Association of poly(rC)-binding protein-2 with sideroflexin-3 through TOM20 as an iron entry pathway to mitochondria

References

• Toyokuni S, Kong Y, Zheng H, et al. Iron as spirit of life to share under monopoly. J Clin Biochem Nutr. 2022;71(2):78–88. doi: 10.3164/jcbn.22-43.
   PubMed Web of Science ®Google Scholar
• Toyokuni S, Zheng H, Kong Y, et al. Low-temperature plasma as magic wand to differentiate between the good and the evil. Free Radic Res. 2023;57(1):38–46. doi: 10.1080/10715762.2023.2190860.
   PubMed Web of Science ®Google Scholar
• Toyokuni S, Yanatori I, Kong Y, et al. Ferroptosis at the crossroads of infection, aging and cancer. Cancer Sci. 2020;111(8):2665–2671. doi: 10.1111/cas.14496.
   PubMed Web of Science ®Google Scholar
• Hsieh WP, Deschamps F, Okuchi T, et al. Effects of iron on the lattice thermal conductivity of earth’s deep mantle and implications for mantle dynamics. Proc Natl Acad Sci U S A. 2018;115(16):4099–4104. doi: 10.1073/pnas.1718557115.
   PubMed Web of Science ®Google Scholar
• Koppenol WH, Hider RH. Iron and redox cycling. Do’s and don’ts. Free Radic Biol Med. 2019;133:3–10. doi: 10.1016/j.freeradbiomed.2018.09.022.
   PubMed Web of Science ®Google Scholar
• Yanatori I, Kishi F. DMT1 and iron transport. Free Radic Biol Med. 2019;133:55–63. doi: 10.1016/j.freeradbiomed.2018.07.020.
   PubMed Web of Science ®Google Scholar
• Donegan RK, Moore CM, Hanna DA, et al. Handling heme: the mechanisms underlying the movement of heme within and between cells. Free Radic Biol Med. 2018;133:88–100. doi: 10.1016/j.freeradbiomed.2018.08.005.
   PubMed Web of Science ®Google Scholar
• Toyokuni S, Kong Y, Cheng Z, et al. Carcinogenesis as side effects of iron and oxygen utilization: from the unveiled truth toward ultimate bioengineering. Cancers (Basel). 2020;12(11):3320. doi: 10.3390/cancers12113320.
   PubMed Web of Science ®Google Scholar
• Koleini N, Shapiro JS, Geier J, et al. Ironing out mechanisms of iron homeostasis and disorders of iron deficiency. J Clin Invest. 2021;131(11):e148671. doi: 10.1172/JCI148671.
   PubMed Web of Science ®Google Scholar
• Ali MY, Oliva CR, Flor S, et al. Mitoferrin, cellular and mitochondrial iron homeostasis. Cells. 2022;11(21):3464. doi: 10.3390/cells11213464.
   PubMed Web of Science ®Google Scholar
• Seguin A, Jia X, Earl AM, et al. The mitochondrial metal transporters mitoferrin1 and mitoferrin2 are required for liver regeneration and cell proliferation in mice. J Biol Chem. 2020;295(32):11002–11020. doi: 10.1074/jbc.RA120.013229.
   PubMed Web of Science ®Google Scholar
• Yanatori I, Richardson DR, Toyokuni S, et al. The new role of poly (rC)-binding proteins as iron transport chaperones: proteins that could couple with inter-organelle interactions to safely traffic iron. Biochim Biophys Acta Gen Subj. 2020;1864(11):129685. doi: 10.1016/j.bbagen.2020.129685.
   PubMed Web of Science ®Google Scholar
• Yanatori I, Yasui Y, Tabuchi M, et al. Chaperone protein involved in transmembrane transport of iron. Biochem J. 2014;462(1):25–37. doi: 10.1042/BJ20140225.
