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- W2017047805 abstract "In skeletal muscle fibers, local Ca2+ sparks and global Ca2+ transients arise from the synchronous activation of arrays of skeletal ryanodine receptors (RyR1) in the sarcoplasmic reticulum. Marx et al. (1998) first described that synchronous Ca2+ signaling in cells could be explained by the coordinated gating of neighboring RyR1; i.e. coupled gating. We have previously reported that coupled gating of multiple RyR1 requires luminal Ca2+ as current carrier and ATP/Mg2+ in the cytosolic solution. As ATP is the most effective nucleotide for coupled gating in the presence of cytosolic Mg2+, the role of ATP to modulate RyR1 as a substrate of protein kinases to phosphorylate the channel or to stabilize RyR1-RyR1 interactions via the cytoskeleton remains possible. Consequently, we investigate the role of kinases/phosphatases and cytoskeleton modulators (colchicine and cytochalasin D) on RyR-mediated Ca2+ leak from SR microsomes as well as on coupled RyR1. We also investigated role of FKBP12 in coupled RyR1 gating by adding FKBP12 to partially coupled RyR1 or rapamycin to coupled RyR1 in planar lipid bilayers. Our results suggest the RyR1-RyR1 interactions that are essential for coupled gating were not significantly affected by addition of kinases/phosphatases, cytoskeleton modulators or the addition/removal of FKBP12 by rapamycin. Yet, some of the agents affected the overall activity of the RyR1. (Supported by NIH R01 GM078665)." @default.
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- W2017047805 date "2011-02-01" @default.
- W2017047805 modified "2023-10-18" @default.
- W2017047805 title "Effect of Phosphorylation, Cytoskeleton and FK-506 Binding Protein on the Gating of Coupled Skeletal Ryanodine Receptors" @default.
- W2017047805 doi "https://doi.org/10.1016/j.bpj.2010.12.2462" @default.
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