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- W2944544356 abstract "Ryanodine receptors (RyRs) are intracellular Ca2+ release channels controlling essential cellular functions. RyRs are targeted by cyclic AMP (cAMP)-dependent protein kinase A (PKA), a controversial regulation implicated in disorders ranging from heart failure to Alzheimer’s. Using crystal structures, we show that the phosphorylation hotspot domain of RyR2 embraces the PKA catalytic subunit, with an extensive interface not seen in PKA complexes with peptides. We trapped an intermediary open-form PKA bound to the RyR2 domain and an ATP analog, showing that PKA can engage substrates in an open form. Phosphomimetics or prior phosphorylation at nearby sites in RyR2 either enhance or reduce the activity of PKA. Finally, we show that a phosphomimetic at S2813, a well-known target site for calmodulin-dependent kinase II, induces the formation of an alpha helix in the phosphorylation domain, resulting in increased interactions and PKA activity. This shows that the different phosphorylation sites in RyR2 are not independent." @default.
- W2944544356 created "2019-05-16" @default.
- W2944544356 creator A5079772694 @default.
- W2944544356 creator A5081117863 @default.
- W2944544356 creator A5085675550 @default.
- W2944544356 date "2019-07-01" @default.
- W2944544356 modified "2023-09-26" @default.
- W2944544356 title "The Cardiac Ryanodine Receptor Phosphorylation Hotspot Embraces PKA in a Phosphorylation-Dependent Manner" @default.
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- W2944544356 doi "https://doi.org/10.1016/j.molcel.2019.04.019" @default.
- W2944544356 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31078384" @default.
- W2944544356 hasPublicationYear "2019" @default.