   PubMedGoogle Scholar
• Yanatori I, Richardson DR, Toyokuni S, et al. The iron chaperone poly(rC)-binding protein 2 forms a metabolon with the heme oxygenase 1/cytochrome P450 reductase complex for heme catabolism and iron transfer. J Biol Chem. 2017;292(32):13205–13229. doi: 10.1074/jbc.M117.776021.
   PubMed Web of Science ®Google Scholar
• Yanatori I, Richardson DR, Imada K, et al. Iron export through the transporter ferroportin 1 is modulated by the iron chaperone PCBP2. J Biol Chem. 2016;291(33):17303–17318. doi: 10.1074/jbc.M116.721936.
   PubMed Web of Science ®Google Scholar
• Clayton DA, Shadel GS. Isolation of mitochondria from tissue culture cells. Cold Spring Harb Protoc. 2014;2014(10):pdb prot080002. doi: 10.1101/pdb.prot080002.
   PubMedGoogle Scholar
• Hirayama T. Fluorescent probes for the detection of catalytic Fe(II) ion. Free Radic Biol Med. 2019;133:38–45. doi: 10.1016/j.freeradbiomed.2018.07.004.
   PubMed Web of Science ®Google Scholar
• Kawai K, Hirayama T, Imai H, et al. Molecular imaging of labile heme in living cells using a small molecule fluorescent probe. J Am Chem Soc. 2022;144(9):3793–3803. doi: 10.1021/jacs.1c08485.
   PubMed Web of Science ®Google Scholar
• Stockwell BR, Friedmann Angeli JP, Bayir H, et al. Ferroptosis: a regulated cell death nexus linking metabolism, redox biology, and disease. Cell. 2017;171(2):273–285. doi: 10.1016/j.cell.2017.09.021.
   PubMed Web of Science ®Google Scholar
• Liao PC, Bergamini C, Fato R, et al. Isolation of mitochondria from cells and tissues. Methods Cell Biol. 2020;155:3–31. doi: 10.1016/bs.mcb.2019.10.002.
   PubMed Web of Science ®Google Scholar
• Fleming MD, Campagna DR, Haslett JN, et al. A mutation in a mitochondrial transmembrane protein is responsible for the pleiotropic hematological and skeletal phenotype of flexed-tail (f/f) mice. Genes Dev. 2001;15(6):652–657. doi: 10.1101/gad.873001.
   PubMed Web of Science ®Google Scholar
• Miotto G, Tessaro S, Rotta GA, et al. In silico analyses of Fsf1 sequences, a new group of fungal proteins orthologous to the metazoan sideroblastic anemia-related sideroflexin family. Fungal Genet Biol. 2007;44(8):740–753. doi: 10.1016/j.fgb.2006.12.004.
   PubMed Web of Science ®Google Scholar
• Kory N, Wyant GA, Prakash G, et al. SFXN1 is a mitochondrial serine transporter required for one-carbon metabolism. Science. 2018;362(6416):eaat9528. doi: 10.1126/science.aat9528.
   PubMed Web of Science ®Google Scholar
• Paul BT, Tesfay L, Winkler CR, et al. Sideroflexin 4 affects Fe-S cluster biogenesis, iron metabolism, mitochondrial respiration and heme biosynthetic enzymes. Sci Rep. 2019;9(1):19634. doi: 10.1038/s41598-019-55907-z.
   PubMedGoogle Scholar
• Vile GF, Basu-Modak S, Waltner C, et al. Heme oxygenase 1 mediates an adaptive response to oxidative stress in human skin fibroblasts. Proc Natl Acad Sci U S A. 1994;91(7):2607–2610. doi: 10.1073/pnas.91.7.2607.
   PubMed Web of Science ®Google Scholar
• Gan B. Mitochondrial regulation of ferroptosis. J Cell Biol. 2021;220(9):e202105043. doi: 10.1083/jcb.202105043.
   PubMed Web of Science ®Google Scholar
• Soula M, Weber RA, Zilka O, et al. Metabolic determinants of cancer cell sensitivity to canonical ferroptosis inducers. Nat Chem Biol. 2020;16(12):1351–1360. doi: 10.1038/s41589-020-0613-y.
