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Signal Transduction Through Prion Protein

2000; American Association for the Advancement of Science; Volume: 289; Issue: 5486 Linguagem: Inglês

10.1126/science.289.5486.1925

1095-9203

Sophie Mouillet‐Richard, Myriam Ermonval, C. Chebassier, Jean Laplanche, Sylvain Lehmann, Jean‐Marie Launay, Odile Kellermann,

Trace Elements in Health

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