IR@PKUHSC  > 北京大学基础医学院  > 生物物理学系
学科主题基础医学
CLIC2-RyR1 Interaction and Structural Characterization by Cryo-electron Microscopy
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
2009-03-27
DOI10.1016/j.jmb.2009.01.059
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
WOS记录号WOS:000264941400006
项目编号0430076N ; AR40615 ; RR01219
资助机构American Heart Association ; National Institutes of Health ; NIH Biotechnological Resource
引用统计
被引频次:32[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
版本出版稿
条目标识符http://ir.bjmu.edu.cn/handle/400002259/53585
专题北京大学基础医学院_生物物理学系
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
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GB/T 7714
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.
APA Meng, Xing.,Wang, Guoliang.,Viero, Cedric.,Wang, Qiongling.,Mi, Wei.,...&Yin, Chang-Cheng.(2009).CLIC2-RyR1 Interaction and Structural Characterization by Cryo-electron Microscopy.JOURNAL OF MOLECULAR BIOLOGY,387(2),320-334.
MLA Meng, Xing,et al."CLIC2-RyR1 Interaction and Structural Characterization by Cryo-electron Microscopy".JOURNAL OF MOLECULAR BIOLOGY 387.2(2009):320-334.
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