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Polarized Translocation of Fluorescent Proteins in Xenopus Ectoderm in Response to Wnt Signaling

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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.

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Mimicking the Function of Signaling Proteins: Toward Artificial Signal Transduction Therapy

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Published on: September 29, 2016

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.