Evidence for conformational coupling between two calcium channels

被引：58
作者：
Paolini, C
Fessenden, JD
Pessah, IN
Franzini-Armstrong, C
机构：
[1] Univ Penn, Dept Cell & Dev Biol, Philadelphia, PA 19104 USA
[2] Brigham & Womens Hosp, Dept Anesthesia Res, Boston, MA 02115 USA
[3] Univ Calif Davis, Sch Vet Med, Dept Mol Biosci, Davis, CA 95616 USA
来源：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2004年 / 101卷 / 34期
关键词：
dihydropyridine receptors; ryanodine receptors; skeletal muscle; ryanodine; E4032A mutant ryanodine receptor;
D O I：
10.1073/pnas.0404836101
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
Ryanodine receptor 1 (RyR1, the sarcoplasmic reticulum Ca2+ release channel) and alsdihydropyridine receptor (DHPR, the surface membrane voltage sensor) of skeletal muscle belong to separate membrane systems but are functionally and structurally linked. Four alpha(15)DHPRs 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 (approximate to2-nm) shift in the alpha(15)DHPR positions, indicating that ryanodine induces large conformational changes in the RyR1 cytoplasmic domain and that the alpha(15)DHPR-RyR complex acts as a unit.
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收藏
页码：12748 / 12752
页数：5
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