TY - JOUR
T1 - TRPA5 encodes a thermosensitive ankyrin ion channel receptor in a triatomine insect
AU - Liénard, Marjorie A.
AU - Baez-Nieto, David
AU - Tsai, Cheng-Chia
AU - Valencia-Montoya, Wendy A.
AU - Werin, Balder
AU - Johanson, Urban
AU - Lassance, Jean-Marc
AU - Pan, Jen Q.
AU - Yu, Nanfang
AU - Pierce, Naomi E.
N1 - © 2024 The Author(s).
PY - 2024/4/19
Y1 - 2024/4/19
N2 - As ectotherms, insects need heat-sensitive receptors to monitor
environmental temperatures and facilitate thermoregulation. We show that
TRPA5, a class of ankyrin transient receptor potential (TRP)
channels absent in dipteran genomes, may function as insect heat
receptors. In the triatomine bug Rhodnius prolixus (order:
Hemiptera), a vector of Chagas disease, the channel RpTRPA5B displays a
uniquely high thermosensitivity, with biophysical determinants including
a large channel activation enthalpy change (72 kcal/mol), a high
temperature coefficient (Q10 = 25), and in vitro temperature-induced currents from 53°C to 68°C (T0.5 =
58.6°C), similar to noxious TRPV receptors in mammals. Monomeric and
tetrameric ion channel structure predictions show reliable parallels
with fruit fly dTRPA1, with structural uniqueness in ankyrin repeat
domains, the channel selectivity filter, and potential TRP functional
modulator regions. Overall, the finding of a member of TRPA5 as a temperature-activated receptor illustrates the diversity of insect molecular heat detectors.
AB - As ectotherms, insects need heat-sensitive receptors to monitor
environmental temperatures and facilitate thermoregulation. We show that
TRPA5, a class of ankyrin transient receptor potential (TRP)
channels absent in dipteran genomes, may function as insect heat
receptors. In the triatomine bug Rhodnius prolixus (order:
Hemiptera), a vector of Chagas disease, the channel RpTRPA5B displays a
uniquely high thermosensitivity, with biophysical determinants including
a large channel activation enthalpy change (72 kcal/mol), a high
temperature coefficient (Q10 = 25), and in vitro temperature-induced currents from 53°C to 68°C (T0.5 =
58.6°C), similar to noxious TRPV receptors in mammals. Monomeric and
tetrameric ion channel structure predictions show reliable parallels
with fruit fly dTRPA1, with structural uniqueness in ankyrin repeat
domains, the channel selectivity filter, and potential TRP functional
modulator regions. Overall, the finding of a member of TRPA5 as a temperature-activated receptor illustrates the diversity of insect molecular heat detectors.
U2 - 10.1016/j.isci.2024.109541
DO - 10.1016/j.isci.2024.109541
M3 - Article
C2 - 38577108
SN - 2589-0042
VL - 27
JO - iScience
JF - iScience
IS - 4
M1 - 109541
ER -