title: Signal transduction through prion protein.
abstract: 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.
authors.affiliation: Différenciation Cellulaire, CNRS-Institut Pasteur, 75724 Paris Cedex 15, France. srichard@pasteur.fr
authors.forename: S
authors.initials: S
authors.lastname: Mouillet-Richard
authors.forename: M
authors.initials: M
authors.lastname: Ermonval
authors.forename: C
authors.initials: C
authors.lastname: Chebassier
authors.forename: J L
authors.initials: JL
authors.lastname: Laplanche
authors.forename: S
authors.initials: S
authors.lastname: Lehmann
authors.forename: J M
authors.initials: JM
authors.lastname: Launay
authors.forename: O
authors.initials: O
authors.lastname: Kellermann
mesh_terms: D000818:Animals; D051242:Caveolin 1; D022461:Caveolins; D002451:Cell Compartmentation; D002454:Cell Differentiation; D004789:Enzyme Activation; D008565:Membrane Proteins / Q000378:metabolism; D051379:Mice; D009474:Neurons / Q000166:cytology / Q000378:metabolism; D018621:PrPC Proteins / Q000378:metabolism*; D011518:Proto-Oncogene Proteins / Q000378:metabolism; D051076:Proto-Oncogene Proteins c-fyn; D015398:Signal Transduction
chemical_list: C495541:Cav1 protein, mouse; D051242:Caveolin 1; D022461:Caveolins; D008565:Membrane Proteins; D018621:PrPC Proteins; D011518:Proto-Oncogene Proteins; C494960:Fyn protein, mouse; D051076:Proto-Oncogene Proteins c-fyn