Referenced in: none

Automatically associated channels: Cav1.2

Title: The Ca(2+)-dependent interaction of calpastatin domain L with the C-terminal tail of the Cav1.2 channel.

Authors: Wei Sun, Rui Feng, Huiyuan Hu, Feng Guo, Qinghua Gao, Dongxue Shao, Dandan Yin, Hongmei Wang, Xuefei Sun, Meimi Zhao, Etsuko Minobe, Yingxian Sun, Guangyu Jiao, Masaki Kameyama, Liying Hao

Journal, date & volume: FEBS Lett., 2014 Mar 3 , 588, 665-71

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/24462690

Abstract
To demonstrate the interaction of calpastatin (CS) domain L (CSL) with Cav1.2 channel, we investigated the binding of CSL with various C-terminus-derived peptides at≈free, 100 nM, 10 μM, and 1mM Ca(2+) by using the GST pull-down assay method. Besides binding with the IQ motif, CSL was also found to bind with the PreIQ motif. With increasing [Ca(2+)], the affinity of the CSL-IQ interaction gradually decreased, and the affinity of the CSL-PreIQ binding gradually increased. The results suggest that CSL may bind with both the IQ and PreIQ motifs of the Cav1.2 channel in different Ca(2+)-dependent manners.