   PubMed Web of Science ®Google Scholar
• Busch JD, Fielden LF, Pfanner N, et al. Mitochondrial protein transport: versatility of translocases and mechanisms. Mol Cell. 2023;83(6):890–910. doi: 10.1016/j.molcel.2023.02.020.
   PubMed Web of Science ®Google Scholar
• Akhmedov D, Braun M, Mataki C, et al. Mitochondrial matrix pH controls oxidative phosphorylation and metabolism-secretion coupling in INS-1E clonal beta cells. Faseb J. 2010;24(11):4613–4626. doi: 10.1096/fj.10-162222.
   PubMed Web of Science ®Google Scholar
• Porcelli AM, Ghelli A, Zanna C, et al. pH difference across the outer mitochondrial membrane measured with a green fluorescent protein mutant. Biochem Biophys Res Commun. 2005;326(4):799–804. doi: 10.1016/j.bbrc.2004.11.105.
   PubMed Web of Science ®Google Scholar
• Moroishi T, Nishiyama M, Takeda Y, et al. The FBXL5-IRP2 axis is integral to control of iron metabolism in vivo. Cell Metab. 2011;14(3):339–351. doi: 10.1016/j.cmet.2011.07.011.
   PubMed Web of Science ®Google Scholar
• Amorim IS, Graham LC, Carter RN, et al. Sideroflexin 3 is an alpha-synuclein-dependent mitochondrial protein that regulates synaptic morphology. J Cell Sci. 2017;130(2):325–331.
   PubMed Web of Science ®Google Scholar
• van der Weyden L, Karp NA, Swiatkowska A, et al. Genome wide in vivo mouse screen data from studies to assess host regulation of metastatic colonisation. Sci Data. 2017;4(1):170129. doi: 10.1038/sdata.2017.129.
   PubMedGoogle Scholar
• van der Weyden L, Swiatkowska A, Iyer V, et al. A genome-wide screen in mice to identify cell-extrinsic regulators of pulmonary metastatic colonisation. G3 (Bethesda). 2020;10(6):1869–1877. doi: 10.1534/g3.120.401128.
   PubMedGoogle Scholar
• Ingham NJ, Pearson SA, Vancollie VE, et al. Mouse screen reveals multiple new genes underlying mouse and human hearing loss. PLoS Biol. 2019;17(4):e3000194. doi: 10.1371/journal.pbio.3000194.
   PubMed Web of Science ®Google Scholar
• Collins SC, Mikhaleva A, Vrcelj K, et al. Large-scale neuroanatomical study uncovers 198 gene associations in mouse brain morphogenesis. Nat Commun. 2019;10(1):3465. doi: 10.1038/s41467-019-11431-2.
   PubMedGoogle Scholar
• Ledahawsky LM, Terzenidou ME, Edwards R, et al. The mitochondrial protein sideroflexin 3 (SFXN3) influences neurodegeneration pathways in vivo. Febs J. 2022;289(13):3894–3914. doi: 10.1111/febs.16377.
   PubMed Web of Science ®Google Scholar
• Toyokuni S, Kong Y, Zheng H, et al. Three-dimensional regulation of ferroptosis at the intersection of iron, sulfur, and oxygen executing scrap and build toward evolution. Antioxid Redox Signal. 2023;39(10–12):807–815. doi: 10.1089/ars.2022.0142.
   PubMed Web of Science ®Google Scholar
• Kong Y, Akatsuka S, Motooka Y, et al. BRCA1 haploinsufficiency promotes chromosomal amplification under fenton reaction-based carcinogenesis through ferroptosis-resistance. Redox Biol. 2022;54:102356. doi: 10.1016/j.redox.2022.102356.
   PubMed Web of Science ®Google Scholar
• Motooka Y, Toyokuni S. Ferroptosis as ultimate target of cancer therapy. Antioxid Redox Signal. 2023;39(1-3):206–223. doi: 10.1089/ars.2022.0048.
   PubMed Web of Science ®Google Scholar