Referenced in: none

Automatically associated channels: Cav1.2

Title: The individual N- and C-lobes of calmodulin tether to the Cav1.2 channel and rescue the channel activity from run-down in ventricular myocytes of guinea-pig heart.

Authors: Dongxue Shao, Meimi Zhao, Jianjun Xu, Rui Feng, Feng Guo, Huiyuan Hu, Xuefei Sun, Qinghua Gao, Guilin He, Wei Sun, Hongmei Wang, Lifeng Yu, Suyuan Liu, Yaonan Zhu, Etsuko Minobe, Tong Zhu, Masaki Kameyama, Liying Hao

Journal, date & volume: FEBS Lett., 2014 Nov 3 , 588, 3855-61

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/25268113

Abstract
The present study examined the binding of the individual N- and C-lobes of calmodulin (CaM) to Cav1.2 at different Ca(2+) concentration ([Ca(2+)]) from ≈ free to 2mM, and found that they may bind to Cav1.2 Ca(2+)-dependently. In particular, using the patch-clamp technique, we confirmed that the N- or C-lobes can rescue the basal activity of Cav1.2 from run-down, demonstrating the functional relevance of the individual lobes. The data imply that at resting [Ca(2+)], CaM may tether to the channel with its single lobe, leading to multiple CaM molecule binding to increase the grade of Ca(2+)-dependent regulation of Cav1.2.