The role of 14-3-3 dimerization in its modulation of the CaV2.2 channel

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 Ca(V)2.2 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 Ca(V)2.2 pore-forming alpha(1B) subunit. In this addendum, we present our new finding that 14-3-3 self-dimerization is not required for its modulation of Ca(V)2.2 channel inactivation. These studies will help to understand the molecular mechanism underlying 14-3-3-dependent modulation of Ca(V)2.2 channels.