The atomic structure of GtACR1 provides new insight into the chemical mechanism of natural light-gated anion membrane conductance, and enables its optimization for optogenetic photoinhibition of neuron firing.

The homomeric structure of human SWELL1 (LRRC8A) provides insights into properties of a novel chloride channel family.

Members of UAW 5810—the union for postdoctoral researchers at the University of California—describe how their union has led to improved terms and conditions for postdocs.

Identification of Cl⁻-induced folding advances the field’s understanding of prestin’s unique voltage-sensing mechanism and its involvement in mammalian hearing sensation.

Novel evidence on the molecular determinants of the dual function, anion permeation and substrate transport, of excitatory amino acid transporters opens avenues toward illuminating how these transporters regulate synaptic function and contribute to neurological conditions.

Asp234 is deprotonated in the ground state and forms the proton transfer pathway that proceeds from the Schiff base toward Glu68 in the intermediate state of the anion channelrhodopsin GtACR1.

The structural and functional characterization of SLC26A6 provides greater understanding of coupled versus uncoupled transport processes for the SLC26 transporter family.

S-type anion channel activity, which promotes stomatal closure and improves anti-fungal immunity in plants, is directly regulated through phosphorylation by a kinase of the chitin receptor complex.

In the extremely selective fluoride channels from the bacterial Fluc family, fluoride ions access the pore via two points, an electropositive vestibule and a triad of conserved residues involved in anion recognition.

Substrate-induced structural changes in GtACR1 provide new insight into the chemical mechanism of natural light-gated anion conductance and facilitate its optimization for photoinhibition of neuron firing in optogenetics.