Abstract
Voltage dependent inactivation is an important property of voltage gated calcium channels. Recently, we have reported that 14 3 3 proteins profoundly reduce inactivation of the CaV2.2 channel at both open and closed states. Using a combination of molecular, biochemical and electrophysiological approaches, we have shown that the modulation is mediated by 14 3 3 binding to the carboxyl tail of the CaV2.2 pore forming α1B subunit. In this addendum, we present our new finding that 14 3 3 self dimerization is not required for its modulation of CaV2.2 channel inactivation. These studies will help to understand the molecular mechanism underlying 14 3 3 dependent modulation of CaV2.2 channels.
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