期刊
ANNUAL REVIEW OF BIOPHYSICS, VOL 45
卷 45, 期 -, 页码 371-398出版社
ANNUAL REVIEWS
DOI: 10.1146/annurev-biophys-062215-011034
关键词
gating models; temperature sensor; thermodynamics; heat activation pathways; ligand binding; phosphatidylinositol 4,5-bisphosphate
类别
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.
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