ArticleProceedings of the National Academy of Sciences of the United States of America2016
Low-cost functional plasticity of TRPV1 supports heat tolerance in squirrels and camels.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed.
- Cold-gated potentiation of mechanotransduction supports touch sensation below 5°C in a mammalian hibernator.Current biology : CB · 2026Article
- Sensing Underwater: Diversifying Selection, Convergent Evolution and Inactivation in Sensory Receptors' Genes of Aquatic Mammals.Journal of molecular evolution · 2026Article
- Turtle's sex feels the heat.Science bulletin · 2026Article
- Understanding animal temperature sensation: from molecular thermosensors to physiological impacts.Science China. Life sciences · 2026Review
- Temperature-induced structural changes in thermosensitive transient receptor potential channels (thermoTRPs).Frontiers in molecular neuroscience · 2026Review
- Comparing cryo-EM methods and molecular dynamics simulation to investigate heterogeneity in ligand-bound TRPV1.Nature communications · 2025Article
- Pathway-dependent cold activation of heat-responsive TRPV channels.Scientific reports · 2025Article
- Physiological functions and pharmacological targeting of transient receptor potential channels.Pharmacological reviews · 2025Review
- Article
- Human TRPV1 is an efficient thermogenetic actuator for chronic neuromodulation.Cellular and molecular life sciences : CMLS · 2024Article
- Tetherless Optical Neuromodulation: Wavelength from Orange-red to Mid-infrared.Neuroscience bulletin · 2024Review
- Association between Variants of the TRPV1 Gene and Body Composition in Sub-Saharan Africans.Genes · 2024Article
- Implications of a temperature-dependent heat capacity for temperature-gated ion channels.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Genetic Diversity of a Heat Activated Channel-TRPV1 in Two Desert Gerbil Species with Different Heat Sensitivity.International journal of molecular sciences · 2023Article
- "ThermoTRP" Channel Expression in Cancers: Implications for Diagnosis and Prognosis (Practical Approach by a Pathologist).International journal of molecular sciences · 2023Review
- Two single-point mutations in Ankyrin Repeat one drastically change the threshold temperature of TRPV1.Nature communications · 2023Article
- Human TRPV1 structure and inhibition by the analgesic SB-366791.Nature communications · 2023Article
- Mutagenesis studies of TRPV1 subunit interfaces informed by genomic variant analysis.Biophysical journal · 2023Article
- Progress in the Structural Basis of thermoTRP Channel Polymodal Gating.International journal of molecular sciences · 2023Review
- A molecular perspective on identifying TRPV1 thermosensitive regions and disentangling polymodal activation.Temperature (Austin, Tex.) · 2023Review
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Authors and funding
5 authors.
Funding
Abstract
The ability to sense heat is crucial for survival. Increased heat tolerance may prove beneficial by conferring the ability to inhabit otherwise prohibitive ecological niches. This phenomenon is widespread and is found in both large and small animals. For example, ground squirrels and camels can tolerate temperatures more than 40 °C better than many other mammalian species, yet a molecular mechanism subserving this ability is unclear. Transient receptor potential vanilloid 1 (TRPV1) is a polymodal ion channel involved in the detection of noxious thermal and chemical stimuli by primary afferents of the somatosensory system. Here, we show that thirteen-lined ground squirrels (Ictidomys tridecemlineatus) and Bactrian camels (Camelus ferus) express TRPV1 orthologs with dramatically reduced temperature sensitivity. The loss of sensitivity is restricted to temperature and does not affect capsaicin or acid responses, thereby maintaining a role for TRPV1 as a detector of noxious chemical cues. We show that heat sensitivity can be reengineered in both TRPV1 orthologs by a single amino acid substitution in the N-terminal ankyrin-repeat domain. Conversely, reciprocal mutations suppress heat sensitivity of rat TRPV1, supporting functional conservation of the residues. Our studies suggest that squirrels and camels co-opt a common molecular strategy to adapt to hot environments by suppressing the efficiency of TRPV1-mediated heat detection at the level of somatosensory neurons. Such adaptation is possible because of the remarkable functional flexibility of the TRPV1 molecule, which can undergo profound tuning at the minimal cost of a single amino acid change.
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