title: Structure of thermally activated TRP channels.
abstract: Temperature sensation is important for adaptation and survival of organisms. While temperature has the potential to affect all biological macromolecules, organisms have evolved specific thermosensitive molecular detectors that are able to transduce temperature changes into physiologically relevant signals. Among these thermosensors are ion channels from the transient receptor potential (TRP) family. Prime candidates include TRPV1-4, TRPA1, and TRPM8 (the so-called "thermoTRP" channels), which are expressed in sensory neurons and gated at specific temperatures. Electrophysiological and thermodynamic approaches have been employed to determine the nature by which thermoTRPs detect temperature and couple temperature changes to channel gating. To further understand how thermoTRPs sense temperature, high-resolution structures of full-length thermoTRPs channels will be required. Here, we will discuss current progress in unraveling the structures of thermoTRP channels.
authors.affiliation: Department of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, OH, USA; Department of Physiology & Biophysics, Case Western Reserve University School of Medicine, Cleveland, OH, USA.
authors.forename: Matthew R
authors.initials: MR
authors.lastname: Cohen
authors.affiliation: Department of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, OH, USA; Department of Physiology & Biophysics, Case Western Reserve University School of Medicine, Cleveland, OH, USA.
authors.forename: Vera Y
authors.initials: VY
authors.lastname: Moiseenkova-Bell
mesh_terms: D000818:Animals; D006801:Humans; D013697:Thermosensing; D050051:Transient Receptor Potential Channels / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D050051:Transient Receptor Potential Channels
keywords: Ankyrin repeats; Cryo-electron microscopy; TRPA1; TRPM8; TRPV1; TRPV2; Thermochannels; X-ray crystallography