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Mast cells are important effector cells in IgE-mediated allergic reactions. As both FcepsilonRI and the endosomal/lysosomal compartment are known to be involved in signal transduction, we investigated the possibility that IgE receptor surface expression could involve cis-trans PDIA1-FcepsilonRI interactions. To this end, we conducted a yeast two hybrid screen and discovered an association of PDIA1 with the IgG Fc gamma receptor FcepsilonRI alpha chain. In addition, co-immunoprecipitation experiments using mast cells revealed that PDIA1 bound to the alpha chain of FcepsilonRI. Also, the isolation of PDIA1 was followed by a mass spectrometry analysis that identified the alpha chain of FcepsilonRI as one of the PDIA1 binding partners in mast cells. The C-terminal polypeptide of FcepsilonRI alpha was important for the PDIA1-FcepsilonRI interaction. In line with previous studies, PDIA1 was involved in IgE-dependent signaling as shown by monitoring FcepsilonRI-mediated degranulation. In addition, we found that IgE-mediated stimulation resulted in a higher degranulation response in the presence of PDIA1. However, FcepsilonRI-mediated degranulation as well as the anti-IgE-induced Ca(2+) release were not affected by PDIA1 overexpression. Therefore, PDIA1 plays an important role in FcepsilonRI-mediated degranulation, but it does not modulate any of the steps of mast cell activation that depend on FcepsilonRI and G alpha q.Pharmacological doses of nicotine can cause either beneficial effects or adverse effects, depending on the interaction with the many modulatory sites and cellular mechanisms that control brain activity. In the present proposal, we will examine
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