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The structural basis of cold sensitivity.

Kevin Y Choi1,2,3,4, Xiaoxuan Lin1,4, Yifan Cheng1,5

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Summary
This summary is machine-generated.

The menthol receptor TRPM8 (transient receptor potential melastatin 8) opens in response to cold and menthol. This study reveals its unique

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Area of Science:

  • Structural biology
  • Molecular biophysics
  • Ion channel gating mechanisms

Background:

  • Thermosensitive transient receptor potential (TRP) ion channels mediate thermal sensation.
  • TRPM8, the mammalian cold and menthol receptor, is activated below ~26°C.
  • Understanding the structural basis of TRPM8 gating by temperature remains a challenge.

Purpose of the Study:

  • To elucidate the structural mechanisms underlying TRPM8 channel gating by cold and menthol.
  • To visualize temperature-evoked conformational states of TRPM8 in a cellular membrane environment.
  • To integrate structural data with thermodynamic measurements to map gating dynamics.

Main Methods:

  • Cryogenic electron microscopy (cryo-EM) to capture TRPM8 structures.
  • Hydrogen-deuterium exchange mass spectrometry (HDX-MS) for thermodynamic measurements.
  • Comparative analysis of human and avian TRPM8 orthologues.

Main Results:

  • Visualized bona fide cold- and menthol-evoked open states of TRPM8 in cellular membranes.
  • Identified a novel 'semi-swapped' architecture with rearranged interdigitation of subunits.
  • Pinpointed pore and TRP helices as key regions undergoing stimulus-evoked conformational changes driving gating.

Conclusions:

  • The study reveals a novel structural mechanism for TRPM8 gating involving a 'semi-swapped' architecture.
  • Pore and TRP helices are critical for temperature- and ligand-induced conformational dynamics.
  • A free energy landscape model explains TRPM8 gating by cold and cooling agents.