Enhancing calstabin binding to ryanodine receptors improves cardiac and skeletal muscle function in heart failure -- Wehrens et al. 102 (27): 9607 Data Supplement - HTML Page - index.htslp -- Proceedings of the National Academy of Sciences

Wehrens et al. 10.1073/pnas.0500353102.

Supporting Information

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Supporting Table 1
Supporting Figure 6

Supporting Figure 6

Fig. 6. Increased calstabin-1 binding to skeletal muscle ryanodine receptor (RyR)1 channels after treatment with JTV519. (A) Binding curves of ³⁵S-labeled calstabin-1 to nonphosphorylated or phosphorylated RyR1 in the presence or absence of JTV519. For comparison, binding curves are shown for calstabin-2 and RyR2. (B) WT RyR2 channels were phosphorylated by protein kinase A (PKA) in the absence or presence of PKI_5-24 and incubated with calstabin-2 (Left) or calstabin-1 (Right) in the presence of JTV519 at the indicated concentrations. Immunoblot shows the amounts of calstabin associated with immunoprecipitated RyR after incubation with the indicated concentrations of JTV519.