ArticleThe Biochemical journal1997
Cross-linking analysis of the ryanodine receptor and alpha1-dihydropyridine receptor in rabbit skeletal muscle triads.
Article in The Biochemical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 80 citations in OpenAlex.
- Proteomic profiling of impaired excitation-contraction coupling and abnormal calcium handling in muscular dystrophy.Proteomics · 2022Review
- Comparative gel-based proteomic analysis of chemically crosslinked complexes in dystrophic skeletal muscle.Electrophoresis · 2018Article
- Chemical crosslinking analysis of β-dystroglycan in dystrophin-deficient skeletal muscle.HRB open research · 2018Article
- Mass spectrometric identification of dystrophin, the protein product of the Duchenne muscular dystrophy gene, in distinct muscle surface membranes.International journal of molecular medicine · 2017Article
- Junctophilin 1 and 2 proteins interact with the L-type Ca2+ channel dihydropyridine receptors (DHPRs) in skeletal muscle.The Journal of biological chemistry · 2011Article
- Multi-minicore disease and atypical periodic paralysis associated with novel mutations in the skeletal muscle ryanodine receptor (RYR1) gene.Neuromuscular disorders : NMD · 2010Article
- Central core disease.Orphanet journal of rare diseases · 2007Review
- The junctional SR protein JP-45 affects the functional expression of the voltage-dependent Ca2+ channel Cav1.1.Journal of cell science · 2006Article
- Role of sustained overexpression of central nervous system IGF-I in the age-dependent decline of mouse excitation-contraction coupling.The Journal of membrane biology · 2006Article
- Novel sarco(endo)plasmic reticulum proteins and calcium homeostasis in striated muscles.Journal of muscle research and cell motility · 2005Review
- Deficiency in Cardiac Dystrophin Affects the Abundance of the $\alpha$ -/ $\beta$ -Dystroglycan Complex.Journal of biomedicine & biotechnology · 2005Article
- Drastic reduction of sarcalumenin in Dp427 (dystrophin of 427 kDa)-deficient fibres indicates that abnormal calcium handling plays a key role in muscular dystrophy.The Biochemical journal · 2004Article
- Two domains in dihydropyridine receptor activate the skeletal muscle Ca(2+) release channel.Biophysical journal · 2001Article
- Brain dystrophin-glycoprotein complex: persistent expression of beta-dystroglycan, impaired oligomerization of Dp71 and up-regulation of utrophins in animal models of muscular dystrophy.BMC cell biology · 2001Article
- Identification of a novel 45 kDa protein (JP-45) from rabbit sarcoplasmic-reticulum junctional-face membrane.The Biochemical journal · 2000Article
- Activation and inhibition of skeletal RyR channels by a part of the skeletal DHPR II-III loop: effects of DHPR Ser687 and FKBP12.Biophysical journal · 1999Article
- Protein-protein interactions in intracellular Ca2+-release channel function.The Biochemical journal · 1999Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
In mature skeletal muscle, excitation-contraction (EC) coupling is thought to be mediated by direct physical interactions between the transverse tubular, voltage-sensing dihydropyridine receptor (DHPR) and the ryanodine receptor (RyR) Ca2+ release channel of the sarcoplasmic reticulum (SR). Although previous attempts at demonstrating interactions between purified RyR and alpha1-DHPR have failed, the cross-linking analysis shown here indicates low-level complex formation between the SR RyR and the junctional alpha1-DHPR. After cross-linking of membranes highly enriched in triads with dithiobis-succinimidyl propionate, distinct complexes of more than 3000 kDa were detected. This agrees with numerous physiological and electron-microscopic findings, as well as co-immunoprecipitation experiments with triad receptors and receptor domain-binding studies. However, a distinct overlap of immunoreactivity between receptors was not observed in crude microsomal preparations, indicating that the triad complex is probably of low abundance. Disulphide-bonded, high-molecular-mass clusters of triadin, the junctional protein proposed to mediate interactions in triads, were confirmed to be linked to the RyR. Calsequestrin and the SR Ca2+-ATPase were not found in cross-linked complexes of the RyR and alpha1-DHPR. Thus, whereas recent studies indicate that the two receptors exhibit temporal differences in their developmental inductions and that receptor interactions are not essential for the formation and maintenance of triads, this study supports the signal transduction hypothesis of direct physical interactions between triad receptors in adult skeletal muscle.
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