title: 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.
authors.affiliation: 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.
authors.forename: Yong
authors.initials: Y
authors.lastname: Li
authors.forename: Yuying
authors.initials: Y
authors.lastname: Wu
authors.forename: Rui
authors.initials: R
authors.lastname: Li
authors.forename: Yi
authors.initials: Y
authors.lastname: Zhou
mesh_terms: 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
chemical_list: D048948:14-3-3 Proteins; C500545:CACNA1B protein, human; D020864:Calcium Channels, N-Type