Subunit organization and functional transitions in Ci-VSP

被引:112
作者
Kohout, Susy C. [1 ]
Ulbrich, Maximilian H. [1 ]
Bell, Sarah C. [2 ]
Isacoff, Ehud Y. [1 ,3 ,4 ]
机构
[1] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA
[2] Univ Calif Berkeley, Chem Biol Grad Program, Berkeley, CA 94720 USA
[3] Lawrence Berkeley Natl Lab, Div Mat Sci, Berkeley, CA 94720 USA
[4] Lawrence Berkeley Natl Lab, Phys Biosci Div, Berkeley, CA 94720 USA
关键词
D O I
10.1038/nsmb1320
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
Voltage-sensing domains (VSDs) confer voltage dependence on effector domains of membrane proteins. Ion channels use four VSDs to control a gate in the pore domain, but in the recently discovered phosphatase Ci-VSP, the number of subunits has been unknown. Using single-molecule microscopy to count subunits and voltage clamp fluorometry to detect structural dynamics, we found Ci-VSP to be a monomer, which operates independently, but nevertheless undergoes multiple voltage-dependent conformational transitions.
引用
收藏
页码:106 / 108
页数:3
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