期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2004
卷号：101
期号：34
页码：12748-12752
DOI：10.1073/pnas.0404836101
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Ryanodine receptor 1 (RyR1, the sarcoplasmic reticulum Ca2+ release channel) and {alpha}1Sdihydropyridine receptor (DHPR, the surface membrane voltage sensor) of skeletal muscle belong to separate membrane systems but are functionally and structurally linked. Four {alpha}1SDHPRs associated with the four identical subunits of a RyR form a tetrad. We treated skeletal muscle cell lines with ryanodine, at concentrations that block RyRs, and determined whether this treatment affects the distance between DHPRs in the tetrad. We find a substantial ({approx}2-nm) shift in the {alpha}1SDHPR positions, indicating that ryanodine induces large conformational changes in the RyR1 cytoplasmic domain and that the {alpha}1SDHPR-RyR complex acts as a unit.
