CAMTA transcription factors are evolutionarily conserved regulators of neuronal levels of the major Ca²⁺ sensor calmodulin.

Cryo-EM structures reveal how the canonical TRPC4 cation channel is regulated by calmodulin, and how it is modulated by pyridazinone-based inhibitors.

The pseudokinase-like Legionella effector SidJ catalyzes the glutamylation of bacterial ubiquitin ligases in a calmodulin-dependent manner.

NHE1-CaM complexes of multiple stoichiometries regulate cellular Ca²⁺-dependent NHE1 activity and can contribute to NHE1 dimerization, the latter shown by the NMR structure of CaM linking two NHE1 cytosolic tails.

IQ domain phosphorylation regulates calmodulin binding and myosin-1 function.

The ability of calcium waves to exert different effects on calcineurin activity depending on subcellular location is mediated by the distribution of calmodulin.

Calcium drives interactions for both calcium-binding domains of calmodulin in complex with KCa2.1 peptides and both domains are required for normal channel function.

Calmodulin mediates in the protective augmentation of K_V7-currents in response to oxidative stress in a calcium-dependent manner by an unconventional signaling mechanism.

The Ca²⁺-driven functional coupling of CaV1.2 channels is a mechanism of channel memory that may modulate the amplification of Ca²⁺ influx.

The multipronged chemical biology approach unraveled a novel mechanism by which mTOR is regulated by the second messenger calcium.