Referenced in: none

Automatically associated channels: Cav1.2

Title: Lobe-related concentration- and Ca(2+)-dependent interactions of calmodulin with C- and N-terminal tails of the CaV1.2 channel.

Authors: Guilin He, Feng Guo, Tong Zhu, Dongxue Shao, Rui Feng, Dandan Yin, Xuefei Sun, Huiyuan Hu, Ahhyeon Hwang, Etsuko Minobe, Masaki Kameyama, Liying Hao

Journal, date & volume: J Physiol Sci, 2013 Sep , 63, 345-53

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/23733657

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.