Calcium activates purified human TRPA1 with and without its N-terminal ankyrin repeat domain in the absence of calmodulin

Research output: Contribution to journalArticle

Abstract

Extracellular influx of calcium or release of calcium from intracellular stores have been shown to activate mammalian TRPA1 as well as to sensitize and desensitize TRPA1 electrophilic activation. Calcium binding sites on both intracellular N- and C-termini have been proposed. Here, we demonstrate based on Förster resonance energy transfer (FRET) and bilayer patch-clamp studies, a direct calmodulin-independent action of calcium on the purified human TRPA1 (hTRPA1), causing structural changes and activation without immediate subsequent desensitization of hTRPA1 with and without its N-terminal ankyrin repeat domain (N-ARD). Thus, calcium alone activates hTRPA1 by a direct interaction with binding sites outside the N-ARD.

Details

Authors
Organisations
External organisations
  • Linköping University
  • Pasteur Institute
  • Institut Fresnel
  • Aix-Marseille University
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Cell and Molecular Biology

Keywords

  • Calcium, Calmodulin, Pain, TRP channel, TRPA1
Original languageEnglish
Article number102228
JournalCell Calcium
Volume90
Publication statusPublished - 2020
Publication categoryResearch
Peer-reviewedYes