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

Moparthi, Lavanya LU ; Moparthi, Satish Babu ; Wenger, Jérôme and Zygmunt, Peter M. LU (2020) In Cell Calcium 90.
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.

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author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Calcium, Calmodulin, Pain, TRP channel, TRPA1
in
Cell Calcium
volume
90
article number
102228
publisher
Elsevier
external identifiers
  • pmid:32554053
  • scopus:85086356873
ISSN
0143-4160
DOI
10.1016/j.ceca.2020.102228
language
English
LU publication?
yes
id
8dc9dc9f-89b5-4f90-a76e-1b0ce768d821
date added to LUP
2020-06-30 08:33:38
date last changed
2020-09-23 08:12:35
@article{8dc9dc9f-89b5-4f90-a76e-1b0ce768d821,
  abstract     = {<p>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.</p>},
  author       = {Moparthi, Lavanya and Moparthi, Satish Babu and Wenger, Jérôme and Zygmunt, Peter M.},
  issn         = {0143-4160},
  language     = {eng},
  publisher    = {Elsevier},
  series       = {Cell Calcium},
  title        = {Calcium activates purified human TRPA1 with and without its N-terminal ankyrin repeat domain in the absence of calmodulin},
  url          = {http://dx.doi.org/10.1016/j.ceca.2020.102228},
  doi          = {10.1016/j.ceca.2020.102228},
  volume       = {90},
  year         = {2020},
}