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Abstrakty
Ferroportin (Fpn) is a membrane protein representing the major cellular iron exporter, essential for metal translocation from cells into plasma. Despite its pivotal role in human iron homeostasis, many questions on Fpn structure and biology remain unanswered. In this work, we present two novel and more reliable structural models of human Fpn (hFpn; inward-facing and outwardfacing conformations) obtained using as templates the recently solved crystal structures of a bacterial homologue of hFpn, Bdellovibrio bacteriovorus Fpn. In the absence of an experimentally solved structure of hFpn, the structural predictions described here allow to analyze the role of pathogenic mutations in the Fpn-linked hereditary hemochromatosis disease and represent a valuable alternative for reliable structure-based functional studies on this human iron exporter.
Słowa kluczowe
Czasopismo
Rocznik
Tom
Strony
215--222
Opis fizyczny
Bibliogr. 34 poz., rys.
Twórcy
autor
- Department of Sciences, Roma Tre University, 00146 Rome, Italy
- Department of Biochemical Sciences, Sapienza University of Roma, 00185 Rome, Italy
autor
- Department of Sciences, Roma Tre University, 00146 Rome, Italy
autor
- Department of Biosciences and Territory, University of Molise, 86090 Pesche, Italy
autor
- Department of Sciences, Roma Tre University, Viale Guglielmo Marconi 446, 00146 Rome, Italy, Phone: +39-06-57336362, Fax: +39-06-57336321
Bibliografia
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- 3. Drakesmith H, Nemeth E, Ganz T. Ironing out ferroportin. Cell Metab 2015;22:777–87.
- 4. Montosi G, Donovan A, Totaro A, Garuti C, Pignatti E, Cassanelli S, et al. Autosomal-dominant hemochromatosis is associated with a mutation in the ferroportin (SLC11A3) gene. J Clin Invest 2001;108:619–23.
- 5. Pietrangelo A. The ferroportin disease: pathogenesis, diagnosis and treatment. Haematologica 2017;102:1972–84.
- 6. Yan N. Structural biology of the major facilitator superfamily transporters. Annu Rev Biophys 2015;44:257–83.7.
- 7. Tortosa V, Bonaccorsi di Patti MC, Musci G, Polticelli F. The human iron exporter ferroportin. Insight into the transport mechanism by molecular modeling. Bio-Algorithms Med-Systems 2016;12:1–7.
- 8. Wallace DF, Harris JM, Subramaniam VN. Functional analysis and theoretical modeling of ferroportin reveals clustering of mutations according to phenotype. Am J Physiol Cell Physiol 2010;298:C75–84.
- 9. Huang Y, Lemieux MJ, Song J, Auer M, Wang DN. Structure and mechanism of the glycerol-3 phosphate transporter from Escherichia coli. Science 2003;301:616–20.
- 10. Le Gac G, Ka C, Joubrel R, Gourlaouen I, Lehn P, Mornon JP, et al. Structure-function analysis of the human ferroportin iron exporter (SLC40A1): effect of hemochromatosis type 4 disease mutations and identification of critical residues. Hum Mutat 2013;34:1371–80.
- 11. Yin Y, He X, Szewczyk P, Nguyen T, Chang G. Structure of the multidrug transporter EmrD from Escherichia coli. Science 2006;312:741–4.
- 12. Bonaccorsi di Patti MC, Polticelli F, Cece G, Cutone A, Felici F, Persichini T, et al. A structural model of human ferroportin and of its iron binding site. FEBS J 2014;281:2851–60.
- 13. Dang S, Sun L, Huang Y, Lu F, Liu Y, Gong H, et al. Structure of a fucose transporter in an outward-open conformation. Nature 2010;467:734–8.
- 14. Taniguchi R, Kato HE, Deshpande CN, Wada M, Ito K, Ishitani R, et al. Outward- and inward-facing structures of a putative bacterial transition-metal transporter with homology to ferroportin. Nat Commun 2015;6:8545.
- 15. Bonaccorsi di Patti MC, Polticelli F, Tortosa V, Furbetta PA, Musci G. A bacterial homologue of the human iron exporter ferroportin. FEBS Lett 2015;21:3829–35.
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- 18. Yang J, Yan R, Roy A, Xu D, Poisson J, Zhang Y. The I-TASSER suite: protein structure and function prediction. Nat Methods 2015;12:7–8.
- 19. Wu S, Zhang Y. LOMETS: a local meta-threading-server for protein structure prediction. Nucleic Acids Res 2007;35:3375–82.
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- 24. Jordan JB, Poppe L, Haniu M, Arvedson T, Syed R, Li V, et al. Hepcidin revisited, disulfide connectivity, dynamics, and structure. J Biol Chem 2009;284:24155–67.
- 25. Pierce BG, Wiehe K, Hwang H, Kim BH, Vreven T, Weng Z. ZDOCK server: interactive docking prediction of protein–protein complexes and symmetric multimers. Bioinformatics 2014;30:1771–3.
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- 27. Mayr R, Janecke AR, Schranz M, Griffiths WJ, Vogel W, Pietrangelo A, et al. Ferroportin disease: a systematic meta-analysis of clinical and molecular findings. J Hepatol 2010;53:941–49.
- 28. Jiang D, Zhao Y, Wang X, Fan J, Heng J, Liu X, et al. Structure of the YajR transporter suggests a transport mechanism based on the conserved motif A. Proc Natl Acad Sci USA 2013;110:14664–9.
- 29. Madej MG, Soro SN, Kaback HR. Apo-intermediate in the transport cycle of lactose permease (LacY). Proc Natl Acad Sci USA 2012;109:E2970–8.
- 30. Jiang D, Zhao Y, Wang X, Fan J, Henga J, Liua X, et al. Structure of the YajR transporter suggests a transport mechanism based on the conserved motif A. Proc Natl Acad Sci USA 2013;110:14664–69.
- 31. Fernandes A, Preza GC, Phung Y, De Domenico I, Kaplan J, Ganz T, et al. The molecular basis of hepcidin-resistant hereditary hemochromatosis. Blood 2009;114:437–43.
- 32. Preza GC, Ruchala P, Pinon R, Ramos E, Qiao B, Peralta MA, et al. Minihepcidins are rationally designed small peptides that mimic hepcidin activity in mice and may be useful for the treatment of iron overload. J Clin Investigation 2011;121:4880–8.
- 33. Qiao B, Sugianto P, Fung E, del-Castillo-Rueda A, Moran-Jimenez MJ, Ganz T, et al. Hepcidin-induced endocytosis of ferroportin is dependent on ferroportin ubiquitination. Cell Met 2012;15:918–24.
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Typ dokumentu
Bibliografia
Identyfikator YADDA
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