Encyclopedia of Signaling Molecules

Living Edition
| Editors: Sangdun Choi

Apoptosis-Inducing Factor 1, Mitochondrial

  • Patricia Ferreira
  • Raquel Villanueva
  • Marta Martínez-Júlvez
  • Milagros Medina
Living reference work entry
DOI: https://doi.org/10.1007/978-1-4614-6438-9_101522-1

Abstract

Apoptosis-inducing factor (AIF); Programmed cell death protein 8 (PDCD8)

Keywords

Flavin Adenine Dinucleotide Charge Transfer Complex Respiratory Chain Complex Flavin Adenine Dinucleotide Mitochondrial Intermembrane Space 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Notes

Acknowledgments

We thank Luis Martinez Lostao (University of Zaragoza) for helping us with the graphical illustration in Figure 1.

References

  1. Ardissone A, Piscosquito G, Legati A, Langella T, Lamantea E, Garavaglia B, et al. A slowly progressive mitochondrial encephalomyopathy widens the spectrum of AIFM1 disorders. Neurology. 2015;84:2193–5. doi:10.1212/WNL.0000000000001613.CrossRefPubMedPubMedCentralGoogle Scholar
  2. Artus C, Boujrad H, Bouharrour A, Brunelle MN, Hoos S, Yuste VJ, et al. AIF promotes chromatinolysis and caspase-independent programmed necrosis by interacting with histone H2AX. EMBO J. 2010;29:1585–99. doi:10.1038/emboj.2010.43.CrossRefPubMedPubMedCentralGoogle Scholar
  3. Cande C, Vahsen N, Kouranti I, Schmitt E, Daugas E, Spahr C, et al. AIF and cyclophilin A cooperate in apoptosis-associated chromatinolysis. Oncogene. 2004;23:1514–21. doi:10.1038/sj.onc.1207279.CrossRefPubMedGoogle Scholar
  4. Ferreira P, Villanueva R, Martínez-Júlvez M, Herguedas B, Marcuello C, Fernandez-Silva P, et al. Structural insights into the coenzyme mediated monomer-dimer transition of the pro-apoptotic apoptosis inducing factor. Biochemistry. 2014;53:4204–15. doi:10.1021/bi500343r.CrossRefPubMedGoogle Scholar
  5. Ghezzi D, Sevrioukova I, Invernizzi F, Lamperti C, Mora M, D’Adamo P, et al. Severe X-linked mitochondrial encephalomyopathy associated with a mutation in apoptosis-inducing factor. Am J Hum Genet. 2010;86:639–49. doi:10.1016/j.ajhg.2010.03.002.CrossRefPubMedPubMedCentralGoogle Scholar
  6. Hangen E, Féraud O, Lachkar S, Mou H, Doti N, Fimia GM, et al. Interaction between AIF and CHCHD4 regulates respiratory chain biogenesis. Mol Cell. 2015;58:1001–14. doi:10.1016/j.molcel.2015.04.020.CrossRefPubMedGoogle Scholar
  7. Kettwig M, Schubach M, Zimmermann FA, Klinge L, Mayr JA, Biskup S, et al. From ventriculomegaly to severe muscular atrophy: expansion of the clinical spectrum related to mutations in AIFM1. Mitochondrion. 2015;21C:12–8. doi:10.1016/j.mito.2015.01.001.CrossRefGoogle Scholar
  8. Lui JC, Kong SK. Heat shock protein 70 inhibits the nuclear import of apoptosis-inducing factor to avoid DNA fragmentation in TF-1 cells during erythropoiesis. FEBS Lett. 2007;581:109–17. doi:10.1016/j.febslet.2006.11.082.CrossRefPubMedGoogle Scholar
