scholarly journals In vivoexpression of G-protein β1γ2dimer in adult mouse skeletal muscle alters L-type calcium current and excitation-contraction coupling

2010 ◽  
Vol 588 (15) ◽  
pp. 2945-2960 ◽  
Author(s):  
Norbert Weiss ◽  
Claude Legrand ◽  
Sandrine Pouvreau ◽  
Hicham Bichraoui ◽  
Bruno Allard ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
G Protein ◽  
Calcium Current ◽  
Adult Mouse ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
Mouse Skeletal Muscle

scholarly journals Short-Term Regulation of Excitation-Contraction Coupling by the β1a Subunit in Adult Mouse Skeletal Muscle

2005 ◽  
Vol 89 (6) ◽  
pp. 3976-3984 ◽  
Author(s):  
María C. García ◽  
Elba Carrillo ◽  
José M. Galindo ◽  
Ascensión Hernández ◽  
Julio A. Copello ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Adult Mouse ◽  
Short Term ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
Mouse Skeletal Muscle

scholarly journals Dual Roles of Extracellular Calcium in Excitation-Contraction Coupling of Mouse Skeletal Muscle

2012 ◽  
Vol 102 (3) ◽  
pp. 363a
Author(s):  
Juan Ferreira ◽  
Lourdes Figueroa ◽  
Monika Sztretye ◽  
Carlo Manno ◽  
Eduardo Ríos ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Extracellular Calcium ◽  
Dual Roles ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
Mouse Skeletal Muscle

scholarly journals External Ca2+-dependent excitation-contraction coupling in a population of ageing mouse skeletal muscle fibres

2004 ◽  
Vol 560 (1) ◽  
pp. 137-155 ◽  
Author(s):  
Anthony Michael Payne ◽  
Zhenlin Zheng ◽  
Estela González ◽  
Zhong-Min Wang ◽  
María Laura Messi ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fibres ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
Mouse Skeletal Muscle ◽  
Skeletal Muscle Fibres

scholarly journals G-proteins in skeletal muscle. Evidence for a 40 kDa pertussis-toxin substrate in purified transverse tubules

1988 ◽  
Vol 254 (2) ◽  
pp. 405-409 ◽  
Author(s):  
M Toutant ◽  
J Barhanin ◽  
J Bockaert ◽  
B Rouot
Keyword(s):  
Skeletal Muscle ◽  
G Protein ◽  
G Proteins ◽  
Pertussis Toxin ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
Adp Ribosylation ◽  
Alpha Subunits ◽  
Low Salt ◽  
T Tubules

In muscle, it has been established that guanosine 5′-[gamma-thio]triphosphate (GTP[S]), a non-hydrolysable GTP analogue, elicits a rise in tension in chemically skinned fibres, and that pretreatment with Bordetella pertussis toxin (PTX) decreases GTP[S]-induced tension development [Di Virgilio, Salviati, Pozzan & Volpe (1986) EMBO J. 5, 259-262]. In the present study, G-proteins were analysed by PTX-catalysed ADP-ribosylation and by immunoblotting experiments at cellular and subcellular levels. First, the nature of the G-proteins present in neural and aneural zones of rat diaphragm muscle was investigated. PTX, known to catalyse the ADP-ribosylation of the alpha subunit of several G-proteins, was used to detect G-proteins. Three sequential extractions (low-salt-soluble, detergent-soluble and high-salt-soluble) were performed, and PTX was found to label two substrates of 41 and 40 kDa only in the detergent-soluble fraction. The addition of pure beta gamma subunits of G-proteins to the low-salt-soluble extract did not provide a way to detect PTX-catalysed ADP-ribosylation of G-protein alpha subunits in this hydrophilic fraction. In neural as well as in aneural zones, the 39 kDa PTX substrate, very abundant in the nervous system (Go alpha), was not observed. We then studied the nature of the G alpha subunits present in membranes from transverse tubules (T-tubules) purified from rabbit skeletal muscle. Only one 40 kDa PTX substrate was found in T-tubules, known to be the key element of excitation-contraction coupling. The presence of a G-protein in T-tubule membranes was further confirmed by the immunoreactivity detected with an anti-beta-subunit antiserum. A 40 kDa protein was also detected in T-tubule membranes with an antiserum raised against a purified bovine brain Go alpha. The presence of two PTX substrates (41 and 40 kDa) in equal amounts in total muscle extracts, compared with only one (40 kDa) found in purified T-tubule membranes, suggests that this 40 kDa PTX substrate might be involved in excitation-contraction coupling.

scholarly journals Triadin Binding to the C-Terminal Luminal Loop of the Ryanodine Receptor is Important for Skeletal Muscle Excitation–Contraction Coupling

2007 ◽  
Vol 130 (4) ◽  
pp. 365-378 ◽  
Author(s):  
Sanjeewa A. Goonasekera ◽  
Nicole A. Beard ◽  
Linda Groom ◽  
Takashi Kimura ◽  
Alla D. Lyfenko ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Ryanodine Receptor ◽  
Calcium Release ◽  
Striated Muscle ◽  
Single Channel ◽  
Triple Mutant ◽  
Double Mutation ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
Functional Studies

Ca2+ release from intracellular stores is controlled by complex interactions between multiple proteins. Triadin is a transmembrane glycoprotein of the junctional sarcoplasmic reticulum of striated muscle that interacts with both calsequestrin and the type 1 ryanodine receptor (RyR1) to communicate changes in luminal Ca2+ to the release machinery. However, the potential impact of the triadin association with RyR1 in skeletal muscle excitation–contraction coupling remains elusive. Here we show that triadin binding to RyR1 is critically important for rapid Ca2+ release during excitation–contraction coupling. To assess the functional impact of the triadin-RyR1 interaction, we expressed RyR1 mutants in which one or more of three negatively charged residues (D4878, D4907, and E4908) in the terminal RyR1 intraluminal loop were mutated to alanines in RyR1-null (dyspedic) myotubes. Coimmunoprecipitation revealed that triadin, but not junctin, binding to RyR1 was abolished in the triple (D4878A/D4907A/E4908A) mutant and one of the double (D4907A/E4908A) mutants, partially reduced in the D4878A/D4907A double mutant, but not affected by either individual (D4878A, D4907A, E4908A) mutations or the D4878A/E4908A double mutation. Functional studies revealed that the rate of voltage- and ligand-gated SR Ca2+ release were reduced in proportion to the degree of interruption in triadin binding. Ryanodine binding, single channel recording, and calcium release experiments conducted on WT and triple mutant channels in the absence of triadin demonstrated that the luminal loop mutations do not directly alter RyR1 function. These findings demonstrate that junctin and triadin bind to different sites on RyR1 and that triadin plays an important role in ensuring rapid Ca2+ release during excitation–contraction coupling in skeletal muscle.

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