Ion channel targets
Print ISSN 1933-6950; Online ISSN 1933-6969

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Article Addendum

The Role of 14-3-3 Dimerization in Its Modulation of the CaV2.2 Channel

Yong Li, Yuying Wu, Rui Li and Yi Zhou

volume 1 | issue 1

January/February 2007
Pages: 1 - 2

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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.

Authors

Yong Li

Huashan Hospital

Yuying Wu

University of Alabama at Birmingham

Rui Li

University of Alabama at Birmingham

Yi Zhou

University of Alabama at Birmingham



We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link:
 Download PDF

If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.