Functional equivalence of dihydropyridine receptor a1S and b1a subunits in triggering excitation-contraction coupling in skeletal muscle

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 muta...

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Main Authors: ROBERTO CORONADO, CHRIS A AHERN, DAVID C SHERIDAN, WEIJUN CHENG, LEAH CARBONNEAU, DIPANKAR BHATTACHARYA
Format: Article
Language:English
Published: BMC 2004-01-01
Series:Biological Research
Subjects:
Online Access:http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602004000400010
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spelling doaj-e64f2d5ee9e745f28952520457d9e0842020-11-25T00:47:43ZengBMCBiological Research0716-97600717-62872004-01-01374565575Functional equivalence of dihydropyridine receptor a1S and b1a subunits in triggering excitation-contraction coupling in skeletal muscleROBERTO CORONADOCHRIS A AHERNDAVID C SHERIDANWEIJUN CHENGLEAH CARBONNEAUDIPANKAR BHATTACHARYAMolecular 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 pairhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602004000400010L-type Ca2+ channelCa2+ transientsconfocal imagingcDNA expressionb1 KO myotubesDHPR voltage sensor
collection DOAJ
language English
format Article
sources DOAJ
author ROBERTO CORONADO
CHRIS A AHERN
DAVID C SHERIDAN
WEIJUN CHENG
LEAH CARBONNEAU
DIPANKAR BHATTACHARYA
spellingShingle ROBERTO CORONADO
CHRIS A AHERN
DAVID C SHERIDAN
WEIJUN CHENG
LEAH CARBONNEAU
DIPANKAR BHATTACHARYA
Functional equivalence of dihydropyridine receptor a1S and b1a subunits in triggering excitation-contraction coupling in skeletal muscle
Biological Research
L-type Ca2+ channel
Ca2+ transients
confocal imaging
cDNA expression
b1 KO myotubes
DHPR voltage sensor
author_facet ROBERTO CORONADO
CHRIS A AHERN
DAVID C SHERIDAN
WEIJUN CHENG
LEAH CARBONNEAU
DIPANKAR BHATTACHARYA
author_sort ROBERTO CORONADO
title Functional equivalence of dihydropyridine receptor a1S and b1a subunits in triggering excitation-contraction coupling in skeletal muscle
title_short Functional equivalence of dihydropyridine receptor a1S and b1a subunits in triggering excitation-contraction coupling in skeletal muscle
title_full Functional equivalence of dihydropyridine receptor a1S and b1a subunits in triggering excitation-contraction coupling in skeletal muscle
title_fullStr Functional equivalence of dihydropyridine receptor a1S and b1a subunits in triggering excitation-contraction coupling in skeletal muscle
title_full_unstemmed Functional equivalence of dihydropyridine receptor a1S and b1a subunits in triggering excitation-contraction coupling in skeletal muscle
title_sort functional equivalence of dihydropyridine receptor a1s and b1a subunits in triggering excitation-contraction coupling in skeletal muscle
publisher BMC
series Biological Research
issn 0716-9760
0717-6287
publishDate 2004-01-01
description 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
topic L-type Ca2+ channel
Ca2+ transients
confocal imaging
cDNA expression
b1 KO myotubes
DHPR voltage sensor
url http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602004000400010
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