ArticleThe Biochemical journal2008
Localization of PKA phosphorylation site, Ser(2030), in the three-dimensional structure of cardiac ryanodine receptor.
Article in The Biochemical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 46 citations in OpenAlex.
- Structural and Functional Regulation of RyR2 in Cardiac Calcium Handling and Arrhythmogenesis.Biomedicines · 2026Review
- Phosphorylation of phospholamban promotes SERCA2a activation by dwarf open reading frame (DWORF).Cell calcium · 2024Article
- RyR2/IRBIT regulates insulin gene transcript, insulin content, and secretion in the insulinoma cell line INS-1.Scientific reports · 2022Article
- The crosstalk between cardiomyocyte calcium and inflammasome signaling pathways in atrial fibrillation.Pflugers Archiv : European journal of physiology · 2021Review
- Multisite phosphorylation of the cardiac ryanodine receptor: a random or coordinated event?Pflugers Archiv : European journal of physiology · 2020Review
- Phosphorylation of the ryanodine receptor 2 at serine 2030 is required for a complete β-adrenergic response.The Journal of general physiology · 2019Article
- Dyadic Plasticity in Cardiomyocytes.Frontiers in physiology · 2018Review
- Regulation of sarcoplasmic reticulum CaJournal of molecular and cellular cardiology · 2016Review
- Two potential calmodulin-binding sequences in the ryanodine receptor contribute to a mobile, intra-subunit calmodulin-binding domain.Journal of cell science · 2013Article
- Ligand-dependent conformational changes in the clamp region of the cardiac ryanodine receptor.The Journal of biological chemistry · 2013Article
- Ryanodine receptors are uncoupled from contraction in rat vena cava.Cell calcium · 2013Article
- Structural determination of the phosphorylation domain of the ryanodine receptor.The FEBS journal · 2012Article
- Article
- Ryanodine receptors.Skeletal muscle · 2011Article
- Localization of the dantrolene-binding sequence near the FK506-binding protein-binding site in the three-dimensional structure of the ryanodine receptor.The Journal of biological chemistry · 2011Article
- IP(3) receptors: toward understanding their activation.Cold Spring Harbor perspectives in biology · 2010Review
- Is ryanodine receptor phosphorylation key to the fight or flight response and heart failure?The Journal of clinical investigation · 2010Article
- Protein Kinases as Drug Development Targets for Heart Disease Therapy.Pharmaceuticals (Basel, Switzerland) · 2010Review
- Three-dimensional structure of recombinant type 1 inositol 1,4,5-trisphosphate receptor.The Biochemical journal · 2010Article
- Dynamic, inter-subunit interactions between the N-terminal and central mutation regions of cardiac ryanodine receptor.Journal of cell science · 2010Article
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Authors and funding
8 authors at 2 institutions in 1 country.
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Abstract
PKA (protein kinase A)-dependent phosphorylation of the cardiac Ca2+-release channel/RyR2 (type 2 ryanodine receptor)is believed to directly dissociate FKBP12.6 (12.6 kDa FK506-binding protein) from the channel, causing abnormal channel activation and Ca2+ release. To gain insight into the structural basis of the regulation of RyR2 by PKA, we determined the three-dimensional location of the PKA site Ser2030. GFP (green fluorescent protein) was inserted into RyR2-wt (wild-type RyR2)and RyR2 mutant, A4860G, after Thr2023. The resultant GFP-RyR2 fusion proteins, RyR2T2023-GFP and RyR2(A4860G)T2023-GFP, were expressed in HEK-293 (human embryonic kidney) cells and functionally characterized. Ca2+-release assays revealed that both GFP-RyR2 fusion proteins formed caffeine- and ryanodine-sensitive Ca2+-release channels. Further analyses using[3H]ryanodine binding demonstrated that the insertion of GFPinto RyR2-wt after Thr2023 reduced the sensitivity of the channelto activation by Ca2+ or caffeine. RyR2(A4860G)T2023-GFP was found to be structurally more stable than RyR2T2023-GFP and was subsequently used as a basis for three-dimensional reconstruction. Cryo-electronmicroscopy and single particle image processing of the purified RyR2(A4860G)T2023-GFP protein revealed the location of the inserted GFP, and hence the Ser2030 PKA site in domain 4,a region that may be involved in signal transduction between the transmembrane and cytoplasmic domains. Like the Ser2808 PKA site reported previously, the Ser2030 site is not located close to the FKBP12.6-binding site mapped previously, indicating that neither of these PKA sites is directly involved in FKBP12.6 binding. On the basis of the three-dimensional localizations of a number of residues or regions, a model for the subunit organization in the structure of RyR2 is proposed.
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