Signal transduction through prion protein
S Mouillet-Richard, M Ermonval, C Chebassier… - Science, 2000 - science.org
Science, 2000•science.org
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 …
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 …
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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