Journal article
Functional equivalence of dihydropyridine receptor α1S and β1a subunits in triggering excitation-contraction coupling in skeletal muscle
Biological research, Vol.37(4), pp.565-575
2004
DOI: 10.4067/S0716-97602004000400010
Abstract
Molecular understanding of the mechanism of excitation-contraction (EC) coupling in skeletal muscle has been made possible by cultured myotube models lacking specific dihydropyridine receptor (DHPR) subunits and ryanodine receptor type 1 (RyR1) isoforms. Transient expression of missing cDNAs in mutant myotubes leads to a rapid recovery, within days, of various Ca2+ current and EC coupling phenotypes. These myotube models have thus permitted structure-function analysis of EC coupling domains present in the DHPR controlling the opening of RyR1. The purpose of this brief review is to highlight advances made by this laboratory towards understanding the contribution of domains present in a1S and b1a subunits of the skeletal DHPR to EC coupling signaling. Our main contention is that domains of the a1S II-III loop are necessary but not sufficient to recapitulate skeletal-type EC coupling. Rather, the structural unit that controls the EC coupling signal appears to be the a1S/b1a pair
Details
- Title: Subtitle
- Functional equivalence of dihydropyridine receptor α1S and β1a subunits in triggering excitation-contraction coupling in skeletal muscle
- Creators
- Roberto CoronadoChris A AhernDavid C SheridanWeijun ChengLeah CarbonneauDipankar Bhattacharya
- Resource Type
- Journal article
- Publication Details
- Biological research, Vol.37(4), pp.565-575
- DOI
- 10.4067/S0716-97602004000400010
- ISSN
- 0716-9760
- eISSN
- 0717-6287
- Publisher
- Sociedad de Biología de Chile
- Language
- English
- Date published
- 2004
- Academic Unit
- Molecular Physiology and Biophysics; Iowa Neuroscience Institute
- Record Identifier
- 9984071729002771
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