Why the study?
Available structural information allows predictions to be made about how disease-causing mutations impact desmosomal protein structure, desmosomal adhesion, and related life-threatening diseases including arrhythmogenic right ventricular cardiomyopathy.
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Design
Graphical review
May inform desmosomal variant interpretation in ARVC; leaves open prospective validation before clinical adoption.
In this graphical review we focus on the structural characteristics of desmosomal proteins, their interactions with each other and with the intermediate filament cytoskeleton. The wealth of structural information that is now available allows predictions to be made about the pathogenic effect of disease-causing mutations. We have selected representative examples of missense mutations that are buried, semi-buried or surface exposed, and demonstrate how such variants could affect the structural fold of desmosomal proteins that are expressed in the heart. We explain how such alterations could compromise desmosomal adhesion, resulting in life threatening diseases including arrhythmogenic right ventricular cardiomyopathy.
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Mohammed et al. (2021) studied this question.
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