Ion channels articles from across Nature Portfolio

Using HDX-MS and MD simulations, the authors demonstrate that Ca²⁺ and Na⁺ binding to specific domains rigidifies specific structural elements of the NCX protein, revealing regulatory modules and molecular mechanisms governing ion transport rates.

TRAAK, TREK-1 and TREK-2 are mechanosensitive potassium channels involved in action potential propagation among other roles. Here, authors quantify their tension response and show ultrasound can generate tension to activate ion channels.

Multiscale molecular dynamics simulations reveal rapidly exchanging lipid binding sites on the nicotinic acetylcholine receptor, including sites with high affinity for phosphatidic acid and promiscuous cholesterol sites in inter-α-helix grooves.

Pannexins are large pore channels involved in ion and ATP release. Here the authors use cryo-EM structures of Pannexins 1 and 3 to demonstrate the effects of distinct residue substitutions on channel structure and function.

CaV1.2 is crucial in cardiac, vascular and neuronal function, serving as a target for many drugs. Here, authors identify the binding site of herb-derived drug tetrandrine, and explore inhibitory mechanism of L/T-type selective DHP drug benidipine.

The K⁺ ion channel KCNQ2 modulates neuronal excitability and is targeted by retigabine, an anti-epileptic drug that enhances the probability of channel opening. New activators have now been discovered to increase unitary conductance through an unprecedented mechanism.

By drawing inspiration from ion transport in biology, researchers have developed highly selective channels for the separation and enrichment of Li⁺ ions from complex aqueous solutions.

A study analyses the nanotopography of presynaptic calcium channels and release sensors and the degree of their coupling during maturation of an inhibitory synapse.

To activate noncanonical LC3B lipidation and NLRP3 inflammasome formation, stimulator of interferon genes (STING) forms a proton channel in Golgi membranes.

Volume-regulated anion channels (VRACs) are critical for cell volume regulation, neuron–glia interaction, metabolism, and immunity. They are formed as heteromers of LRRC8 proteins with unknown stoichiometry. Two papers now reveal the structures of heteromeric LRRC8A and LRRC8C channels, providing insights into channel assembly and gating.