Key result
Recent high-resolution structures of Ryanodine Receptors provide novel insights into the controversial functional role and regulation of their interaction with FK506-binding proteins in the heart.
This review synthesizes recent structural and functional data to clarify the controversial regulatory role of FKBPs on cardiac Ryanodine Receptors.
Ryanodine Receptors (RyRs) are intracellular Ca2+ channels that mediate Ca2+ flux from the sarco(endo)plasmic reticulum in many cell types. The interaction of RyRs with FK506-binding proteins (FKBPs) has been proposed as an important regulatory mechanism, where the loss of this interaction leads to channel dysfunction. In the heart, phosphorylation of RyR has been suggested to disrupt the RyR-FKBP interaction promoting altered Ca2+ signaling, heart failure and arrhythmias. However, the functional result of FKBP interaction with RyR and how this interaction is regulated remains highly controversial. Recently, high resolution structures of RyR have provided novel aspects to the ongoing debate. This review will discuss the most recent functional data in light of these new structures.
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Gonano et al. (2017) conducted a review in Heart failure and arrhythmias. Recent high-resolution structures of Ryanodine Receptors provide novel insights into the controversial functional role and regulation of their interaction with FK506-binding proteins in the heart.
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