کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
4323115 | 1291752 | 2006 | 17 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Modulation of Inactivation Properties of CaV2.2 Channels by 14-3-3 Proteins Modulation of Inactivation Properties of CaV2.2 Channels by 14-3-3 Proteins](/preview/png/4323115.png)
SummaryInactivation of presynaptic CaV2.2 channels may play a role in regulating short-term synaptic plasticity. Here, we report a direct modulation of CaV2.2 channel inactivation properties by 14-3-3, a family of signaling proteins involved in a wide range of biological processes. The structural elements critical for 14-3-3 binding and channel modulation lie in the carboxyl tail of the pore-forming α1B subunit, where we have identified two putative 14-3-3 interaction sites, including a phosphoserine-containing motif that directly binds to 14-3-3 and a second region near the EF hand and IQ domain. In transfected tsA 201 cells, 14-3-3 coexpression dramatically slows open-state inactivation and reduces cumulative inactivation of CaV2.2 channels. In hippocampal neurons, interference with 14-3-3 binding accelerates CaV2.2 channel inactivation and enhances short-term synaptic depression. These results demonstrate that 14-3-3 proteins are important regulators of CaV2.2 channel activities and through this mechanism may contribute to their regulation of synaptic transmission and plasticity.
Journal: - Volume 51, Issue 6, 21 September 2006, Pages 755–771