Single-molecule measurement of conformational dynamics using a genetically encoded fluorescent probe suggests that the selectivity filter region of TRPV1 channels undergoes dynamic motion during agonist activation.
An atomic model of the 3744-residue Tra1 protein reveals multiple transcription activator binding sites, its integration within the SAGA chromatin coactivator complex, and a striking similarity to DNA-repair factor DNA-PKcs.
Novel capsaicin analogs with conserved chemistry but varying sizes were used as molecular rulers to investigate energetics of conformational changes in the ligand-binding pocket and mechanisms of TRPV1 ligand-gating.
The activation and membrane localization of the broadly-tuned noxious chemosensory cation channel TRPA1 are regulated by direct interactions with cholesterol via CRAC motifs in transmembane segments 2 and 4.
A pain-relaying ion channel on a hypersensitive population of sensory neurons can instead elicit sensations of itch in both fish and mice when directly activated, providing a novel model of itch transduction.