PloS one, 2009-02, Vol.4 (2), p.e4446-e4446
2009
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Details
- Autor(en) / Beteiligte
- Titel
- The comprehensive native interactome of a fully functional tagged prion protein
- Ist Teil von
- PloS one, 2009-02, Vol.4 (2), p.e4446-e4446
- Ort / Verlag
- United States: Public Library of Science
- Erscheinungsjahr
- 2009
- Quelle
- Free E-Journal (出版社公開部分のみ）
- Beschreibungen/Notizen
- 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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 1932-6203eISSN: 1932-6203DOI: 10.1371/journal.pone.0004446Titel-ID: cdi_plos_journals_1289789710
- Format
- –
- Schlagworte
- Amino acids, Animals, Antigenic determinants, Biochemistry/Protein Chemistry, Cell Membrane - drug effects, Cell Membrane - metabolism, Chemical Biology/Protein Chemistry and Proteomics, Chemokines, Crassostrea gigas, Cytokines, Detergents - pharmacology, Elution, Endoplasmic reticulum, Enumeration, Epitopes, Genetic engineering, Glycosylphosphatidylinositol, Homeostasis, Hospitals, Immunoglobulins, Infectious Diseases/Prion Diseases, Isotope Labeling, Laboratory animals, Lipid rafts, Mass Spectrometry, Mass spectroscopy, Mice, Mice, Transgenic, Molecular Biology, Myc protein, Nervous System - drug effects, Nervous System - metabolism, Nervous System - pathology, Neurological Disorders, Neuropathology, Neuroscience/Neurobiology of Disease and Regeneration, Neurotoxicity, Prion protein, Prions, Prions (Proteins), Prions - isolation & purification, Prions - metabolism, Protein Binding - drug effects, Protein Transport - drug effects, Proteins, PrPSc Proteins - isolation & purification, PrPSc Proteins - metabolism, Rafts, Recombinant Fusion Proteins - isolation & purification, Recombinant Fusion Proteins - metabolism, Scientific imaging, Survival Analysis, Tags, Toxicity, Transgenic animals, Transgenic mice