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- W1972925672 abstract "ThermoTRP channels sense ambient temperature and function as thermosensor, however, the mechanism for sensitive temperature-dependent activation remains unknown. Recent studies point to the outer pore region as an important gating structure. Our previous study shows pore turret moves substantially during temperature-driven activation, which isn’t seen during capsaicin-driven activation. Present research focuses on contribution of pore turret to heat-induced activation using a structural perturbation approach. Partial deletions and sequence replacements are performed with TRPV1 turret. Additionally, the turret is swamped between TRPV1 and TRPV2/TRPV3. All mutant channels exhibit similar capsaicin sensitivity to wildtype TRPV1 with a less than 10-fold shift in EC50, which is consistent with the notion that temperature and ligand activate TRPV1 through different pathways. In contrast, deletion and replacement mutants exhibit activation at a very different temperature, show rapid inactivation during heating, or lose temperature response. Interestingly, TRPV1 chimera containing TRPV3 turret V1/3S behaves like wildtype TRPV3 and activates at a much lower temperature, while TRPV1 chimera containing TRPV2 turret V1/2S activates at a much higher temperature like wildtype TRPV2. These results reveal that pore turret is a portable domain contributing to temperature sensing." @default.
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- W1972925672 date "2011-02-01" @default.
- W1972925672 modified "2023-09-29" @default.
- W1972925672 title "The Pore Turret of ThermoTRP Channels is a Portable Domain Contributing to Temperature Sensing" @default.
- W1972925672 doi "https://doi.org/10.1016/j.bpj.2010.12.3043" @default.
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