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学科主题基础医学
Structural Insights into KChIP4a Modulation of Kv4.3 Inactivation
Liang, Ping1; Wang, Huayi2; Chen, Hao1; Cui, Yuanyuan1; Gu, Lichuan3; Chai, Jijie2; Wang, KeWei1
刊名JOURNAL OF BIOLOGICAL CHEMISTRY
2009-02-20
DOI10.1074/jbc.M807704200
284期:8页:4960-4967
收录类别SCI
文章类型Article
WOS标题词Science & Technology
类目[WOS]Biochemistry & Molecular Biology
资助者Chinese Ministry of Science and Technology ; National Science Foundation of China ; Ministry of Science Technology of China ; Chinese Ministry of Science and Technology ; National Science Foundation of China ; Ministry of Science Technology of China
研究领域[WOS]Biochemistry & Molecular Biology
关键词[WOS]CHANNEL-INTERACTING PROTEINS ; CLOSED-STATE INACTIVATION ; A-TYPE ; K+ CHANNELS ; POTASSIUM CHANNELS ; FUNCTIONAL INTERACTION ; I-TO ; SUBUNIT ; EXPRESSION ; CALCIUM
英文摘要

Dynamic inactivation in Kv4 A-type K(+) current plays a critical role in regulating neuronal excitability by shaping action potential waveform and duration. Multifunctional auxiliary KChIP1-4 subunits, which share a high homology in their C-terminal core regions, exhibit distinctive modulation of inactivation and surface expression of pore-forming Kv4 subunits. However, the structural differences that underlie the functional diversity of Kv channel-interacting proteins (KChIPs) remain undetermined. Here we have described the crystal structure of KChIP4a at 3.0 angstrom resolution, which shows distinct N-terminal alpha-helices that differentiate it from other KChIPs. Biochemical experiments showed that competitive binding of the Kv4.3 N-terminal peptide to the hydrophobic groove of the core of KChIP4a causes the release of the KChIP4a N terminus that suppresses the inactivation of Kv4.3 channels. Electrophysiology experiments confirmed that the first N-terminal alpha-helix peptide (residues 1-34) of KChIP4a, either by itself or fused to N-terminal truncated Kv4.3, can confer slow inactivation. We propose that N-terminal binding of Kv4.3 to the core of KChIP4a mobilizes the KChIP4a N terminus, which serves as the slow inactivation gate.

语种英语
所属项目编号2003-AA210090 ; 30630017 ; 2006AA02Z183 ; 2007CB512100
资助者Chinese Ministry of Science and Technology ; National Science Foundation of China ; Ministry of Science Technology of China ; Chinese Ministry of Science and Technology ; National Science Foundation of China ; Ministry of Science Technology of China
WOS记录号WOS:000263416600026
引用统计
被引频次:16[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/400002259/61067
专题基础医学院_神经生物学系
作者单位1.Natl Inst Biol Sci, Beijing 102206, Peoples R China
2.Peking Univ, Ctr Prot Sci, Dept Neurobiol, Neurosci Res Inst,Key Lab Neurosci,Minist Educ, Beijing 100083, Peoples R China
3.Shandong Univ, State Key Lab Microbial Technol, Jinan 250100, Peoples R China
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GB/T 7714
Liang, Ping,Wang, Huayi,Chen, Hao,et al. Structural Insights into KChIP4a Modulation of Kv4.3 Inactivation[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2009,284(8):4960-4967.
APA Liang, Ping.,Wang, Huayi.,Chen, Hao.,Cui, Yuanyuan.,Gu, Lichuan.,...&Wang, KeWei.(2009).Structural Insights into KChIP4a Modulation of Kv4.3 Inactivation.JOURNAL OF BIOLOGICAL CHEMISTRY,284(8),4960-4967.
MLA Liang, Ping,et al."Structural Insights into KChIP4a Modulation of Kv4.3 Inactivation".JOURNAL OF BIOLOGICAL CHEMISTRY 284.8(2009):4960-4967.
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