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Figure 2


Fig. 2. Identification of the JP-45 domain interacting with Cav1.1. (A) GST-JP-45 fusion proteins encompassing different domains of JP-45 were bound to glutathione-Sepharose beads and incubated with solubilized rabbit skeletal-muscle microsomal vescicles as described in Materials and Methods. Proteins present in the void (V), last wash (LW) and bound to the beads (B) were separated on a 10% SDS-PAGE, transferred onto nitrocellulose and the presence of the bound Cav1.1 was revealed by western blotting with commercial anti-Cav1.1 Abs. (B) Co-immunoprecipitation experiment with monoclonal anti-JP-45 Ab to pull-down Cav1.1. Experiments were performed as described in the Materials and Methods. Where indicated, recombinant GST-JP-45 domain-2 fusion protein was used to compete-out the interaction between endogenous proteins present in the microsomes forming a supramolecular complex.





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