Functional equivalence of dihydropyridine receptor alpha1S and beta1a subunits in triggering excitation-contraction coupling in skeletal muscle
| Autor: | Christopher A. Ahern, Weijun Cheng, Leah Carbonneau, David C. Sheridan, Roberto Coronado, Dipankar Bhattacharya |
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| Rok vydání: | 2005 |
| Předmět: |
Gene isoform
DNA Complementary Calcium Channels L-Type Mutant Muscle Fibers Skeletal L-type Ca2+ channel confocal imaging Models Biological General Biochemistry Genetics and Molecular Biology DHPR voltage sensor Ca2+ transients medicine cDNA expression Animals Muscle Skeletal lcsh:QH301-705.5 RYR1 Microscopy Confocal Voltage-dependent calcium channel Ryanodine receptor Chemistry Myogenesis Skeletal muscle Ryanodine Receptor Calcium Release Channel General Medicine musculoskeletal system b1 KO myotubes Coupling (electronics) Electrophysiology medicine.anatomical_structure Biochemistry lcsh:Biology (General) Biophysics General Agricultural and Biological Sciences Muscle Contraction |
| Zdroj: | Biological Research, Vol 37, Iss 4, Pp 565-575 (2004) Biological Research v.37 n.4 2004 SciELO Chile CONICYT Chile instacron:CONICYT Biological Research, Volume: 37, Issue: 4, Pages: 565-575, Published: 2004 |
| ISSN: | 0716-9760 |
| Popis: | 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 alpha1S and beta1a subunits of the skeletal DHPR to EC coupling signaling. Our main contention is that domains of the alpha1S 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 alpha1S/beta1a pair. |
| Databáze: | OpenAIRE |
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