The Ca-dependent interaction of calpastatin domain L with the C-terminal tail of the Cav1.2 channel |
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| 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 |
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| Institution: | 1. Department of Pharmaceutical Toxicology, School of Pharmacy, China Medical University, Shenyang 110001, China;2. Cardiovascular Institute of China Medical University, Shenyang 110001, China;3. Department of Physiology, Graduate School of Medical and Dental Sciences, Kagoshima University, Kagoshima 890-8544, Japan;4. Respiratory Department and Intensive Care Unit, Shengjing Hospital of China Medical University, Shenyang 110004, China |
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| 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 1 mM Ca2+ 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 Ca2+], 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 Ca2+-dependent manners. |
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| Keywords: | Calpastatin Ca2+ Cav1 2 Binding Affinity |
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