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Mol Biol Rep ; 37(5): 2295-300, 2010 Jun.
Article in English | MEDLINE | ID: mdl-19685161

ABSTRACT

The cellular prion protein (PrP(C)) is a highly conserved protein among mammals and is considered to have important cellular functions. Despite decades of intensive research, however, the physiological function of PrP(C) remains unclear. Sho (Shadoo, shadow of prion protein) and PrP(C) have similar N-terminals, which suggests that the two proteins share biological functions. Using truncation mutants of both proteins and yeast two-hybrid analysis, with validation by co-immunoprecipitation and surface plasmon resonance (SPR), we have identified an interaction between Sho 61-77 and PrP(C) 108-126 domains. This indicates that Sho may play a role in the physiological function of PrP(C) and prion pathogenesis.


Subject(s)
Nerve Tissue Proteins/metabolism , Prions/metabolism , Protein Interaction Mapping , Animals , GPI-Linked Proteins , Immunoprecipitation , Mice , Nerve Tissue Proteins/chemistry , Prions/chemistry , Protein Binding , Protein Structure, Tertiary , Reproducibility of Results , Surface Plasmon Resonance , Two-Hybrid System Techniques
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