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  • Title: PrPC interacts with potassium channel tetramerization domain containing 1 (KCTD1) protein through the PrP(51-136) region containing octapeptide repeats.
    Author: Huang T, Xu J, Xiang J, Lu Y, Chen R, Huang L, Xiao G, Sun G.
    Journal: Biochem Biophys Res Commun; 2012 Jan 06; 417(1):182-6. PubMed ID: 22138399.
    Abstract:
    To identify molecular interaction partners of the cellular prion protein (PrP(C)), we applied a yeast two-hybrid screen on a bovine brain cDNA expression library and identified the potassium channel tetramerization domain containing 1 (KCTD1) as a PrP(C) interacting protein. Deletion mapping showed that PrP(C) specifically binds KCTD1 through the unstructured PrP(51-136) region. We further confirmed the interaction between PrP(C) and KCDT1 protein by co-immunoprecipitation in vivo and by a biosensor assay in vitro. Interestingly, the binding of an insertion mutant PrP(8OR) to KCTD1 is higher than that of wild-type PrP(C), suggesting an important role for an unstructured region harboring octapeptide repeats in the KCTD1-PrP(C) interaction. Our results identify a novel PrP(C)-interacting protein and suggest a new approach to investigating the unidentified physiological cellular function of PrP(C).
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