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...
Main Authors: | , , , , , |
---|---|
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 |
id |
doaj-e64f2d5ee9e745f28952520457d9e084 |
---|---|
record_format |
Article |
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 |
work_keys_str_mv |
AT robertocoronado functionalequivalenceofdihydropyridinereceptora1sandb1asubunitsintriggeringexcitationcontractioncouplinginskeletalmuscle AT chrisaahern functionalequivalenceofdihydropyridinereceptora1sandb1asubunitsintriggeringexcitationcontractioncouplinginskeletalmuscle AT davidcsheridan functionalequivalenceofdihydropyridinereceptora1sandb1asubunitsintriggeringexcitationcontractioncouplinginskeletalmuscle AT weijuncheng functionalequivalenceofdihydropyridinereceptora1sandb1asubunitsintriggeringexcitationcontractioncouplinginskeletalmuscle AT leahcarbonneau functionalequivalenceofdihydropyridinereceptora1sandb1asubunitsintriggeringexcitationcontractioncouplinginskeletalmuscle AT dipankarbhattacharya functionalequivalenceofdihydropyridinereceptora1sandb1asubunitsintriggeringexcitationcontractioncouplinginskeletalmuscle |
_version_ |
1725258996603944960 |