The notion that the lumen of the ATP synthase membrane rotor is the long-sought megachannel that triggers the onset of the mitochondrial permeability transition is found to be inconsistent with its actual structural and functional properties.

Polymorphic residues of a vacuolar Ca²⁺ sensor site in TPC1 channels differ between species of Brassicacea and Fabaceae and lead to distinct TPC1 gating behavior.

Loss of the F-ATP synthase c-subunit inhibits a pathological mitochondrial permeability transition pore that is coupled to a maladaptive mitochondrial unfolded protein response while also extending lifespan.

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 molecular mechanism that candidalysin uses to perforate membranes is unraveled, which opens the door to the rational design of inhibitors against candidiasis.

A 3.2 Å resolution structure of Vps4 provides a detailed model for protein substrate binding and translocation by AAA ATPases.

Cryo-EM structures of Cys-loop receptor Alpo4 from the thermophilic worm Alvinella pompejana show that a sterol derivative CHAPS binds in and outside of its orthosteric binding site and induces a quaternary twist.

Electron and atomic force microscopy show how bacterial toxins bind to a host membrane and assemble into arcs and rings, before undergoing a dramatic, concerted conformational change to insert into the membrane.

T-cell receptor signaling actively regulates gating of the nuclear pore complex (NPC) in T cells by inducing translocation of protein kinase C-θ to the NPC to promote the sumoylation of RanGAP1.

The conformation of an isoleucine gate located along the TM6 segment on the intracellular side below the selectivity filter is a critical component leading to a non-conductive state in the C-type inactivation process of K⁺ channels.