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The present study examined the binding of the individual N- and C-lobes of calmodulin (CaM) to Cav1.2 at different Ca2+ concentration ([Ca2+]) from ≈ free to 2mM, and found that they may bind to Cav1.2 Ca2+-dependently. In particular, using the patch-clamp technique, we confirmed that the N- or C-lobes can rescue the basal activity of Cav1.2 from run-down, demonstrating the functional relevance of...
To demonstrate the interaction of calpastatin (CS) domain L (CSL) with Cav1.2 channel, we investigated the binding of CSL with various C-terminus-derived peptides at≈free, 100nM, 10μM, and 1mM Ca2+ by using the GST pull-down assay method. Besides binding with the IQ motif, CSL was also found to bind with the PreIQ motif. With increasing [Ca2+], the affinity of the CSL–IQ interaction gradually decreased,...
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