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Related Concept Videos

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Peripheral thermosensation is the perception of external temperature. A change in temperature (on the surface of the skin and other tissues) is detected by a family of temperature-sensitive ion channels called Transient Receptor Potential, or TRP, receptors. These receptors are located on free nerve endings. Those detecting cold temperatures are closer to the surface of the skin than the nerve endings detecting warmth. These thermoTRP channels, while temperature selective, have relatively...
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GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
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The relative difference in electrical charge, or voltage, between the inside and the outside of a cell membrane, is called the membrane potential. It is generated by differences in permeability of the membrane to various ions and the concentrations of these ions across the membrane.
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Related Experiment Video

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A Simple and Inexpensive Method for Determining Cold Sensitivity and Adaptation in Mice
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Structural Basis of Cold and Menthol Sensing by TRPM8.

Hyuk-Joon Lee1, Cheon-Gyu Park1, Justin Gerald Fedor1

  • 1Department of Biochemistry, Duke University School of Medicine, Durham, North Carolina, 27710, USA.

Biorxiv : the Preprint Server for Biology
|September 18, 2025
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Summary

Researchers uncovered how the TRPM8 channel senses cold and menthol. Structural and functional studies reveal distinct activation pathways for cold and menthol, explaining cool sensation mechanisms.

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Area of Science:

  • Molecular Biology
  • Neuroscience
  • Structural Biology

Background:

  • The transient receptor potential melastatin member 8 (TRPM8) is a key ion channel responsible for detecting cold and menthol stimuli in mammals.
  • Previous structural research has not fully elucidated the precise mechanisms of TRPM8 activation by cold and menthol.

Purpose of the Study:

  • To determine the molecular mechanisms underlying cold and menthol activation of the TRPM8 channel.
  • To elucidate how TRPM8 integrates multiple sensory modalities.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to capture structural snapshots of TRPM8 during activation.
  • Extensive functional analyses to correlate structural findings with channel activity.

Main Results:

  • Cryo-EM structures revealed distinct pore rearrangements during cooling-induced activation, providing insight into cold sensing.
  • Dynamic menthol binding was observed, suggesting a mechanism for menthol's specific activation of TRPM8.
  • Overlapping yet non-identical pathways for cold and menthol activation were identified, highlighting a temperature-specific "cold spot".

Conclusions:

  • TRPM8 activation by cold involves significant pore rearrangement, elucidating its cold-sensing mechanism.
  • Menthol activates TRPM8 through dynamic binding, explaining its specificity.
  • TRPM8 integrates cold and menthol stimuli via distinct pathways, advancing our understanding of cool sensation.