The prion-like protein Doppel fails to interact with itself, the prion protein and the 37 kDa/67 kDa laminin receptor in the yeast two-hybrid system

Biochimica et Biophysica Acta - Molecular Basis of Disease

Volumn 1689, Issue 1, 2004, Pages 1-5

  Hundt, Christoph ^a   Weiss, Stefan ^a  

^a UNIVERSITY OF MUNICH   (Germany)

Author keywords

37 kDa 67 kDa laminin receptor; Doppel; Dpl; Ligand; LRP LR; Prion; PrP; Scrapie; Yeast two hybrid system

Indexed keywords

LAMININ RECEPTOR; PRION PROTEIN; PROTEIN; PROTEIN DOPPEL; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; HUMAN; HUMAN CELL; LIGAND BINDING; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; TWO HYBRID SYSTEM; YEAST;

HUMANS; MOLECULAR WEIGHT; PRIONS; PROTEIN BINDING; RECEPTORS, LAMININ; TWO-HYBRID SYSTEM TECHNIQUES;

EID: 2442685141     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2004.02.003     Document Type: Article

References (42)

1. Aguzzi A., Weissmann C. Prion diseases. Haemophilia. 4:1998;619-627
2. Prusiner S.B., Scott M.R., DeArmond S.J., Cohen F.E. Prion protein biology. Cell. 93:1998;337-348
3. Lasmézas C.I., Weiss S. Molecular biology of prion diseases. Cary J.W., Linz J.E., Bhatnagar D. Microbial Foodborne Diseases. Mechanisms of Pathogenicity and Toxin Synthesis. 2000;495-537 Technomic Publishing CO., INC, Lancaster, USA
4. Prusiner S.B. Shattuck lecture - neurodegenerative diseases and prions. N. Engl. J. Med. 344:2001;1516-1526
5. Post K., Pitschke M., Schafer O., Wille H., Appel T.R., Kirsch D., Mehlhorn I., Serban H., Prusiner S.B., Riesner D. Rapid acquisition of beta-sheet structure in the prion protein prior to multimer formation. Biol. Chem. 379:1998;1307-1317
6. Jansen K., Schafer O., Birkmann E., Post K., Serban H., Prusiner S.B., Riesner D. Structural intermediates in the putative pathway from the cellular prion protein to the pathogenic form. Biol. Chem. 382:2001;683-691
7. Knaus K.J., Morillas M., Swietnicki W., Malone M., Surewicz W.K., Yee V.C. Crystal structure of the human prion protein reveals a mechanism for oligomerization. Nat. Struct. Biol. 8:2001;770-774
8. Hundt C., Gauczynski S., Leucht C., Riley M.L., Weiss S. Intra- and interspecies interactions between prion proteins and effects of mutations and polymorphisms. Biol. Chem. 384:2003;791-803
9. Gilch S., Wopfner F., Renner-Muller I., Kremmer E., Bauer C., Wolf E., Brem G., Groschup M.H., Schatzl H.M. Polyclonal anti-PrP auto-antibodies induced with dimeric PrP interfere efficiently with PrPSc propagation in prion-infected cells. J. Biol. Chem. 278:2003;18524-18531
10. Meier P., Genoud N., Prinz M., Maissen M., Rulicke T., Zurbriggen A., Raeber A.J., Aguzzi A. Soluble dimeric prion protein binds PrP(Sc) in vivo and antagonizes prion disease. Cell. 113:2003;49-60
11. Riley M.L., Leucht C., Gauczynski S., Hundt C., Brecelj M., Dodson G., Weiss S. High-level expression and characterization of a glycosylated covalently linked dimer of the prion protein. Protein Eng. 15:2002;529-536
12. Kaneko K., Zulianello L., Scott M., Cooper C.M., Wallace A.C., James T.L., Cohen F.E., Prusiner S.B. Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation. Proc. Natl. Acad. Sci. U. S. A. 94:1997;10069-10074
13. Rieger R., Edenhofer F., Lasmézas C.I., Weiss S. The human 37-kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells. Nat. Med. 3:1997;1383-1388
14. Gauczynski S., Peyrin J.M., Haik S., Leucht C., Hundt C., Rieger R., Krasemann S., Deslys J.P., Dormont D., Lasmezas C.I., Weiss S. The 37-kDa/67-kDa laminin receptor acts as the cell-surface receptor for the cellular prion protein. EMBO J. 20:2001;5863-5875
15. Gauczynski S., Hundt C., Leucht C., Weiss S. Interaction of prion proteins with cell surface receptors, molecular chaperones and other molecules. Adv. Protein Chem. 57:2001;229-272
16. Leucht C., Weiss S. Der prion protein rezeptor. Nova Acta Leopold. 87:2002;39-54
17. Leucht C., Simoneau S., Rey C., Vana K., Rieger R., Lasmezas C.I., Weiss S. The 37 kDa/67 kDa laminin receptor is required for PrP(Sc) propagation in scrapie-infected neuronal cells. EMBO Rep. 4:2003;290-295
18. Hundt C., Peyrin J.M., Haik S., Gauczynski S., Leucht C., Rieger R., Riley M.L., Deslys J.P., Dormont D., Lasmezas C.I., Weiss S. Identification of interaction domains of the prion protein with its 37-kDa/67-kDa laminin receptor. EMBO J. 20:2001;5876-5886
19. Leucht C., Vana K., Renner-Mueller I., Dormont D., Lasmézas C.I., Wolf E., Weiss S. Knock-down of the 37-kDa/67-kDa laminin receptor in mouse brain by transgenic expression of specific antisense LRP RNA. Transgenic Res. 13:2004;81-85
