Calmodulin Binding Proteins

Dear Colleagues,

Hundreds of different proteins bind to and are regulated by the small calcium-binding protein calmodulin (CaM). These calmodulin binding proteins (CaMBPs) serve multiple, critical biomedical functions. Unlike other protein-protein interactions, binding to CaM does not involve a defined amino acid sequence. Instead, it is mediated by a diversity of canonical and non-canonical calcium-dependent binding motifs and a smaller but still variable number of calcium-independent IQ, IQ-like and other binding domains. Despite this variability, CaMBP regulation is tightly controlled and these proteins mediate diverse cellular functions as enzymes, tethers, adaptors, translocators, ion channels, and regulators of calcium signal transduction. As a result, CaMBPs are critical to a multitude of central biological processes, from inflammation to learning, and memory, as well as to a diversity of diseases including Alzheimer’s, cancers and cardiac arrythmias, to name a few. This comprehensive Special Issue “Calmodulin Binding Proteins” brings the complexity of these topics to light, serving not only as an introduction but also as a guide for future research.

Prof. Dr. Danton O'Day
Dr. Robert J. Huber
Guest Editors

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