The ZIP-prion connection

Prion

Volumn 6, Issue 4, 2012, Pages 317-321

  Ehsani, Sepehr ^a,b   Mehrabian, Mohadeseh ^a,b   Pocanschi, Cosmin L ^a   Schmitt Ulms, Gerold ^a,b  

^a UNIVERSITY OF TORONTO   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

Author keywords

Evolution; Prion; Retrogene; Zinc; ZIP metal ion transporter

Indexed keywords

CARRIER PROTEIN; PRION PROTEIN; UNCLASSIFIED DRUG; ZRT IRT LIKE METAL ION TRANSPORTER;

AMINO ACID SEQUENCE; HUMAN; NONHUMAN; PRION DISEASE; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; REVIEW; STRUCTURE ANALYSIS;

ANIMALS; CATION TRANSPORT PROTEINS; EVOLUTION, MOLECULAR; HUMANS; MODELS, MOLECULAR; PRIONS; ZINC;

VERTEBRATA;

EID: 84866542211     PISSN: 19336896     EISSN: 1933690X     Source Type: Journal    
DOI: 10.4161/pri.20196     Document Type: Review

References (30)

1. Schmitt-Ulms G, Ehsani S, Watts JC, Westaway D, Wille H. Evolutionary descent of prion genes from the ZIP family of metal ion transporters. PLoS One 2009; e4:7208; PMID:19784368; http://dx.doi.org/10.1371/journal.pone.0007208.
2. Ehsani S, Tao R, Pocanschi CL, Ren H, Harrison PM, Schmitt-Ulms G. Evidence for retrogene origins of the prion gene family. PLoS One 2011; e6:26800; PMID:22046361; http://dx.doi.org/10.1371/journal.pone.0026800.
3. Ehsani S, Huo H, Salehzadeh A, Pocanschi CL, Watts JC, Wille H, et al. Family reunion - the ZIP/prion gene family. Prog Neurobiol 2011; 93:405-20; PMID:21163327; http://dx.doi.org/10.1016/j.pneurobio.2010.12.001.
4. Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216:136-44; PMID:6801762; http://dx.doi.org/10.1126/science. 6801762.
5. Wickner RB, Shewmaker F, Edskes H, Kryndushkin D, Nemecek J, McGlinchey R, et al. Prion amyloid structure explains templating: how proteins can be genes. FEMS Yeast Res 2010; 10:980-91; PMID:20726897; http://dx.doi.org/10.1111/ j.1567-364.2010.00666.x.
6. Watts JC, Huo H, Bai Y, Ehsani S, Jeon AH, Shi T, et al. Interactome analyses identify ties of PrP and its mammalian paralogs to oligomannosidic N-glycans and endoplasmic reticulum-derived chaperones. PLoS Pathog 2009; e5:1000608; PMID:19798432; http://dx.doi.org/10.1371/journal.ppat.1000608.
7. Taylor KM, Morgan HE, Smart K, Zahari NM, Pumford S, Ellis IO, et al. The emerging role of the LIV-1 subfamily of zinc transporters in breast cancer. Mol Med 2007; 13:396-406; PMID:17673939; http://dx.doi.org/10.2119/2007-00040. Taylor.
8. Diringer H. Proposed link between transmissible spongiform encephalopathies of man and animals. Lancet 1995; 346:1208-10; PMID:7475665; http://dx.doi.org/10.1016/S0140-6736(95)92905-3.
9. Lantos PL. From slow virus to prion: a review of transmissible spongiform encephalopathies. Histopathology 1992; 20:1-11; PMID:1531331; ht tp: //dx.doi .org /10.1111/j.1365-2559.1992.tb00909.x.
10. Manuelidis L. Transmissible encephalopathy agents: virulence, geography and clockwork. Virulence 2010; 1:101-4; PMID:21178425; http://dx.doi.org/10. 4161/viru.1.2.10822.
11. Aguzzi A, Rajendran L. The transcellular spread of cytosolic amyloids, prions and prionoids. Neuron 2009; 64:783-90; PMID:20064386; http://dx.doi.org/10.1016/j.neuron.2009.12.016.
12. Prusiner SB. The prion diseases. Sci Am 1995; 272:48-51.
13. Bin BH, Fukada T, Hosaka T, Yamasaki S, Ohashi W, Hojyo S, et al. Biochemical characterization of human ZIP13 protein: a homo-dimerized zinc transporter involved in the spondylocheiro dysplastic Ehlers-Danlos syndrome. J Biol Chem 2011; 286:40255-65; PMID:21917916; http://dx.doi.org/10.1074/jbc.M111. 256784.
