ArticleThe Journal of biological chemistry2013
Oxygen-coupled redox regulation of the skeletal muscle ryanodine receptor/Ca2+ release channel (RyR1): sites and nature of oxidative modification.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 50 citations in OpenAlex.
- Antioxidant Defense and Redox Signaling in Elite Soccer Players: Insights into Muscle Function, Recovery, and Training Adaptations.Antioxidants (Basel, Switzerland) · 2025Review
- Physiological role for S-nitrosylation of RyR1 in skeletal muscle function and development.Biochemical and biophysical research communications · 2024Article
- Hydrogen Sulfide (HBiomolecules · 2024Review
- The mediating role of inflammaging between mitochondrial dysfunction and sarcopenia in aging: a review.American journal of clinical and experimental immunology · 2023Review
- A controversial issue: Can mitochondria modulate cytosolic calcium and contraction of skeletal muscle fibers?The Journal of general physiology · 2022Review
- Mitochondrial ROS, ER Stress, and Nrf2 Crosstalk in the Regulation of Mitochondrial Apoptosis Induced by Arsenite.Antioxidants (Basel, Switzerland) · 2022Review
- Biological Aspects of Selected Myokines in Skeletal Muscle: Focus on Aging.International journal of molecular sciences · 2021Review
- Exercise-Stimulated ROS Sensitive Signaling Pathways in Skeletal Muscle.Antioxidants (Basel, Switzerland) · 2021Review
- Redox basis of exercise physiology.Redox biology · 2020Review
- Immunological Techniques to Assess Protein Thiol Redox State: Opportunities, Challenges and Solutions.Antioxidants (Basel, Switzerland) · 2020Review
- The Arianna thread: the matching of S-100 family with the RyR's muscle receptor.European journal of translational myology · 2020Article
- Swimming Exercise Protects against Insulin Resistance via Regulating Oxidative Stress through Nox4 and AKT Signaling in High-Fat Diet-Fed Mice.Journal of diabetes research · 2020Article
- Redox regulation of ER and mitochondrial CaCell calcium · 2019Review
- Excessive Accumulation of CaFrontiers in physiology · 2019Article
- Mass Spectrometry in Advancement of Redox Precision Medicine.Advances in experimental medicine and biology · 2019Review
- Advanced aging causes diaphragm functional abnormalities, global proteome remodeling, and loss of mitochondrial cysteine redox flexibility in mice.Experimental gerontology · 2018Article
- The structural basis of ryanodine receptor ion channel function.The Journal of general physiology · 2017Review
- GSNOR Deficiency Enhances In Situ Skeletal Muscle Strength, Fatigue Resistance, and RyR1 S-Nitrosylation Without Impacting Mitochondrial Content and Activity.Antioxidants & redox signaling · 2017Article
- Review of RyR1 pathway and associated pathomechanisms.Acta neuropathologica communications · 2016Review
- ROS and intracellular ion channels.Cell calcium · 2016Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
In mammalian skeletal muscle, Ca(2+) release from the sarcoplasmic reticulum (SR) through the ryanodine receptor/Ca(2+)-release channel RyR1 can be enhanced by S-oxidation or S-nitrosylation of separate Cys residues, which are allosterically linked. S-Oxidation of RyR1 is coupled to muscle oxygen tension (pO2) through O2-dependent production of hydrogen peroxide by SR-resident NADPH oxidase 4. In isolated SR (SR vesicles), an average of six to eight Cys thiols/RyR1 monomer are reversibly oxidized at high (21% O2) versus low pO2 (1% O2), but their identity among the 100 Cys residues/RyR1 monomer is unknown. Here we use isotope-coded affinity tag labeling and mass spectrometry (yielding 93% coverage of RyR1 Cys residues) to identify 13 Cys residues subject to pO2-coupled S-oxidation in SR vesicles. Eight additional Cys residues are oxidized at high versus low pO2 only when NADPH levels are supplemented to enhance NADPH oxidase 4 activity. pO2-sensitive Cys residues were largely non-overlapping with those identified previously as hyperreactive by administration of exogenous reagents (three of 21) or as S-nitrosylated. Cys residues subject to pO2-coupled oxidation are distributed widely within the cytoplasmic domain of RyR1 in multiple functional domains implicated in RyR1 activity-regulating interactions with the L-type Ca(2+) channel (dihydropyridine receptor) and FK506-binding protein 12 as well as in "hot spot" regions containing sites of mutation implicated in malignant hyperthermia and central core disease. pO2-coupled disulfide formation was identified, whereas neither S-glutathionylated nor sulfenamide-modified Cys residues were observed. Thus, physiological redox regulation of RyR1 by endogenously generated hydrogen peroxide is exerted through dynamic disulfide formation involving multiple Cys residues.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.