New details on proteins that help animals sense environmental temperature
The ability to sense environmental temperature, which helps animals move away from sub-optimal locations and find those with ideal temperatures, involves various channels on sensory neurons that open at specific temperature ranges. In research published in FEBS Open Bio, scientists found that one such channel—called the transient receptor potential channel TRPM8—from several salamanders that prefer cooler environments exhibits significantly diminished cold sensitivity compared with TRPM8 from frogs, which prefer warmer climates.
The investigators, who conducted their research at the Nagahama Institute of Bio-Science and Technology, in Japan, found that 8 amino acids at the N-terminus of the TRPM8 protein in the cold-preferring salamanders determines the low temperature sensitivity of the channel. They noted that further work is necessary to understand how these amino acids regulate the cold-induced opening of the TRPM8 channel.
The results provide the first insights into the amino acid–level changes in temperature-sensing channels responsible for tailed amphibians’ diminished cold sensitivity.
“The findings of this research are expected to significantly contribute to elucidating the mechanisms by which the diversity of animals inhabiting various temperature environments on Earth has emerged,” said co–corresponding author Osamu Saitoh, PhD. “This paper presents novel and intriguing findings regarding the characteristic evolutionary adaptation of TRPM8 cold sensitivity in salamanders,” added co–corresponding author Shogo Hori, PhD.
URL upon publication: https://onlinelibrary.wiley.com/doi/10.1002/2211-5463.70227
Additional Information
NOTE: The information contained in this release is protected by copyright. Please include journal attribution in all coverage. For more information or to obtain a PDF of any study, please contact: Sara Henning-Stout, newsroom@wiley.com.
About the Journal
FEBS Open Bio is an open access journal for the rapid publication of research articles across the molecular and cellular life sciences. The journal’s rigorous peer review process focusses on the technical and ethical quality of papers, rather than subjective judgements of significance.
About Wiley
Wiley is a global leader in authoritative content and research intelligence for the advancement of scientific discovery, innovation, and learning. With more than 200 years at the center of the scholarly ecosystem, Wiley combines trusted publishing heritage with AI-powered platforms to transform how knowledge is discovered, accessed, and applied. From individual researchers and students to Fortune 500 R&D teams, Wiley enables the transformation of scientific breakthroughs into real-world impact. From knowledge to impact—Wiley is redefining what's possible in science and learning. Visit us at Wiley.com and Investors.Wiley.com. Follow us on Facebook, X, LinkedIn and Instagram.
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The investigators, who conducted their research at the Nagahama Institute of Bio-Science and Technology, in Japan, found that 8 amino acids at the N-terminus of the TRPM8 protein in the cold-preferring salamanders determines the low temperature sensitivity of the channel. They noted that further work is necessary to understand how these amino acids regulate the cold-induced opening of the TRPM8 channel.
The results provide the first insights into the amino acid–level changes in temperature-sensing channels responsible for tailed amphibians’ diminished cold sensitivity.
“The findings of this research are expected to significantly contribute to elucidating the mechanisms by which the diversity of animals inhabiting various temperature environments on Earth has emerged,” said co–corresponding author Osamu Saitoh, PhD. “This paper presents novel and intriguing findings regarding the characteristic evolutionary adaptation of TRPM8 cold sensitivity in salamanders,” added co–corresponding author Shogo Hori, PhD.
URL upon publication: https://onlinelibrary.wiley.com/doi/10.1002/2211-5463.70227
Additional Information
NOTE: The information contained in this release is protected by copyright. Please include journal attribution in all coverage. For more information or to obtain a PDF of any study, please contact: Sara Henning-Stout, newsroom@wiley.com.
About the Journal
FEBS Open Bio is an open access journal for the rapid publication of research articles across the molecular and cellular life sciences. The journal’s rigorous peer review process focusses on the technical and ethical quality of papers, rather than subjective judgements of significance.
About Wiley
Wiley is a global leader in authoritative content and research intelligence for the advancement of scientific discovery, innovation, and learning. With more than 200 years at the center of the scholarly ecosystem, Wiley combines trusted publishing heritage with AI-powered platforms to transform how knowledge is discovered, accessed, and applied. From individual researchers and students to Fortune 500 R&D teams, Wiley enables the transformation of scientific breakthroughs into real-world impact. From knowledge to impact—Wiley is redefining what's possible in science and learning. Visit us at Wiley.com and Investors.Wiley.com. Follow us on Facebook, X, LinkedIn and Instagram.
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