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.

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.

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.

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.

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.

Ligand-induced two-fold symmetric arrangement in TRPV2 is observed in the native-like nanodisc-reconstituted condition using cryo-electron microscopy.

Two domains of the peripheral membrane protein Tim44 interact with two different sectors of a translocase to coordinate the translocation of proteins across the inner mitochondrial membrane.

A new synaptic scaffold important for neurotransmission and synaptic plasticity has been identified.