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TRPA5 encodes a thermosensitive ankyrin ion channel receptor in a triatomine insect

Liénard, Marjorie A. (author)
Lund University,Lunds universitet,Biologiska institutionen,Naturvetenskapliga fakulteten,Department of Biology,Faculty of Science,Harvard University,Broad Institute
Baez-Nieto, David (author)
Broad Institute
Tsai, Cheng-Chia (author)
Columbia University
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Valencia-Montoya, Wendy A. (author)
Harvard University
Werin, Balder (author)
Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
Johanson, Urban (author)
Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
Lassance, Jean-Marc (author)
Harvard University,University of Liège
Pan, Jen Q. (author)
Broad Institute
Yu, Nanfang (author)
Columbia University
Pierce, Naomi E. (author)
Harvard University
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 (creator_code:org_t)
2024
2024
English 25 s.
In: iScience. - 2589-0042. ; 27:4
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • 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.

Subject headings

NATURVETENSKAP  -- Biologi -- Zoologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Zoology (hsv//eng)
NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)

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