| First Author | Rutishauser D | Year | 2009 |
| Journal | PLoS One | Volume | 4 |
| Issue | 2 | Pages | e4446 |
| PubMed ID | 19209230 | Mgi Jnum | J:183308 |
| Mgi Id | MGI:5318268 | Doi | 10.1371/journal.pone.0004446 |
| Citation | Rutishauser D, et al. (2009) The comprehensive native interactome of a fully functional tagged prion protein. PLoS One 4(2):e4446 |
| abstractText | The enumeration of the interaction partners of the cellular prion protein, PrP(C), may help clarifying its elusive molecular function. Here we added a carboxy proximal myc epitope tag to PrP(C). When expressed in transgenic mice, PrP(myc) carried a GPI anchor, was targeted to lipid rafts, and was glycosylated similarly to PrP(C). PrP(myc) antagonized the toxicity of truncated PrP, restored prion infectibility of PrP(C)-deficient mice, and was physically incorporated into PrP(Sc) aggregates, indicating that it possessed all functional characteristics of genuine PrP(C). We then immunopurified myc epitope-containing protein complexes from PrP(myc) transgenic mouse brains. Gentle differential elution with epitope-mimetic decapeptides, or a scrambled version thereof, yielded 96 specifically released proteins. Quantitative mass spectrometry with isotope-coded tags identified seven proteins which co-eluted equimolarly with PrP(C) and may represent component of a multiprotein complex. Selected PrP(C) interactors were validated using independent methods. Several of these proteins appear to exert functions in axomyelinic maintenance. |
