Two structurally-unrelated regulatory proteins utilize parallel molecular mechanisms to selectively tune calcium and calmodulin feedback of calcium and sodium ion channels and reveals a novel strategy to engineer synthetic channel modulators.

Ca_V1.3 channels of the short isoform are coupled via their C-terminal domains in a Ca²⁺-CaM-dependent manner, which facilitates Ca²⁺ influx and increases the discharge of hippocampal neurons.

The 3Å structure and correlated functional analysis of the TRPM2 cation channel from Nematostella vectensis shed light on the molecular mechanisms of TRPM2 regulation by intra- and extracellular Ca²⁺, and of inactivation of human TRPM2.

Drosophila nociceptive neurons convert high-intensity stimuli into characteristic fluctuations of firing rates, quiescent periods of which are regulated by hyperpolarization through small conductance Ca²⁺-activated K⁺ channels.

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

C-terminus mediated inhibition is one emerging modality of intervention for L-type Ca²⁺ channels, which coordinate multiple motifs to acutely tune Ca²⁺ current and Ca²⁺ influx down to the lower limits preset by end-stage Ca²⁺-dependent inactivation.

Channel activity is a novel regulatory mechanism for channel mobility in the plasma membrane.

A newly characterized calcium-activated chloride channel has been implicated in the immune system of Drosophila, shedding light on an enigmatic family of transmembrane proteins that are ubiquitous in nature.

Polyunsaturated fatty acid analogues show selectivity for different cardiac ion channels, suggesting their potential use for the treatment of different subtypes of Long QT Syndrome.

Super-resolution imaging reveals a novel multi-channel arrangement that explains how big potassium (BK) channel activation closely tracks the opening of low-voltage-activated L-type calcium channels.