Cyclic nucleotide-gated cation channels articles from across Nature Portfolio

Voltage sensing of ion channels relies on charged transmembrane helices. Here authors use live-cell FLIM-FRET and nonsense suppression-mediated fluorescence labeling to reveal that voltage sensors undergo direct modulation by compartmentalized membrane domains.

Hu et al. present eight cryo-EM structures of the human cone photoreceptor CNGA3/CNGB3 channel in the closed, intermediate, pre-open and open states, all fully bound with cGMP. These structures provide an unprecedented view of the conformational trajectory of CNG channel activation.

Visualizing conformational changes during ion channel gating is crucial to understand their regulation. Here, Gao et al. capture multiple gating intermediates in a CNG channel as well as subtle, lateral voltage sensor movements necessary for channel opening.

A cryo-EM structure of the human cone photoreceptor CNG channel reveals an odd subunit stoichiometry and unique structural features conferred by a distinct subunit, providing a framework to study cone CNG channel physiology and channelopathies.

NaK is a bacterial non-selective cation channel. Here, the authors use solution NMR to show that selectivity filter (SF) in NaK is dynamic, with structural differences between the Na+ and K + -bound states. The conformation of the SF is communicated to the pore-lining helices similarly as in the K + -selective channels.

Retinal photoreceptor cyclic nucleotide-gated (CNG) ion channels convert light signals to electrical signals in the eye. Their structures have been solved at ~3 Å resolution by cryo-EM; the asymmetric subunit assembly of heteromeric CNG channels produces a unique ion-permeation pathway with an unusual gating apparatus that indicates distinct subunit contributions for ligand-dependent channel activation.