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Signal transduction through prion protein
S Mouillet-Richard1, M Ermonval, C Chebassier
1Différenciation Cellulaire, CNRS-Institut Pasteur, 75724 Paris Cedex 15, France. srichard@pasteur.fr
Science (New York, N.Y.)
|September 16, 2000
Summary
The cellular prion protein (PrPc) may act as a signal transducer. Antibody cross-linking revealed PrPc couples to the Fyn tyrosine kinase in differentiated neuronal cells, primarily at neurites.
Area of Science:
- Neuroscience
- Cell Biology
- Biochemistry
Background:
- The cellular prion protein (PrPc) is a cell-surface protein with an undefined biological role.
- Understanding PrPc's function is crucial for neurobiology and disease research.
Purpose of the Study:
- To investigate potential signal transduction roles of PrPc.
- To identify signaling pathways associated with PrPc in neuronal differentiation.
Main Methods:
- Utilized the murine 1C11 neuronal differentiation model.
- Employed antibody-mediated cross-linking to probe PrPc interactions.
- Investigated the involvement of caveolin-1 and clathrin in PrPc signaling.
Main Results:
- Demonstrated a caveolin-1-dependent coupling of PrPc to the tyrosine kinase Fyn.
- Observed potential contribution of clathrin to this coupling.
- Found PrPc-dependent Fyn activation was specific to differentiated serotonergic and noradrenergic 1C11 cell progenies.
- Localized PrPc signaling activity predominantly to neurites.
Conclusions:
- Suggests PrPc functions as a signal transduction protein.
- Highlights the role of PrPc in neuronal signaling pathways.
- Indicates PrPc's signaling capacity is linked to specific neuronal differentiation states.
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