RRC ID 77372
Author Hori S, Tateyama M, Shirai T, Kubo Y, Saitoh O.
Title Two single-point mutations in Ankyrin Repeat one drastically change the threshold temperature of TRPV1.
Journal Nat Commun
Abstract TRPV1 plays an important role in the thermosensory system; however, the mechanism controlling its heat activation property is not well understood. Here, we determine the heat activation properties of TRPV1 cloned from tailed amphibians, which prefer cooler environments, finding the threshold temperatures were approximately 10 °C lower compared with rat TRPV1 (rTRPV1). We find that two amino acid residues (Gln, Leu/Val) in the Ankyrin Repeat 1 (ANK1) region of the N-terminal domain are conserved among tailed amphibians and different from those (Arg, Lys) in rTRPV1. We observe the activation by heat in all urodelan TRPV1s is markedly elevated by substitution of these two amino acids. Conversely, reciprocal substitutions of rTRPV1 apparently lowers the high threshold temperature. Our studies demonstrate that tailed amphibians express TRPV1 with a reduced heat-activation threshold by substitution of two amino acid residues in the ANK1 region that likely contribute to cool-habitat selection.
Volume 14(1)
Pages 2415
Published 2023-5-11
DOI 10.1038/s41467-023-38051-1
PII 10.1038/s41467-023-38051-1
PMID 37169739
PMC PMC10175561
MeSH Amino Acids / genetics Animals Ankyrin Repeat* / genetics Hot Temperature Point Mutation* Rats TRPV Cation Channels / metabolism Temperature
IF 12.121
Clawed frogs / Newts Pleurodeles waltl