016.06.035 27476594
14. Morata G, Ripoll P. Minutes: mutants of drosophila autonomously affecting cell division rate. Dev Biol. 1975; 42: 211–221. doi: 10.1016/0012-1606(75)90330-9 1116643
15. Menéndez J, Pérez-Garijo A, Calleja M, Morata G. A tumor-suppressing mechanism in Drosophila involving cell competition and the Hippo pathway. Proc Natl Acad Sci U S A. 2010; 107: 14651–14656. doi: 10.1073/pnas.1009376107 20679206
16. Hirschhorn T, Stockwell BR. The development of the concept of ferroptosis. Free Radic Biol Med. 2019; 133: 130–143. doi: 10.1016/j.freeradbiomed.2018.09.043 30268886
17. Wang YQ, Chang SY, Wu Q, Gou YJ, Jia L, Cui YM, et al. The Protective Role of Mitochondrial Ferritin on Erastin-Induced Ferroptosis. Front Aging Neurosci. 2016; 8: 308. doi: 10.3389/fnagi.2016.00308 28066232
18. Missirlis F, Holmberg S, Georgieva T, Dunkov BC, Rouault TA, Law JH. Characterization of mitochondrial ferritin in Drosophila. Proc Natl Acad Sci U S A. 2006; 103: 5893–5898. doi: 10.1073/pnas.0601471103 16571656
19. Chen PH, Wu J, Ding CC, Lin CC, Pan S, Bossa N, et al. Kinome screen of ferroptosis reveals a novel role of ATM in regulating iron metabolism. Cell Death Differ. 2019; doi: 10.1038/s41418-019-0393-7 31320750
20. Missirlis F, Rahlfs S, Dimopoulos N, Bauer H, Becker K, Hilliker A, et al. A putative glutathione peroxidase of Drosophila encodes a thioredoxin peroxidase that provides resistance against oxidative stress but fails to complement a lack of catalase activity. Biol Chem. 2003; 384: 463–72. doi: 10.1515/BC.2003.052 12715897
21. Owusu-Ansah E, Banerjee U. Reactive oxygen species prime Drosophila haematopoietic progenitors for differentiation. Nature. 2009; 461: 537–541. doi: 10.1038/nature08313 19727075
22. Yoon S, Cho B, Shin M, Koranteng F, Cha N, Shim J. Iron Homeostasis Controls Myeloid Blood Cell Differentiation in Drosophila. Mol Cells. 2017; 40: 976–985. doi: 10.14348/molcells.2017.0287 29237257
23. Bersuker K, Hendricks J, Li Z, Magtanong L, Ford B, Tang PH, et al. The CoQ oxidoreductase FSP1 acts parallel to GPX4 to inhibit ferroptosis. Nature. 2019; doi: 10.1038/s41586-019-1705-2 31634900
24. Doll S, Freitas FP, Shah R, Aldrovandi M, da Silva MC, Ingold I, et al. FSP1 is a glutathione-independent ferroptosis suppressor. Nature. 2019; doi: 10.1038/s41586-019-1707-0 31634899
25. Hamburger AE, West AP Jr, Hamburger ZA, Hamburger P, Bjorkman PJ. Crystal structure of a secreted insect ferritin reveals a symmetrical arrangement of heavy and light chains. J Mol Biol. 2005; 349: 558–569. doi: 10.1016/j.jmb.2005.03.074 15896348
26. Gutiérrez L, Zubow K, Nield J, Gambis A, Mollereau B, Lázaro FJ, et al. Biophysical and genetic analysis of iron partitioning and ferritin function in Drosophila melanogaster. Metallomics. 2013; 5: 997–1005. doi: 10.1039/c3mt00118k 23771129
27. Jiang XZ, Cong L, Niu JZ, Dou W, Wang JJ. Alternative splicing contributes to the coordinated regulation of ferritin subunit levels in Bactrocera dorsalis (Hendel). Sci Rep. 2014; 4: 4806. doi: 10.1038/srep04806 24763285
28. Walter-Nuno AB, Taracena ML, Mesquita RD, Oliveira PL, Paiva-Silva GO. Silencing of Iron and Heme-Related Genes Revealed a Paramount Role of Iron in the Physiology of the Hematophagous Vector Rhodnius prolixus. Front Genet. 2018; 9: 19. doi: 10.3389/fgene.2018.00019 29456553
29. Xiao G, Liu ZH, Zhao M, Wang HL, Zhou B. Transferrin 1 Functions in Iron Trafficking and Genetically Interacts with Ferritin in Drosophila melanogaster. Cell Rep. 2019; 26: 748–758.e5. doi: 10.1016/j.celrep.2018.12.053 30650364
30. Mandilaras K, Missirlis F. Genes for iron metabolism influence circadian rhythms in Drosophila melanogaster. Metallomics. 2012; 4: 928–936. doi: 10.1039/c2mt20065a 22885802
31. Rosas-Arellano A, Vásquez-Procopio J, Gambis A, Blowes LM, Steller H, Mollereau B, et al. Ferritin Assembly in Enterocytes of Drosophila melanogaster. Int J Mol Sci. 2016; 17: 27. doi: 10.3390/ijms17020027 26861293
32. Zhang P, Pei C, Wang X, Xiang J, Sun BF, Cheng Y, et al. A Balance of Yki/Sd Activator and E2F1/Sd Repressor Complexes Controls Cell Survival and Affects Organ Size. Dev Cell. 2017; 43: 603–617.e5. doi: 10.1016/j.devcel.2017.10.033 29207260
Štítky
Genetika Reprodukčná medicínaČlánok vyšiel v časopise
PLOS Genetics
2020 Číslo 1
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