It has been reported that cellular prion protein (PrPc) is enriched in caveolae or caveolae-like domains with caveolin-1 (Cav-1) participating to signal transduction events by Fyn kinase recruitment. By using the Glutathione-S-transferase (GST)-fusion proteins assay we observed that PrPc strongly interacts in vitro with Cav-1. Thus, we ascertained the PrPc caveolar localization in a hypothalamic neuronal cell line (GN11), by confocal microscopy analysis, flotation on density gradient and co-immunoprecipitation experiments. Following the anti-PrPc antibody-mediated stimulation of live GN11 cells, we observed that PrPc clustered on plasma membrane domains rich in Cav-1 in which Fyn kinase converged to be activated. After these events, a signaling cascade through p42/44 MAP kinase (Erk 1/2) was triggered, suggesting that following translocation from rafts to caveolae or caveolae-like domains PrPc could interact with Cav-1 and induce signal transduction events.
M.Toni, E.Spisni, C.Griffoni, S.Santi, M.Riccio, P.Lenaz, et al. (2006). Cellular prion protein and Caveolin-1 interaction in a neuronal cell line precedes FYN / ERK1/2 signal transduction. JOURNAL OF BIOMEDICINE AND BIOTECHNOLOGY, 2006, 69469/1-69469/13.
Cellular prion protein and Caveolin-1 interaction in a neuronal cell line precedes FYN / ERK1/2 signal transduction
TONI, MATTIA;SPISNI, ENZO;GRIFFONI, CRISTIANA;TOMASI, VITTORIO
2006
Abstract
It has been reported that cellular prion protein (PrPc) is enriched in caveolae or caveolae-like domains with caveolin-1 (Cav-1) participating to signal transduction events by Fyn kinase recruitment. By using the Glutathione-S-transferase (GST)-fusion proteins assay we observed that PrPc strongly interacts in vitro with Cav-1. Thus, we ascertained the PrPc caveolar localization in a hypothalamic neuronal cell line (GN11), by confocal microscopy analysis, flotation on density gradient and co-immunoprecipitation experiments. Following the anti-PrPc antibody-mediated stimulation of live GN11 cells, we observed that PrPc clustered on plasma membrane domains rich in Cav-1 in which Fyn kinase converged to be activated. After these events, a signaling cascade through p42/44 MAP kinase (Erk 1/2) was triggered, suggesting that following translocation from rafts to caveolae or caveolae-like domains PrPc could interact with Cav-1 and induce signal transduction events.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
