[HTML][HTML] Prion protein is a component of the multimolecular signaling complex involved in T cell activation
V Mattei, T Garofalo, R Misasi, A Circella, V Manganelli… - FEBS letters, 2004 - Elsevier
V Mattei, T Garofalo, R Misasi, A Circella, V Manganelli, G Lucania, A Pavan, M Sorice
FEBS letters, 2004•ElsevierIn this study we analyzed the interaction of prion protein PrPC with components of
glycosphingolipid-enriched microdomains in lymphoblastoid T cells. PrPC was distributed in
small clusters on the plasma membrane, as revealed by immunoelectron microscopy. PrPC
is present in microdomains, since it coimmunoprecipitates with GM3 and the raft marker
GM1. A strict association between PrPC and Fyn was revealed by scanning confocal
microscopy and coimmunoprecipitation experiments. The phosphorylation protein ZAP-70 …
glycosphingolipid-enriched microdomains in lymphoblastoid T cells. PrPC was distributed in
small clusters on the plasma membrane, as revealed by immunoelectron microscopy. PrPC
is present in microdomains, since it coimmunoprecipitates with GM3 and the raft marker
GM1. A strict association between PrPC and Fyn was revealed by scanning confocal
microscopy and coimmunoprecipitation experiments. The phosphorylation protein ZAP-70 …
In this study we analyzed the interaction of prion protein PrPC with components of glycosphingolipid-enriched microdomains in lymphoblastoid T cells. PrPC was distributed in small clusters on the plasma membrane, as revealed by immunoelectron microscopy. PrPC is present in microdomains, since it coimmunoprecipitates with GM3 and the raft marker GM1. A strict association between PrPC and Fyn was revealed by scanning confocal microscopy and coimmunoprecipitation experiments. The phosphorylation protein ZAP-70 was immunoprecipitated by anti-PrP after T cell activation. These results demonstrate that PrPC interacts with ZAP-70, suggesting that PrPC is a component of the multimolecular signaling complex within microdomains involved in T cell activation.
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