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Science 15 September 2000:
Vol. 289. no. 5486, pp. 1925 - 1928
DOI: 10.1126/science.289.5486.1925
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Reports

Signal Transduction Through Prion Protein

S. Mouillet-Richard,1* M. Ermonval,1 C. Chebassier,12 J. L. Laplanche,2 S. Lehmann,3 J. M. Launay,2 O. Kellermann1

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.

1 Différenciation Cellulaire, CNRS-Institut Pasteur, 75724 Paris Cedex 15, France.
2 CR Claude Bernard, Service de Biochimie, Hôpital Lariboisière, 75009 Paris, and Faculté de Pharmacie, 75005 Paris, France.
3 IGH du CNRS, UPR 1142, 34396 Montpellier Cedex 5, France.
*   To whom correspondence should be addressed. E-mail: srichard{at}pasteur.fr

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J. Biol. Chem. 278, 9064-9072
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Molecular Evolution of the Mammalian Prion Protein.
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Prion and doppel proteins bind to granule cells of the cerebellum.
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Protein Conformation and Diagnostic Tests: The Prion Protein.
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Intercellular Transfer of the Cellular Prion Protein.
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A. C. Magalhaes, J. A. Silva, K. S. Lee, V. R. Martins, V. F. Prado, S. S. G. Ferguson, M. V. Gomez, R. R. Brentani, and M. A. M. Prado (2002)
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