Behavioral assays using Caenorhabditis elegans show that a learned pathogen avoidance following intestinal distention requires specific chemosensory neurons and TRPM channels in the intestine and excretory cell.

The cooling agent pocket in TRPM8 is conserved in a subset of other TRPM channels and the cooling agent icilin can regulate opening of TRPM4 channels in response to calcium and voltage.

Structure-based alignment of TRP channels enables comparison of structural changes, ion permeation pathways and ligand-binding sites and reveals over-representation of structures that represent non-conducting states.

Newly identified gain-of-function variants indicate TRPM3 as the cause of a spectrum of autosomal dominant neurodevelopmental disorders with frequent cerebellar involvement in humans.

Joint sequence, structure, and phylogenetic analyses identify highly conserved features in transmembrane domains of transient receptor potential (TRP) ion channel proteins that offer a novel explanation for how TRPs could integrate stimuli into cellular signals.

The 3Å structure and correlated functional analysis of the TRPM2 cation channel from Nematostella vectensis shed light on the molecular mechanisms of TRPM2 regulation by intra- and extracellular Ca²⁺, and of inactivation of human TRPM2.

The first comprehensive study on the regulation mechanism of miR-252 and temperature receptor CcTRPM on insect seasonal polyphenism will also conducive to designing a new method for pest control.

A nonspecific cation current mediated by TRPM4 channels is a major contributor to the increase in excitability induced by cholinergic modulation in hippocampal CA1 pyramidal neurons, which are thought to play an important role in episodic memory.

Cryo-EM structure reveals architecture, lipid-binding sites, and ion-conducting pore of the human TRPC3 cation channel.

The TRPV1, TRPV2 and TRPV3 channels are gated on the cytosolic side of the pore, whereas structural changes in the ion selectivity filter associated with activation don't control cation access.