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Article

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

Biochimica et biophysica acta. General subjects - 1 Apr 2023

Thanassoulas Angelos, Vassilakopoulou Vyronia, Calver Brian L, Buntwal Luke, Smith Adrian, Lai Christopher, Kontogianni Iris, Livaniou Evangelia, Nounesis George, Lai F Anthony, Nomikos Michail

Abstract excerpt

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 (Ca2+) release. Many genetic studies have reported a series of CaM missense mutations in patients with a history of...

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PMID: 36693454
DOI: 10.1016/j.bbagen.2023.130313

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

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