钙调蛋白与 Cav1.2 通道 C 端和 N 端尾部的依赖浓度和 Ca(2+)的结构域相关相互作用。
Lobe-related concentration- and Ca(2+)-dependent interactions of calmodulin with C- and N-terminal tails of the CaV1.2 channel.
机构信息
Department of Pharmaceutical Toxicology, School of Pharmaceutical Science, China Medical University, Shenyang 110001, China.
出版信息
J Physiol Sci. 2013 Sep;63(5):345-53. doi: 10.1007/s12576-013-0270-y. Epub 2013 Jun 4.
Abstract
This study examined the bindings of calmodulin (CaM) and its mutants with the C- and N-terminal tails of the voltage-gated Ca(2+) channel CaV1.2 at different CaM and Ca(2+) concentrations ([Ca(2+)]) by using the pull-down assay method to obtain basic information on the binding mode, including its concentration- and Ca(2+)-dependencies. Our data show that more than one CaM molecule could bind to the CaV1.2 C-terminal tail at high [Ca(2+)]. Additionally, the C-lobe of CaM is highly critical in sensing the change of [Ca(2+)] in its binding to the C-terminal tail of CaV1.2, and the binding between CaM and the N-terminal tail of CaV1.2 requires high [Ca(2+)]. Our data provide new details on the interactions between CaM and the CaV1.2 channel.
摘要
本研究采用 pull-down assay 方法，研究了在不同 CaM 和 Ca²⁺浓度([Ca²⁺])下，钙调蛋白（CaM）及其突变体与电压门控 Ca²⁺通道 CaV1.2 的 C 端和 N 端尾部的结合情况，以获得有关结合模式的基本信息，包括其浓度和 Ca²⁺依赖性。我们的数据表明，在高 [Ca²⁺] 下，一个以上的 CaM 分子可以与 CaV1.2 C 端尾部结合。此外，CaM 的 C 结构域在感知其与 CaV1.2 C 端尾部结合时 Ca²⁺浓度变化方面非常关键，而 CaM 与 CaV1.2 N 端尾部的结合需要高 [Ca²⁺]。我们的数据为 CaM 和 CaV1.2 通道之间的相互作用提供了新的细节。
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