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学科主题: 基础医学
题名:
CLIC2-RyR1 Interaction and Structural Characterization by Cryo-electron Microscopy
作者: Meng, Xing2; Wang, Guoliang3; Viero, Cedric1; Wang, Qiongling3; Mi, Wei4; Su, Xiao-Dong4; Wagenknecht, Terence2; Williams, Alan J.1; Liu, Zheng2; Yin, Chang-Cheng3
关键词: Ca2+-release channel ; Ca2+ signaling ; chloride intracellular channel 2 ; cryo-electron microscopy ; ryanodine receptor
刊名: JOURNAL OF MOLECULAR BIOLOGY
发表日期: 2009-03-27
DOI: 10.1016/j.jmb.2009.01.059
卷: 387, 期:2, 页:320-334
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology
类目[WOS]: Biochemistry & Molecular Biology
研究领域[WOS]: Biochemistry & Molecular Biology
关键词[WOS]: CALCIUM-RELEASE CHANNEL ; CARDIAC RYANODINE RECEPTOR ; CHLORIDE-ION CHANNEL ; MUSCLE SARCOPLASMIC-RETICULUM ; SKELETAL-MUSCLE ; 3-DIMENSIONAL STRUCTURE ; MOLECULAR-CLONING ; CRYSTAL-STRUCTURE ; ANGSTROM RESOLUTION ; ELECTRON-MICROSCOPY
英文摘要:

Chloride intracellular channel 2 (CLIC2), a newly discovered small protein distantly related to the glutathione transferase (GST) structural family, is highly expressed in cardiac and skeletal muscle, although its physiological function in these tissues has not been established. In the present study, [H-3] ryanodine binding, Ca2+ efflux from skeletal sarcoplasmic reticulum (SR) vesicles, single channel recording, and cryo-electron microscopy were employed to investigate whether CLIC2 can interact with skeletal ryanodine receptor (RyR1) and modulate its channel activity. We found that: (1) CLIC2 facilitated [H-3]ryanodine binding to skeletal SR and purified RyR1, by increasing the binding affinity of ryanodine for its receptor without significantly changing the a parent maximal binding capacity; (2) CLIC2 reduced the maximal Ca2+ efflux rate from skeletal SR vesicles; (3) CLIC2 decreased the open probability of RyR1 channel, through increasing the mean closed time of the channel; (4) CLIC2 bound to a region between domains 5 and 6 in the clamp-shaped region of RyR1; (5) and in the same clamp region, domains 9 and 10 became separated after CLIC2 binding, indicating CLIC2 induced a conformational change of RyR1. These data suggest that CLIC2 can interact with RyR1 and modulate its channel activity. We propose that CLIC2 functions as an intrinsic stabilizer of the closed state of RyR channels. (C) 2009 Elsevier Ltd. All rights reserved.

语种: 英语
所属项目编号: 0430076N ; AR40615 ; RR01219
项目资助者: American Heart Association ; National Institutes of Health ; NIH Biotechnological Resource
WOS记录号: WOS:000264941400006
Citation statistics:
内容类型: 期刊论文
版本: 出版稿
URI标识: http://ir.bjmu.edu.cn/handle/400002259/53585
Appears in Collections:基础医学院_生物物理学系_期刊论文

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作者单位: 1.Cardiff Univ, Sch Med, Wales Heart Res Inst, Dept Cardiol, Cardiff CF14 4XN, S Glam, Wales
2.New York State Dept Hlth, Wadsworth Ctr, Albany, NY 12201 USA
3.Peking Univ, Peking Univ Hlth Sci Ctr, Dept Biophys, Beijing 100191, Peoples R China
4.Peking Univ, Coll Life Sci, Natl Lab Prot Engn & Plant Genet Engn, Beijing 100871, Peoples R China

Recommended Citation:
Meng, Xing,Wang, Guoliang,Viero, Cedric,et al. CLIC2-RyR1 Interaction and Structural Characterization by Cryo-electron Microscopy[J]. JOURNAL OF MOLECULAR BIOLOGY,2009,387(2):320-334.
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