The role of 14-3-3 dimerization in its modulation of the CaV2.2 channel.
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.
Li
Yong
Y
Department of Neurobiology, Evelyn F. McKnight Brain Institute and Civitan International Research Center, School of Medicine, University of Alabama at Birmingham, Birmingham, Alabama 35294 , USA.
Wu
Yuying
Y
Li
Rui
R
Zhou
Yi
Y
D048948:14-3-3 Proteins / Q000378:metabolism*; D000818:Animals; D020864:Calcium Channels, N-Type / Q000378:metabolism*; D019281:Dimerization; D055724:Electrophysiological Phenomena / Q000502:physiology; D006801:Humans; D011485:Protein Binding / Q000502:physiology; D017434:Protein Structure, Tertiary / Q000502:physiology
D048948:14-3-3 Proteins; C500545:CACNA1B protein, human; D020864:Calcium Channels, N-Type