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The role of 14-3-3 dimerization in its modulation of the CaV2.2 channel
1Department of Neurobiology, Evelyn F. McKnight Brain Institute and Civitan International Research Center, School of Medicine, University of Alabama at Birmingham, Birmingham, Alabama 35294 , USA.
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.
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