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The N-terminal Ankyrin Repeat domain is not required for electrophile and heat activation of the purified mosquito TRPA1 receptor

Survery, Sabeen LU ; Moparthi, Lavanya LU ; Kjellbom, Per LU ; Högestätt, Edward D. LU ; Zygmunt, Peter M. LU and Johanson, Urban LU (2016) In Journal of Biological Chemistry 291(52). p.26899-26912
Abstract

Temperature sensors are crucial for animals to optimize living conditions. The temperature response of the ion channel transient receptor potential A1 (TRPA1) is intriguing; some orthologs have been reported to be activated by cold and others by heat, but the molecular mechanisms responsible for its activation remain elusive. Single-channel electrophysiological recordings of heterologously expressed and purified Anopheles gambiae TRPA1 (AgTRPA1), with and without the N-terminal ankyrin repeat domain, demonstrate that both proteins are functional because they responded to the electrophilic compounds allyl isothiocyanate and cinnamaldehyde as well as heat. The proteins' similar intrinsic fluorescence properties and corresponding quenching... (More)

Temperature sensors are crucial for animals to optimize living conditions. The temperature response of the ion channel transient receptor potential A1 (TRPA1) is intriguing; some orthologs have been reported to be activated by cold and others by heat, but the molecular mechanisms responsible for its activation remain elusive. Single-channel electrophysiological recordings of heterologously expressed and purified Anopheles gambiae TRPA1 (AgTRPA1), with and without the N-terminal ankyrin repeat domain, demonstrate that both proteins are functional because they responded to the electrophilic compounds allyl isothiocyanate and cinnamaldehyde as well as heat. The proteins' similar intrinsic fluorescence properties and corresponding quenching when activated by allyl isothiocyanate or heat suggest lipid bilayer-independent conformational changes outside the N-terminal domain. The results show that Ag- TRPA1 is an inherent thermo- and chemoreceptor, and analogous to what has been reported for the human TRPA1 ortholog, the N-terminal domain may tune the response but is not required for the activation by these stimuli.

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
291
issue
52
pages
14 pages
publisher
ASBMB
external identifiers
  • scopus:85007099406
  • wos:000391571400026
ISSN
0021-9258
DOI
10.1074/jbc.M116.743443
language
English
LU publication?
yes
id
1e4f52a2-4c40-4988-9263-340824df0a41
date added to LUP
2017-01-13 07:52:36
date last changed
2017-09-18 11:36:47
@article{1e4f52a2-4c40-4988-9263-340824df0a41,
  abstract     = {<p>Temperature sensors are crucial for animals to optimize living conditions. The temperature response of the ion channel transient receptor potential A1 (TRPA1) is intriguing; some orthologs have been reported to be activated by cold and others by heat, but the molecular mechanisms responsible for its activation remain elusive. Single-channel electrophysiological recordings of heterologously expressed and purified Anopheles gambiae TRPA1 (AgTRPA1), with and without the N-terminal ankyrin repeat domain, demonstrate that both proteins are functional because they responded to the electrophilic compounds allyl isothiocyanate and cinnamaldehyde as well as heat. The proteins' similar intrinsic fluorescence properties and corresponding quenching when activated by allyl isothiocyanate or heat suggest lipid bilayer-independent conformational changes outside the N-terminal domain. The results show that Ag- TRPA1 is an inherent thermo- and chemoreceptor, and analogous to what has been reported for the human TRPA1 ortholog, the N-terminal domain may tune the response but is not required for the activation by these stimuli.</p>},
  author       = {Survery, Sabeen and Moparthi, Lavanya and Kjellbom, Per and Högestätt, Edward D. and Zygmunt, Peter M. and Johanson, Urban},
  issn         = {0021-9258},
  language     = {eng},
  month        = {12},
  number       = {52},
  pages        = {26899--26912},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {The N-terminal Ankyrin Repeat domain is not required for electrophile and heat activation of the purified mosquito TRPA1 receptor},
  url          = {http://dx.doi.org/10.1074/jbc.M116.743443},
  volume       = {291},
  year         = {2016},
}