20. Moore R.C., Lee I.Y., Silverman G.L., Harrison P.M., Strome R., Heinrich C., Karunaratne A., Pasternak S.H., Chishti M.A., Liang Y., Mastrangelo P., Wang K., Smit A.F., Katamine S., Carlson G.A., Cohen F.E., Prusiner S.B., Melton D.W., Tremblay P., Hood L.E., Westaway D. Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein Doppel. J. Mol. Biol. 292:1999;797-817
21. Behrens A., Aguzzi A. Small is not beautiful: antagonizing functions for the prion protein PrP(C) and its homologue Dpl. Trends Neurosci. 25:2002;150-154
22. Qin K., Coomaraswamy J., Mastrangelo P., Yang Y., Lugowski S., Petromilli C., Prusiner S.B., Fraser P.E., Goldberg J.M., Chakrabartty A., Westaway D. The PrP-like protein Doppel binds copper. J. Biol. Chem. 278:2003;8888-8896
23. Tuzi N.L., Gall E., Melton D., Manson J.C. Expression of Doppel in the CNS of mice does not modulate transmissible spongiform encephalopathy disease. J. Gen. Virol. 83:2002;705-711
24. Peoc'h K., Volland H., De Gassart A., Beaudry P., Sazdovitch V., Sorgato M.C., Creminon C., Laplanche J.L., Lehmann S. Prion-like protein Doppel expression is not modified in scrapie-infected cells and in the brains of patients with Creutzfeldt-Jakob disease. FEBS Lett. 536:2003;61-65
25. Behrens A., Brandner S., Genoud N., Aguzzi A. Normal neurogenesis and scrapie pathogenesis in neural grafts lacking the prion protein homologue Doppel. EMBO Rep. 2:2001;347-352
26. Shaked Y., Hijazi N., Gabizon R. Doppel and PrP(C) do not share the same membrane microenvironment. FEBS Lett. 530:2002;85-88
27. Sakaguchi S., Katamine S., Nishida N., Moriuchi R., Shigematsu K., Sugimoto T., Nakatani A., Kataoka Y., Houtani T., Shirabe S., Okada H., Hasegawa S., Miyamoto T., Noda T. Loss of cerebellar Purkinje cells in aged mice homozygous for a disrupted PrP gene. Nature. 380:1996;528-531
28. Rossi D., Cozzio A., Flechsig E., Klein M.A., Rulicke T., Aguzzi A., Weissmann C. Onset of ataxia and Purkinje cell loss in PrP null mice inversely correlated with Dpl level in brain. EMBO J. 20:2001;694-702
29. Silverman G.L., Qin K., Moore R.C., Yang Y., Mastrangelo P., Tremblay P., Prusiner S.B., Cohen F.E., Westaway D. Doppel is an N-glycosylated, glycosylphosphatidylinositol-anchored protein. Expression in testis and ectopic production in the brains of Prnp(0/0) mice predisposed to Purkinje cell loss. J. Biol. Chem. 275:2000;26834-26841
30. Behrens A., Genoud N., Naumann H., Rulicke T., Janett F., Heppner F.L., Ledermann B., Aguzzi A. Absence of the prion protein homologue Doppel causes male sterility. EMBO J. 21:2002;3652-3658
31. Vidal M., Legrain P. Yeast forward and reverse 'n'-hybrid systems. Nucleic Acids Res. 27:1999;919-929
32. Warwicker J. Modeling a prion protein dimer: predictions for fibril formation. Biochem. Biophys. Res. Commun. 278:2000;646-652
33. Schätzl H.M., Da-Costa M., Taylor L., Cohen F.E., Prusiner S.B. Prion protein gene variation among primates. J. Mol. Biol. 245:1995;362-374
34. 2+ binding sites in the N-terminal domain of the prion protein by EPR and CD spectroscopy. Biochemistry. 39:2000;13760-13771
35. Atwood C.S., Moir R.D., Huang X., Scarpa R.C., Bacarra N.M., Romano D.M., Hartshorn M.A., Tanzi R.E., Bush A.I. Dramatic aggregation of Alzheimer abeta by Cu(II) is induced by conditions representing physiological acidosis. J. Biol. Chem. 273:1998;12817-12826
36. Priola S.A., Caughey B., Wehrly K., Chesebro B. A 60-kDa prion protein (PrP) with properties of both the normal and scrapie-associated forms of PrP. J. Biol. Chem. 270:1995;3299-3305
37. Peoc'h K., Guerin C., Brandel J.P., Launay J.M., Laplanche J.L. First report of polymorphisms in the prion-like protein gene (PRND): implications for human prion diseases. Neurosci. Lett. 286:2000;144-148
38. Mo H., Moore R.C., Cohen F.E., Westaway D., Prusiner S.B., Wright P.E., Dyson H.J. Two different neurodegenerative diseases caused by proteins with similar structures. Proc. Natl. Acad. Sci. U. S. A. 98:2001;2352-2357
39. Luhrs T., Riek R., Guntert P., Wuthrich K. NMR structure of the human Doppel protein. J. Mol. Biol. 326:2003;1549-1557
40. Lu K., Wang W., Xie Z., Wong B.S., Li R., Petersen R.B., Sy M.S., Chen S.G. Expression and structural characterization of the recombinant human Doppel protein. Biochemistry. 39:2000;13575-13583
41. Wong B.S., Liu T., Paisley D., Li R., Pan T., Chen S.G., Perry G., Petersen R.B., Smith M.A., Melton D.W., Gambetti P., Brown D.R., Sy M.S. Induction of HO-1 and NOS in Doppel-expressing mice devoid of PrP: implications for Doppel function. Mol. Cell. Neurosci. 17:2001;768-775
42. Caughey B. Prion proteins. Adv. Protein Chem. 57:2001;1-405