Cryo-EM structures of the gating cycle of bestrophin reveal the molecular underpinnings of activation and inactivation gating in this calcium-activated chloride channel and reveal a surprisingly wide pore.

Customization of ion channel gating enhances homeostatic regulation through automatic detection and correction of abnormal physiological changes, as illustrated by self-restoration of excitation rhythm in cardiac arrhythmias.

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.

Contrary to a generally accepted principle, the pore properties of KCNQ1 channels depend on the states of voltage-sensing domains activation; KCNE1 alters the voltage-sensing domains-pore coupling to modulate KCNQ1 channel properties.

The gating polarity of a voltage-gated ion channel is primarily determined by turn propensity of residues at a critical position in the middle of the S4 voltage-sensing helix.

The structure of the mechanosensitive channel MscS embedded in a lipid bilayer redefines the nature, location and importance of lipid–protein interactions in the gating of mechanosensitive channels.

Temperature-activated TRPV1 ion channels respond to increased temperatures by opening and then entering an inactivated state from which they cannot recover, suggesting that this form of irreversible gating results from partial unfolding during heat absorption.

A combined systematic alanine scanning and molecular modelling approach reveals the molecular basis for an allosteric inhibition mechanism of K⁺-flux gating in K_2P channels.

High resolution SthK channel cryo-EM structures in different ligand-bound states combined with single-channel functional data in the same conditions constrain a gating mechanism for CNG channels.

Allosteric gating in a transient receptor potential channel is modulated by external sodium ions and a tarantula toxin.