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. 2000 Sep 15;289(5486):1925-8.
doi: 10.1126/science.289.5486.1925.

Signal transduction through prion protein

S Mouillet-Richard  1 , M Ermonval, C Chebassier, J L Laplanche, S Lehmann, J M Launay, O Kellermann
Affiliations

Signal transduction through prion protein

S Mouillet-Richard et al. Science. .

Abstract

The cellular prion protein PrPc is a glycosylphosphatidylinositol-anchored cell-surface protein whose biological function is unclear. We used the murine 1C11 neuronal differentiation model to search for PrPc-dependent signal transduction through antibody-mediated cross-linking. A caveolin-1-dependent coupling of PrPc to the tyrosine kinase Fyn was observed. Clathrin might also contribute to this coupling. The ability of the 1C11 cell line to trigger PrPc-dependent Fyn activation was restricted to its fully differentiated serotonergic or noradrenergic progenies. Moreover, the signaling activity of PrPc occurred mainly at neurites. Thus, PrPc may be a signal transduction protein.

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