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- W2913403841 abstract "The transient receptor potential Ankyrin-1 (TRPA1) ion channel is modulated by myriad noxious stimuli that interact with multiple regions of the channel, including the cytoplasmic N-terminal Ankyrin repeat domains (ARDs) via covalent modification. The way in which TRPA1 cytoplasmic domain modification is transmitted across large spatial distances to open the channel pore has yet to be elucidated. The cryo-EM structure of TRPA1 revealed a tetrameric C-terminal coiled-coil (CC) surrounded by the ARDs, an architecture shared with the canonical transient receptor potential (TRPC) ion channel family. Similarly, structures of the TRP melastatin (TRPM) ion channel family also showed a C-terminal coiled-coil enclosed by N-terminal cytoplasmic domains. This conserved architecture may indicate a common gating mechanism in which modification of cytoplasmic domains can transduce conformational changes to open the ion-conducting pore. We developed an in vitro system in which N-terminal ARDs and C-terminal CC domains can be expressed in bacteria and maintain the ability to interact. We tested whether temperature, the polyphosphate compound IP6, and the covalent modifier allyl isothiocyanate alters N- and C-terminal interactions. We found that none of the modifications tested altered ARD-CC interactions. We found that CCs tetramerize in a concentration dependent manner, with monomers and trimers observed at lower concentrations. Although we did not observe ligand- or temperature-dependent disruption of ARD-CC interactions, our system provides a method for examining the mechanism of oligomerization of TRPA1 cytoplasmic domains." @default.
- W2913403841 created "2019-02-21" @default.
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- W2913403841 date "2019-02-01" @default.
- W2913403841 modified "2023-09-30" @default.
- W2913403841 title "Multimerization of Human TRPA1 Ion Channel Cytoplasmic Domains" @default.
- W2913403841 doi "https://doi.org/10.1016/j.bpj.2018.11.2436" @default.
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