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- W3004625211 abstract "TRPM8 is a polymodally regulated ion channel that is sensitive to diverse stimuli, including chemical ligands, such as menthol, and cold. The function of TRPM8 requires the signaling lipid PIP2 to potentiate the channel. PIRT, an ion channel modulatory protein, directly interacts with both PIP2 and TRPM8 to modulate its function. In an effort to understand the molecular mechanism of PIRT regulation of TRPM8, we have performed NMR and microscale thermophoresis studies to show that there is a competitive interaction between PIRT, TRPM8, and PIP2. We further have determined the solution NMR structure of human PIRT and generated structure-based comparative models of human TRPM8. Leveraging the structural data with chimeric TRPM8-based electrophysiology studies, we can piece together the architecture of the ternary TRPM8-PIRT-PIP2 complex using an integrative approach. Together these data suggest how TRPM8 function is modulated by interactions with PIRT." @default.
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- W3004625211 date "2020-02-01" @default.
- W3004625211 modified "2023-10-16" @default.
- W3004625211 title "Mechanistic and Structural Studies of PIRT Regulation of TRPM8" @default.
- W3004625211 doi "https://doi.org/10.1016/j.bpj.2019.11.2338" @default.
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