Allosterism and Structure in Thermally Activated Transient Receptor Potential Channels

Ignacio Diaz-Franulic, Horacio Poblete, Germán Miño-Galaz, Carlos González, Ramón Latorre

Research output: Contribution to journalArticlepeer-review

46 Citations (Scopus)


The molecular sensors that mediate temperature changes in living organisms are a large family of proteins known as thermosensitive transient receptor potential (TRP) ion channels. These membrane proteins are polymodal receptors that can be activated by cold or hot temperatures, depending on the channel subtype, voltage, and ligands. The stimuli sensors are allosterically coupled to a pore domain, increasing the probability of finding the channel in its ion conductive conformation. In this review we first discuss the allosteric coupling between the temperature and voltage sensor modules and the pore domain, and then discuss the thermodynamic foundations of thermo-TRP channel activation. We provide a structural overview of the molecular determinants of temperature sensing. We also posit an anisotropic thermal diffusion model that may explain the large temperature sensitivity of TRP channels. Additionally, we examine the effect of several ligands on TRP channel function and the evidence regarding their mechanisms of action.

Original languageEnglish
Pages (from-to)371-398
Number of pages28
JournalAnnual Review of Biophysics
Publication statusPublished - 5 Jul 2016


  • gating models
  • heat activation pathways
  • ligand binding
  • phosphatidylinositol 4,5-bisphosphate
  • temperature sensor
  • thermodynamics

ASJC Scopus subject areas

  • Bioengineering
  • Structural Biology
  • Biophysics
  • General Medicine
  • Biochemistry
  • Cell Biology


Dive into the research topics of 'Allosterism and Structure in Thermally Activated Transient Receptor Potential Channels'. Together they form a unique fingerprint.

Cite this