Key result
Testin physically associates with KCNE2 and nullifies KCNE2's effects on Kv1.5 voltage dependence and gating kinetics in vitro.
Why the study?
A better understanding of the genetic predisposition to CAD and its underlying mechanisms is needed, and novel interaction partners for the CAD-associated potassium channel subunit KCNE2 remained to be identified.
Testin acts as a novel tertiary ion channel regulatory protein by interacting with KCNE2 and modulating its effects on Kv1.5 channels, which may have implications for coronary artery disease and arrhythmias.
Testin may modulate KCNE2-Kv1.5 in animal models; leaves open relevance to human arrhythmias.
Coronary Artery Disease (CAD) typically kills more people globally each year than any other single cause of death. A better understanding of genetic predisposition to CAD and the underlying mechanisms will help to identify those most at risk and contribute to improved therapeutic approaches. KCNE2 is a functionally versatile, ubiquitously expressed potassium channel β subunit associated with CAD and cardiac arrhythmia susceptibility in humans and mice. Here, to identify novel KCNE2 interaction partners, we employed yeast two-hybrid screening of adult and fetal human heart libraries using the KCNE2 intracellular C-terminal domain as bait. Testin (encoded by TES), an endothelial cell-expressed, CAD-associated, focal adhesion protein, was identified as a high-confidence interaction partner for KCNE2. We confirmed physical association between KCNE2 and Testin in vitro by co-immunoprecipitation. Whole-cell patch clamp electrophysiology revealed that KCNE2 negative-shifts the voltage dependence and increases the rate of activation of the endothelial cell and cardiomyocyte-expressed Kv channel α subunit, Kv1.5 in CHO cells, whereas Testin did not alter Kv1.5 function. However, Testin nullified KCNE2 effects on Kv1.5 voltage dependence and gating kinetics. In contrast, Testin did not prevent KCNE2 regulation of KCNQ1 gating. The data identify a novel role for Testin as a tertiary ion channel regulatory protein. Future studies will address the potential role for KCNE2-Testin interactions in arterial and myocyte physiology and CAD.
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Papanikolaou et al. (2021) studied Coronary Artery Disease. Testin was evaluated on Interaction between KCNE2 and Testin and effect on Kv1.5 function. Testin physically associates with KCNE2 and nullifies KCNE2's effects on Kv1.5 voltage dependence and gating kinetics in vitro.
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