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- W2019995649 abstract "The RyR2 Ca release channel is activated by the synthetic domain peptide DPc10, which corresponds to a 36-residue sequence within the channel's central mutation hot-spot region. DPc10 activation is hypothesized to result from the destabilization of a critical intramolecular interaction between the N-terminal and central hot-spot regions of the full-length RyR2, and to thereby mimic the effects of arrhythmogenic mutations on this putative intramolecular interaction controlling channel activation. However, the site of DPc10 binding within the RyR2 3D structure is uncertain, and factors that may modulate binding are undefined. To directly monitor and map DPc10 binding to the RyR2, we attached a FRET acceptor at DPc10's N-terminus. A FRET donor was targeted to the RyR2 cytoplasmic assembly via a fluorescent-labeled FKBP12.6. Addition of the acceptor-labeled DPc10 (30 µM) resulted in a marked decrease in fluorescence of the RyR2-bound FKBP12.6. Fluorescence was partially restored upon FKBP12.6 dissociation from the RyR2, indicating that a major fraction of the total fluorescence decrease was attributable to FRET between FKBP12.6 and DPc10 when bound to the channel. The DPc10 dependence of FRET was similar to the DPc10 dependence of RyR2 activation observed previously in bilayer and ryanodine binding studies (EC50 ∼25 µM), consistent with the likelihood that FRET reflected DPc10 binding at its regulatory site on the RyR2. FRET decreased as a function of increasing Ca (30 nM to 300 µM), suggesting that Ca activation of the RyR2 altered either the affinity of DPc10 binding or its proximity to the FKBP12.6 subunit. We conclude that DPc10 binds to a site on the RyR2 within 10 nm of FKBP12.6. Regulatory interactions and structural changes at this site can be monitored using FRET." @default.
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- W2019995649 date "2011-02-01" @default.
- W2019995649 modified "2023-10-18" @default.
- W2019995649 title "Direct Detection of Domain Peptide Binding to the Cardiac Ryanodine Receptor (RYR2) using FRET" @default.
- W2019995649 doi "https://doi.org/10.1016/j.bpj.2010.12.2453" @default.
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