Multimerization of Homo sapiens TRPA1 ion channel cytoplasmic domains

PloS One
Gilbert Q Martinez, Sharona E Gordon

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 cysteine-reactive natural extracts from onion and garlic which modify residues in the cytoplasmic domains. The way in which TRPA1 cytoplasmic domain modification is coupled to opening of the ion-conducting pore has yet to be elucidated. The cryo-EM structure of TRPA1 revealed a tetrameric C-terminal coiled-coil surrounded by N-terminal ankyrin repeat domains (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 surrounded by N-terminal cytoplasmic domains. This conserved architecture may indicate a common gating mechanism by 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 coiled-coil domains can be expressed in bacteria and maintain the ability to interact. We tested three gating regulators: temperature; the polyphosphate compound IP6; and the covalent modifier allyl isothiocya...Continue Reading

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Citations

Jun 12, 2019·Channels·Ana Elena López-RomeroTamara Rosenbaum

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Methods Mentioned

BETA
size exclusion chromatography
size-exclusion
light scattering
circular dichroism
size-exclusion chromatography
pulled down
X-ray

Software Mentioned

Akta Explorer
ImageJ
excel

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