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Cryo-EM structure of human TMEM120A reveals that it is a coenzyme A-binding protein and is unlikely to function as a mechanosensitive channel as was recently proposed.

A functional link between representative family members of the CLCA channel regulator family and TMEM16 channels suggests that these protein families may cooperate in influencing multiple homeostatic and disease physiologies.

Electrophysiological and structural characterizations reveal that a previously proposed ion channel responsible for sensing mechanical pain is insensitive to poking or stretching stimuli for conducting ions and may serve as a coenzyme A-binding protein instead.

The amino acids that are necessary for phospholipid scrambling by ANO6/TMEM16F can, via domain swapping, confer scrambling activity to the chloride ion channel ANO1 that normally does not scramble phospholipids.

Structures of OSCA1.2, a member of a newly characterized family of mechanically activated ion channels, provide insights into mechanism of channel gating by membrane tension.

SOM⁺ GABAergic neuronal signaling and inhibitory transmission in the central lateral amygdala is regulated by TMEM16B, which is also involved in fear and anxiety-like behaviors.

cryo-EM reveals the properties of distinct conformations occupied during activation of the lipid scramblase nhTMEM16 and provides new insights into its interactions with the lipid environment.

A cryo-EM structure of TMEM87A unexpectedly reveals it is structurally related to seven other proteins including Wntless, a chaperone for lipidated and secreted Wnt morphogens, suggesting GOLD-domain seven-transmembrane helix (GOST) proteins may all similarly traffic membrane-associated cargo.

Ano1 deletion disrupts Ca²⁺ waves within Kölliker’s organ, reduces burst-firing activity and frequency selectivity of auditory brainstem neurons in the medial nucleus of the trapezoid body, and impairs the functional refinement of its projections to the lateral superior olive.

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.