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- W2783227455 abstract "The capsaicin receptor, TRPV1, is regulated by phosphatidylinositol-4,5-bisphosphate (PIP2), although the precise nature of this effect (i.e., positive or negative) remains controversial. Here, we reconstitute purified TRPV1 into artificial liposomes, where it retains sensitivity to capsaicin, protons, spider toxins, and heat. Moreover, TRPV1 is fully functional in the absence of any phosphoinositides, arguing against an obligatory role in channel activation. Introduction of various phosphoinositides, including PIP2, PI4P and PI, inhibits chemical and thermal sensitivity of the channel, consistent with a model in which phosphoinositide metabolism by pro-algesic agents enhances TRPV1 sensitivity and contributes to thermal hyperalgesia. using an orthogonal chemical modification strategy, we further show that association of the TRPV1 C-terminus with the bilayer modulates channel gating, consistent with phylogenetic data implicating this region of the channel as a regulatory site for thermal and chemical sensitivity. Beyond TRPV1, these findings are relevant to understanding how membrane lipids modulate a diverse family of “receptor-operated” TRP channels." @default.
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- W2783227455 date "2013-01-01" @default.
- W2783227455 modified "2023-09-30" @default.
- W2783227455 title "TRPV1 Channels are Intrinsically Heat Sensitive and Negatively Regulated by Phosphoinositide Lipids" @default.
- W2783227455 doi "https://doi.org/10.1016/j.bpj.2012.11.2105" @default.
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