Publication | Open Access
Prion protein is a component of the multimolecular signaling complex involved in T cell activation
112
Citations
26
References
2004
Year
ImmunologyImmune RegulationMolecular BiologyCell DeathImmunologic MechanismCellular PhysiologyRaft Marker Gm1Signaling PathwayReceptor Tyrosine KinaseAutophagyCellular Regulatory MechanismPrion DiseaseProteomicsCell SignalingPrp CTranslational ProteomicsGene ExpressionCell BiologyT Cell ActivationSignal TransductionNatural SciencesPrion ProteinCellular BiochemistryCellular Immune ResponseMedicineMultimolecular Signaling Complex
In this study we analyzed the interaction of prion protein PrP C with components of glycosphingolipid‐enriched microdomains in lymphoblastoid T cells. PrP C was distributed in small clusters on the plasma membrane, as revealed by immunoelectron microscopy. PrP C is present in microdomains, since it coimmunoprecipitates with GM3 and the raft marker GM1. A strict association between PrP C 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 PrP C interacts with ZAP‐70, suggesting that PrP C is a component of the multimolecular signaling complex within microdomains involved in T cell activation.
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