Signal transduction through prion protein.
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.
Mouillet-Richard
S
S
Différenciation Cellulaire, CNRS-Institut Pasteur, 75724 Paris Cedex 15, France. srichard@pasteur.fr
Ermonval
M
M
Chebassier
C
C
Laplanche
J L
JL
Lehmann
S
S
Launay
J M
JM
Kellermann
O
O
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
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