  9. Mate MJ, Ortiz-Lombardia M, Boitel B, Haouz A, Tello D, Susin SA, et al. The crystal structure of the mouse apoptosis-inducing factor AIF. Nat Struct Biol. 2002;9:442–6. doi:10.1038/nsb793.CrossRefPubMedGoogle Scholar
  10. Miramar MD, Costantini P, Ravagnan L, Saraiva LM, Haouzi D, Brothers G, et al. NADH oxidase activity of mitochondrial apoptosis-inducing factor. J Biol Chem. 2001;276:16391–8. doi:10.1074/jbc.M010498200.CrossRefPubMedGoogle Scholar
  11. Modjtahedi N, Giordanetto F, Madeo F, Kroemer G. Apoptosis-inducing factor: vital and lethal. Trends Cell Biol. 2006;16:264–72. doi:10.1016/j.tcb.2006.03.008.CrossRefPubMedGoogle Scholar
  12. Otera H, Ohsakaya S, Nagaura Z, Ishihara N, Mihara K. Export of mitochondrial AIF in response to proapoptotic stimuli depends on processing at the intermembrane space. EMBO J. 2005;24:1375–86. doi:10.1038/sj.emboj.7600614.CrossRefPubMedPubMedCentralGoogle Scholar
  13. Rinaldi C, Grunseich C, Sevrioukova IF, Schindler A, Horkayne-Szakaly I, Lamperti C, et al. Cowchock syndrome is associated with a mutation in apoptosis-inducing factor. Am J Hum Genet. 2012;91:1095–102. doi:10.1016/j.ajhg.2012.10.008.CrossRefPubMedPubMedCentralGoogle Scholar
  14. Sevrioukova IF. Apoptosis-inducing factor: structure, function, and redox regulation. Antioxid Redox Signal. 2011;14:2545–79. doi:10.1089/ars.2010.3445.CrossRefPubMedPubMedCentralGoogle Scholar
  15. Shelar SB, Kaminska KK, Reddy SA, Kumar D, Tan CT, Yu VC, et al. Thioredoxin-dependent regulation of AIF-mediated DNA damage. Free Radic Biol Med. 2015;87:FRBMD1500111. doi:10.1016/j.freeradbiomed.2015.06.029.CrossRefGoogle Scholar
  16. Sorrentino L, Calogero AM, Pandini V, Vanoni MA, Sevrioukova IF, Aliverti A. Key role of the adenylate moiety and integrity of the adenylate-binding site for the NAD(+)/H binding to mitochondrial apoptosis-inducing factor. Biochemistry. 2015;54:6996–7009. doi:10.1021/acs.biochem.5b00898.CrossRefPubMedGoogle Scholar
  17. Susin SA, Lorenzo HK, Zamzami N, Marzo I, Snow BE, Brothers GM, et al. Molecular characterization of mitochondrial apoptosis-inducing factor. Nature. 1999;397:441–6. doi:10.1038/17135.CrossRefPubMedGoogle Scholar
  18. Villanueva R, Ferreira P, Marcuello C, Usón A, Miramar MD, Peleato ML, et al. Key residues regulating the reductase activity of the human mitochondrial apoptosis inducing factor. Biochemistry. 2015;54:5175–84. doi:10.1021/acs.biochem.5b00696.CrossRefPubMedGoogle Scholar
  19. Ye H, Cande C, Stephanou NC, Jiang S, Gurbuxani S, Larochette N, et al. DNA binding is required for the apoptogenic action of apoptosis inducing factor. Nat Struct Biol. 2002;9:680–4. doi:10.1038/nsb836.CrossRefPubMedGoogle Scholar

Copyright information

© Springer Science+Business Media LLC 2016

Authors and Affiliations

  • Patricia Ferreira
    • 1
  • Raquel Villanueva
    • 1
  • Marta Martínez-Júlvez
    • 1
  • Milagros Medina
    • 1
  1. 1.Department of Biochemistry and Molecular and Cellular BiologyInstitute for Biocomputation and Physics of Complex Systems, University of ZaragozaZaragozaSpain