Evidence for conformational coupling between two calcium channels

C. Paolini; James D. Fessenden; Isaac N Pessah; C. Franzini-Armstrong

doi:10.1073/pnas.0404836101

Evidence for conformational coupling between two calcium channels

C. Paolini, James D. Fessenden, Isaac N Pessah, C. Franzini-Armstrong

Molecular Biosciences

Research output: Contribution to journal › Article › peer-review

58 Scopus citations

Abstract

Ryanodine receptor 1 (RyR1, the sarcoplasmic reticulum Ca²⁺ release channel) and α_1sdihydropyridine receptor (DHPR, the surface membrane voltage sensor) of skeletal muscle belong to separate membrane systems but are functionally and structurally linked. Four α _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 (≈2-nm) shift in the α_1sDHPR positions, indicating that ryanodine induces large conformational changes in the RyR1 cytoplasmic domain and that the α_1sDHPR-RyR complex acts as a unit.

Original language	English (US)
Pages (from-to)	12748-12752
Number of pages	5
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	101
Issue number	34
DOIs	https://doi.org/10.1073/pnas.0404836101
State	Published - Aug 24 2004

Keywords

Dihydropyridine receptors
E4032A mutant ryanodine receptor
Ryanodine
Ryanodine receptors
Skeletal muscle

ASJC Scopus subject areas

Genetics
General

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10.1073/pnas.0404836101

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title = "Evidence for conformational coupling between two calcium channels",

abstract = "Ryanodine receptor 1 (RyR1, the sarcoplasmic reticulum Ca2+ release channel) and α1sdihydropyridine receptor (DHPR, the surface membrane voltage sensor) of skeletal muscle belong to separate membrane systems but are functionally and structurally linked. Four α 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 (≈2-nm) shift in the α1sDHPR positions, indicating that ryanodine induces large conformational changes in the RyR1 cytoplasmic domain and that the α1sDHPR-RyR complex acts as a unit.",

keywords = "Dihydropyridine receptors, E4032A mutant ryanodine receptor, Ryanodine, Ryanodine receptors, Skeletal muscle",

author = "C. Paolini and Fessenden, {James D.} and Pessah, {Isaac N} and C. Franzini-Armstrong",

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T1 - Evidence for conformational coupling between two calcium channels

AU - Paolini, C.

AU - Fessenden, James D.

AU - Pessah, Isaac N

AU - Franzini-Armstrong, C.

PY - 2004/8/24

Y1 - 2004/8/24

N2 - Ryanodine receptor 1 (RyR1, the sarcoplasmic reticulum Ca2+ release channel) and α1sdihydropyridine receptor (DHPR, the surface membrane voltage sensor) of skeletal muscle belong to separate membrane systems but are functionally and structurally linked. Four α 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 (≈2-nm) shift in the α1sDHPR positions, indicating that ryanodine induces large conformational changes in the RyR1 cytoplasmic domain and that the α1sDHPR-RyR complex acts as a unit.

AB - Ryanodine receptor 1 (RyR1, the sarcoplasmic reticulum Ca2+ release channel) and α1sdihydropyridine receptor (DHPR, the surface membrane voltage sensor) of skeletal muscle belong to separate membrane systems but are functionally and structurally linked. Four α 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 (≈2-nm) shift in the α1sDHPR positions, indicating that ryanodine induces large conformational changes in the RyR1 cytoplasmic domain and that the α1sDHPR-RyR complex acts as a unit.

KW - Dihydropyridine receptors

KW - E4032A mutant ryanodine receptor

KW - Ryanodine

KW - Ryanodine receptors

KW - Skeletal muscle

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DO - 10.1073/pnas.0404836101

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JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

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ER -

Evidence for conformational coupling between two calcium channels

Abstract

Keywords

ASJC Scopus subject areas

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