The Ca2+-dependent interaction of calpastatin domain L with the C-terminal tail of the Cav1.2 channel

被引：17

作者：

Sun, Wei ^{[1
]}

Feng, Rui ^{[1
,2
]}

Hu, Huiyuan ^{[1
,2
]}

Guo, Feng ^{[1
,2
]}

Gao, Qinghua ^{[1
,2
]}

Shao, Dongxue ^{[1
]}

Yin, Dandan ^{[1
]}

Wang, Hongmei ^{[1
]}

Sun, Xuefei ^{[1
,2
]}

Zhao, Meimi ^{[1
,2
]}

Minobe, Etsuko ^{[3
]}

Sun, Yingxian ^{[2
]}

Jiao, Guangyu ^{[4
,5
]}

Kameyama, Masaki ^{[3
]}

Hao, Liying ^{[1
,2
]}

机构：

[1] China Med Univ, Sch Pharm, Dept Pharmaceut Toxicol, Shenyang 110001, Peoples R China

[2] China Med Univ, Cardiovasc Inst, Shenyang 110001, Peoples R China

[3] Kagoshima Univ, Grad Sch Med & Dent Sci, Dept Physiol, Kagoshima 8908544, Japan

[4] China Med Univ, Shengjing Hosp, Resp Dept, Shenyang 110001, Peoples R China

[5] China Med Univ, Shengjing Hosp, Intens Care Unit, Shenyang 110001, Peoples R China

来源：

FEBS LETTERS | 2014年 / 588卷 / 05期

关键词：

Calpastatin; Ca2+; Cav1.2; Binding; Affinity; CALMODULIN-BINDING SITE; CA2+ CHANNELS; RUN-DOWN; INACTIVATION;

D O I：

10.1016/j.febslet.2014.01.019

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 approximate to free, 100 nM, 10 mu M, 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. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：665 / 671

页数：7

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