Abstract
Ca 2+-dependent inactivation (CDI) of L-type voltage-gated Ca 2+ channels limits Ca 2+ entry into neurons, thereby regulating numerous cellular events. Here we present the isolation and purification of the Ca 2+-sensor complex, consisting of calmodulin (CaM) and part of the channel's pore-forming α 1C subunit, and demonstrate the Ca 2+-dependent conformational shift that underlies inactivation. Dominant-negative CaM mutants that prevent CDI block the sensor's Ca 2+-dependent conformational change. We show how Ile1654 in the CaM binding IQ motif of α 1C forms the link between the Ca 2+ sensor and the downstream inactivation machinery, using the α 1C EF hand motif as a signal transducer to activate the putative pore-occluder, the α 1C I-II intracellular linker.
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