Apo calmodulin binding to the L-type voltage-gated calcium channel Cav1.2 IQ peptide

被引：11
作者：
Lian, Lu-Yun
Myatt, Daniel
Kitmitto, Ashraf
机构：
[1] Univ Liverpool, Sch Biol Sci, Liverpool L69 7ZB, Merseyside, England
[2] Univ Manchester, Sch Med Cardiovasc & Endocrine Sci, Manchester M13 9NT, Lancs, England
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2007年 / 353卷 / 03期
关键词：
L-type voltage-gated calcium channels; apocalmodulin; NMR; electron microscopy; protein-protein interactions;
D O I：
10.1016/j.bbrc.2006.12.070
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：
The influx of calcium through the L-type voltage-gated calcium channels (LTCCs) is the trigger for the process of calcium-induced calcium release (CICR) from the sarcoplasmic recticulum, an essential step for cardiac contraction. There are two feedback mechanisms that regulate LTCC activity: calcium-dependent inactivation (CDI) and calcium-dependent facilitation (CDF), both of which are mediated by calmodulin (CaM) binding. The IQ domain (aa 1645-1668) housed within the cytoplasmic domain of the LTCC Ca-v 1.2 subunit has been shown to bind both calcium-loaded (Ca2+CaM) and calcium-free CaM (apoCaM). Here, we provide new data for the structural basis for the interaction of apoCaM with the IQ peptide using NMR, revealing that the apoCaM Globe residues are most significantly perturbed upon complex formation. In addition, we have employed transmission electron microscopy of purified LTCC complexes which shows that both apoCaM and Ca2+CaM can bind to the intact channel. (c) 2006 Elsevier Inc. All rights reserved.
引用
收藏
页码：565 / 570
页数：6
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