scholarly journals Channel Gating Dependence on Pore Lining Helix Glycine Residues in Skeletal Muscle Ryanodine Receptor

2015 ◽  
Vol 290 (28) ◽  
pp. 17535-17545 ◽  
Author(s):  
Yingwu Mei ◽  
Le Xu ◽  
David D. Mowrey ◽  
Raul Mendez Giraldez ◽  
Ying Wang ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Ryanodine Receptor ◽  
Channel Gating ◽  
Pore Lining

scholarly journals G4941K substitution in the pore-lining S6 helix of the skeletal muscle ryanodine receptor increases RyR1 sensitivity to cytosolic and luminal Ca2+

2017 ◽  
Vol 293 (6) ◽  
pp. 2015-2028 ◽  
Author(s):  
Le Xu ◽  
David D. Mowrey ◽  
Venkat R. Chirasani ◽  
Ying Wang ◽  
Daniel A. Pasek ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Ryanodine Receptor ◽  
Pore Lining

Primary structure and expression from complementary DNA of skeletal muscle ryanodine receptor

Nature ◽  
1989 ◽  
Vol 339 (6224) ◽  
pp. 439-445 ◽  
Author(s):  
Hiroshi Takeshima ◽  
Seiichiro Nishimura ◽  
Takeshi Matsumoto ◽  
Hiroyuki Ishida ◽  
Kenji Kangawa ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Ryanodine Receptor ◽  
Primary Structure ◽  
Complementary Dna

scholarly journals Oxygen-coupled redox regulation of the skeletal muscle ryanodine receptor-Ca2+ release channel by NADPH oxidase 4

2011 ◽  
Vol 108 (38) ◽  
pp. 16098-16103 ◽  
Author(s):  
Q.-A. Sun ◽  
D. T. Hess ◽  
L. Nogueira ◽  
S. Yong ◽  
D. E. Bowles ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Nadph Oxidase ◽  
Ryanodine Receptor ◽  
Redox Regulation ◽  
Release Channel ◽  
Nadph Oxidase 4

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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