Development of nanobodies against a model pentameric ligand-gated ion channel demonstrates they can be functionally active as negative or positive allosteric modulators and offers opportunities for future drug development.

Phosphatidylglycerol binding at multiple sites stabilizes the open state relative to the desensitized state of a pentameric ligand-gated ion channel.

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.

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

Ion conduction in the calcium-activated chloride channel TMEM16A is directly regulated by calcium, which binds to a site close to the pore thereby shaping the electrostatics at its intracellular entrance.

Engineered E3 ubiquitin ligases are utilized to elucidate mechanisms underlying ubiquitin regulation of membrane proteins, and to achieve robust post-translational functional knockdown of ion channels.

Allosteric reorganizations of a bacterial channel receptor are mapped along the protein structure, using the site-directed bimane quenching fluorescence technique, through parallel real-time conformational and electrophysiological recordings.

The auxiliary protein Stargazin limits the conformational dynamics of AMPA-type glutamate receptors in cell membranes, as revealed by 'molecular rulers' deployed on the seconds to milliseconds timescale.

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.

Single-particle cryo-EM and electrophysiology studies of the chloride channel TMEM16A reveals the structural basis for anion conduction and uncover its relationship to lipid scramblases of the same family.