Ion transport articles from across Nature Portfolio

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.

Yeast cadmium factor 1 (Ycf1), a heavy metal and glutathione transporter, is regulated by an intrinsically disordered region called the regulatory domain. In this work, the authors show that this domain controls activity through autoinhibition of the glutathione cavity when it is dephosphorylated.

The poison dart toxin batrachotoxin is the most lethal voltage-gated sodium channel toxin. Here authors identify the toxin bound specifically at two homologous receptor sites, which cause channel hyperactivation by positively modulating channel gating and altering ion conductance.

A calcium ion binding site, hidden in the highly conserved gate of the synaptic AMPA-type ionotropic glutamate receptor, reveals upon gating and controls ion transport across the membrane, providing new mechanistic insights on ion permeation.

Inspired by thermal optocapacitive approaches at regulating neuronal activity, the authors explore a photolipid-based non-thermal optocapacitive method that allows for regulating voltage-gated and mechanosensitive ion channels using light.

We report light-gated channels in a fungus-like protist that are highly selective for K⁺ over Na⁺. These microbial rhodopsin channels, named kalium channelrhodopsins, enable robust inhibition of mouse cortical neurons with millisecond precision. In addition, kalium channelrhodopsins reveal a previously unknown potassium selectivity mechanism.

A recent study reports the first high-resolution, cryo-electron microscopy-based structure of zebrafish Na⁺-K⁺-Cl⁻ cotransporter 1 (NKCC1). This structure provides important insights into the determinants of ion translocation by NKCC1 and other cation-Cl⁻ cotransporters such as NKCC2. It could thus facilitate the design of drugs to target these transporters individually.

New structural work sheds light on the architecture of otopetrin channels, offering insights into the mechanisms for proton permeation in this family.

Bacteria sense metal ions using proteins whose interactions with DNA are sensitive to metal ion availability and identity. Less competitive metal ions trigger protein–DNA binding only at high concentrations.