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Divalent cations activate TRPV1 through promoting conformational change of the extracellular region
Yang, Fan1; Ma, Linlin1,2; Cao, Xu1,3; Wang, KeWei3,4; Zheng, Jie1
刊名JOURNAL OF GENERAL PHYSIOLOGY
2014
DOI10.1085/jgp.201311024
143期:1页:91-103
收录类别SCI
文章类型Article
WOS标题词Science & Technology
类目[WOS]Physiology
研究领域[WOS]Physiology
关键词[WOS]CAPSAICIN RECEPTOR TRPV1 ; EXTERNAL PROTONATION SITES ; NUCLEOTIDE-GATED CHANNELS ; GO POTASSIUM CHANNELS ; BARIUM PERMEATION ; ION CHANNELS ; PORE TURRET ; K+ CHANNEL ; VOLTAGE ; CELLS
英文摘要

Divalent cations Mg2+ and Ba2+ selectively and directly potentiate transient receptor potential vanilloid type 1 heat activation by lowering the activation threshold into the room temperature range. We found that Mg2+ potentiates channel activation only from the extracellular side; on the intracellular side, Mg2+ inhibits channel current. By dividing the extracellularly accessible region of the channel protein into small segments and perturbing the structure of each segment with sequence replacement mutations, we observed that the S1-S2 linker, the S3-S4 linker, and the pore turret are all required for Mg2+ potentiation. Sequence replacements at these regions substantially reduced or eliminated Mg2+-induced activation at room temperature while sparing capsaicin activation. Heat activation was affected by many, but not all, of these structural alternations. These observations indicate that extracellular linkers and the turret may interact with each other. Site-directed fluorescence resonance energy transfer measurements further revealed that, like heat, Mg2+ also induces structural changes in the pore turret. Interestingly, turret movement induced by Mg2+ precedes channel activation, suggesting that Mg2+-induced conformational change in the extracellular region most likely serves as the cause of channel activation instead of a coincidental or accommodating structural adjustment.

语种英语
WOS记录号WOS:000329129800012
项目编号R01NS072377 ; B07001 ; 2013CB531302 ; 81221002
资助机构National Institutes of Health ; UC Davis Health System Research Award ; Ministry of Education of China 111 Project ; Ministry of Science and Technology of China ; National Science Foundation of China ; Australian National Health and Medical Research Council fellowship ; American Heart Association predoctoral fellowship
引用统计
被引频次:14[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.bjmu.edu.cn/handle/400002259/57685
专题北京大学药学院
北京大学药学院_分子与细胞药理学系
作者单位1.Univ Calif Davis, Dept Physiol & Membrane Biol, Davis, CA 95616 USA
2.Univ Queensland, Inst Mol Biosci, St Lucia, Qld 4072, Australia
3.Peking Univ, Sch Pharmaceut Sci, Dept Mol & Cellular Pharmacol, State Key Lab Nat & Biomimet Drugs, Beijing 100191, Peoples R China
4.Peking Univ, PKU IDG McGovern Inst Brain Res, Beijing 100871, Peoples R China
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GB/T 7714
Yang, Fan,Ma, Linlin,Cao, Xu,et al. Divalent cations activate TRPV1 through promoting conformational change of the extracellular region[J]. JOURNAL OF GENERAL PHYSIOLOGY,2014,143(1):91-103.
APA Yang, Fan,Ma, Linlin,Cao, Xu,Wang, KeWei,&Zheng, Jie.(2014).Divalent cations activate TRPV1 through promoting conformational change of the extracellular region.JOURNAL OF GENERAL PHYSIOLOGY,143(1),91-103.
MLA Yang, Fan,et al."Divalent cations activate TRPV1 through promoting conformational change of the extracellular region".JOURNAL OF GENERAL PHYSIOLOGY 143.1(2014):91-103.
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