A new mechanism of receptor desensitization is revealed for the novel proton-activated chloride channel, which plays an important role in physiology and disease associated with acidic pH.

PIP₂ inhibits the proton-activated chloride (PAC) channel by selectively stabilizing its desensitized state.

A viral heliorhodopsin from Emiliania huxleyi virus 202 (V2HeR3) is a light-activated proton transporter, which has the potential to depolarize the host cells by light, possibly to overcome the host defense mechanisms or to prevent superinfection.

The H+ influx coupled to nutrient uptake and the plasma membrane H+-ATPase are central actors of the activation of target of rapamycin complex 1 (TORC1) in budding yeast Saccharomyces cerevisiae..

Electrophysiological and computational techniques provide a structural basis for understanding the conformational changes that are required to activate Hv1 proton channels.

Members of the OTOP family of proton-selective ion channels, which includes the sour receptor OTOP1, are differentially sensitive to activation by zinc, which interacts with residues on tm 5-6 and 11-12 linkers that form part of the channel gating apparatus.

The lysosomal ion channel TPC2 emerges as an example of an ion channel in which ion selectivity is not fixed but rather agonist-selective.

The sour receptor, OTOP1, and related proton channel OTOP3 are steeply activated by extracellular protons while OTOP2 is active over a broad pH range and differences in gating are partly attributed to extracellular domains.

TMEM206 proteins are identified as constituting the pore of the widely expressed acid-activated chloride channel PAORAC/ASOR, which is important in acid toxicity.

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.