Evidence for conformational coupling between two calcium channels

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

Research output: Contribution to journalArticle

56 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)12748-12752
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume101
Issue number34
DOIs
StatePublished - 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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