Cytotoxicity associated with APOL1 renal-risk variants occurs through its plasma-membrane localization, where aberrant channel activity drives a sustained sodium and calcium influx leading to cell swelling and eventually cell death.

The structure of a bivalent double-knot tarantula toxin bound to the outer pore of the capsaicin receptor reveals a novel mode of toxin-channel recognition that has important implications for thermosensation.

Computation and experiment together demonstrate that nonspecific membrane–protein interactions could regulate transmembrane protein function and suggest that covalent linkers can be an integral component of the sensing apparatus.

Channel activity is a novel regulatory mechanism for channel mobility in the plasma membrane.

Tension is the activating stimulus of Piezo1 mechanosensitive ion channels and resting membrane tension modulates overall channel sensitivity to mechanical stimulation.

A potassium channel, as a nonconducting function, organizes compartmentalized neuronal calcium signaling microdomains via structural and functional coupling of plasma membrane and endoplasmic reticulum calcium channels.

Combined simulations and electrophysiological experiments show that the CLC channels and exchangers form physically distinct and evolutionarily conserved pathways through which Cl^- and H⁺ ions move when crossing biological membranes.

Structures of a TMEM16 phospholipid scramblase reveal that its Ca²⁺-dependent activation entails global conformational changes and how these rearrangements affect the membrane to enable transbilayer lipid transfer.

Membrane mechanics predict that the ion channel Piezo recruits the surrounding membrane to amplify its sensitivity to changes in membrane tension, with greatest sensitivity in the low-tension regime.

The K(+) uptake system KtrAB is controlled by an allosteric mechanism entirely new for membrane channels, which operates the channel gate over a 35 Å distance.