AI Article Synopsis
- Recent discoveries reveal that dyad structures and functions are more diverse than previously understood, with variations in size and orientation of ryanodine receptor clusters.
- The connection between Ca(v)1.2 and RYR2 isn't always present, leading to different scenarios where dyads might lack couplons or have incomplete couplon associations.
- Proteins like junctophilin-2 and calsequestrin are crucial for maintaining dyad integrity, providing new insights into heart diseases like arrhythmias and heart failure.
Article Abstract
This review highlights recent and ongoing discoveries that are transforming the previously held view of dyad structure and function. New data show that dyads vary greatly in both structure and in their associated molecules. Dyads can contain varying numbers of type 2 ryanodine receptor (RYR2) clusters that range in size from one to hundreds of tetramers and they can adopt numerous orientations other than the expected checkerboard. The association of Ca(v)1.2 with RYR2, which defines the couplon, is not absolute, leading to a number of scenarios such as dyads without couplons and those in which only a fraction of the clusters are in couplons. Different dyads also vary in the transporters and exchangers with which they are associated producing functional differences that amplify their structural diversity. The essential role of proteins, such as junctophilin-2, calsequestrin, triadin, and junctin that maintain both the functional and structural integrity of the dyad have recently been elucidated giving a new mechanistic understanding of heart diseases, such as arrhythmias, hypertension, failure, and sudden cardiac death.
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| http://dx.doi.org/10.1093/cvr/cvt025 | DOI Listing |
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