TRANSDUCTION OF MEMBRANE TENSION BY THE ION-CHANNEL ALAMETHICIN

被引:83
作者
OPSAHL, LR
WEBB, WW
机构
[1] CORNELL UNIV,DEPT PHYS,ITHACA,NY 14853
[2] CORNELL UNIV,SCH APPL & ENGN PHYS,ITHACA,NY 14853
基金
美国国家科学基金会; 美国国家卫生研究院;
关键词
D O I
10.1016/S0006-3495(94)80751-9
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Mechanoelectrical transduction in biological cells is generally attributed to tension-sensitive ion channels, but their mechanisms and physiology remain controversial due to the elusiveness of the channel proteins and potential cytoskeletal interactions. Our discovery of membrane tension sensitivity in ion channels formed by the protein alamethicin reconstituted into pure lipid membranes has demonstrated two simple physical mechanisms of cytoskeleton-independent transduction. Single channel analysis has shown that membrane tension energizes mechanical work for changes of conductance state equal to tension times the associated increase in membrane area. Results show a approximate to 40 Angstrom A(2) increase in pore area and transfer of an 80-Angstrom A(2) polypeptide into the membrane. Both mechanisms may be implicated in mechanical signal transduction by cells.
引用
收藏
页码:71 / 74
页数:4
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