14. Jiayu W, Zhu H, Ming X, Xiong W, Songbo W, Bocui S, et al. Mapping the interaction site of prion protein and Sho. Mol Biol Rep 2010; 37:2295-300; PMID:19685161; http://dx.doi.org/10.1007/s11033-009-9722-0.
15. Hornemann S, Christen B, von Schroetter C, Pérez DR, Wüthrich K. Prion protein library of recombinant constructs for structural biology. FEBS J 2009; 276:2359-67; PMID:19348007; http://dx.doi.org/10.1111/j.1742-4658.2009. 06968.x.
16. Wüthrich K, Riek R. Three-dimensional structures of prion proteins. Adv Protein Chem 2001; 57:55-82; PMID:11447697; http://dx.doi.org/10.1016/S0065- 3233(01)57018-7.
17. Premzl M, Gamulin V. Comparative genomic analysis of prion genes. BMC Genomics 2007; 8:1; PMID:17199895; http://dx.doi.org/10.1186/1471-2164-8-1.
18. Premzl M, Gready JE, Jermiin LS, Simonic T, Marshall Graves JA. Evolution of vertebrate genes related to prion and Shadoo proteins - clues from comparative genomic analysis. Mol Biol Evol 2004; 21:2210-31; PMID:15342797; http://dx.doi.org/10.1093/molbev/msh245.
19. Christen B, Wüthrich K, Hornemann S. Putative prion protein from Fugu (Takifugurubripes). FEBS J 2008; 275:263-70; PMID:18070106; http://dx.doi.org/10.1111/j.1742-4658.2007.06196.x.
20. Ehsani S, Salehzadeh A, Huo H, Reginold W, Pocanschi CL, Ren H, et al. LIV-1 ZIP ectodomain shedding in prion-infected mice resembles cellular response to transition metal starvation. Under review.
21. Kambe T, Andrews GK. Novel proteolytic processing of the ectodomain of the zinc transporter ZIP4 (SLC39A4) during zinc deficiency is inhibited by acrodermatitisenteropathica mutations. Mol Cell Biol 2009; 29:129-39; PMID:18936158; http://dx.doi.org/10.1128/MCB.00963-08.
22. Millhauser GL. Copper and the prion protein: methods, structures, function and disease. Annu Rev Phys Chem 2007; 58:299-320; PMID:17076634; http://dx.doi.org/10.1146/annurev.physchem.58.032806.104657.
23. Dufner-Beattie J, Huang ZL, Geiser J, Xu W, Andrews GK. Mouse ZIP1 and ZIP3 genes together are essential for adaptation to dietary zinc deficiency during pregnancy. Genesis 2006; 44:239-51; PMID:16652366; http://dx.doi.org/10. 1002/dvg.20211.
24. Westaway D, Genovesi S, Daude N, Brown R, Lau A, Lee I, et al. Downregulation of Shadoo in prion infections traces a pre-clinical event inversely related to PrP(Sc) accumulation. PLoS Pathog 2011; e7:1002391; PMID:22114562; http://dx.doi.org/10.1371/journal.ppat.1002391.
25. Watts JC, Stöhr J, Bhardwaj S, Wille H, Oehler A, Dearmond SJ, et al. Protease-resistant prions selectively decrease Shadoo protein. PLoS Pathog 2011; e7:1002382; PMID:22163178; http://dx.doi.org/10.1371/journal.ppat.1002382.
26. Watts JC, Drisaldi B, Ng V, Yang J, Strome B, Horne P, et al. The CNS glycoprotein Shadoo has PrP(C)-like protective properties and displays reduced levels in prion infections. EMBO J 2007; 26:4038- 50; PMID:17703189; http://dx.doi.org/10.1038/sj.emboj.7601830.
27. Chattopadhyay M, Walter ED, Newell DJ, Jackson PJ, Aronoff-Spencer E, Peisach J, et al. The octarepeat domain of the prion protein binds Cu(II) with three distinct coordination modes at pH 7.4. J Am Chem Soc 2005; 127:12647-56; PMID:16144413; http://dx.doi.org/10.1021/ja053254z.
28. Colby DW, Prusiner SB. De novo generation of prion strains. Nat Rev Microbiol 2011; 9:771-7; PMID:21947062; http://dx.doi.org/10.1038/nrmicro2650.
29. Sweeting B, Khan MQ, Chakrabartty A, Pai EF. Structural factors underlying the species barrier and susceptibility to infection in prion disease. Biochem Cell Biol 2010; 88:195-202; PMID:20453922; http://dx.doi.org/10.1139/ O09-172.
30. Weissmann C, Li J, Mahal SP, Browning S. Prions on the move. EMBO Rep 2011; 12:1109-17; PMID:21997298; http://dx.doi.org/10.1038/embor.2011.192.