Life-threatening arrhythmogenic CaM mutations disrupt CaM binding to a distinct RyR2 CaM-binding pocket

Life-threatening arrhythmogenic CaM mutations disrupt CaM binding to a distinct RyR2 CaM-binding pocket

Calmodulin (CaM) modulates the activity of several proteins that play a key role in excitation-contraction coupling (ECC). In cardiac muscle, the major binding partner of CaM is the type-2 ryanodine receptor (RyR2) and altered CaM binding contributes to defects in sarcoplasmic reticulum (SR) calcium...

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Bibliographic Details
Main Author: Angelos, Thanassoulas (author)
Other Authors: Vassilakopoulou, Vyronia (author), Calver, Brian L. (author), Buntwal, Luke (author), Smith, Adrian (author), Lai, Christopher (author), Kontogianni, Iris (author), Livaniou, Evangelia (author), Nounesis, George (author), Lai, F. Anthony (author), Nomikos, Michail (author)
Format: article
Published: 2023
Subjects:
Calmodulin
Ryanodine receptor
RyR2
Arrhythmias
Cardiac disease
Online Access:http://dx.doi.org/10.1016/j.bbagen.2023.130313
https://www.sciencedirect.com/science/article/pii/S0304416523000119
http://hdl.handle.net/10576/39329
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