Department of Biochemistry, Duke University School of Medicine, Durham, NC 27710, USA.
Department of Biological Sciences, Lehigh University, Bethlehem, PA 18015, USA.
Sci Adv. 2024 Aug 2;10(31):eadp2211. doi: 10.1126/sciadv.adp2211.
Our sensory adaptation to cold and chemically induced coolness is mediated by the intrinsic property of TRPM8 channels to desensitize. TRPM8 is also implicated in cold-evoked pain disorders and migraine, highlighting its inhibitors as an avenue for pain relief. Despite the importance, the mechanisms of TRPM8 desensitization and inhibition remained unclear. We found, using cryo-electron microscopy, electrophysiology, and molecular dynamics simulations, that TRPM8 inhibitors bind selectively to the desensitized state of the channel. These inhibitors were used to reveal the overlapping mechanisms of desensitization and inhibition and that cold and cooling agonists share a common desensitization pathway. Furthermore, we identified the structural determinants crucial for the conformational change in TRPM8 desensitization. Our study illustrates how receptor-level conformational changes alter cold sensation, providing insights into therapeutic development.
我们对冷和化学诱导凉爽的感觉适应是由 TRPM8 通道的固有脱敏特性介导的。TRPM8 也与冷诱发疼痛障碍和偏头痛有关,这凸显了其抑制剂作为缓解疼痛的一种途径。尽管具有重要意义,但 TRPM8 脱敏和抑制的机制仍不清楚。我们通过低温电子显微镜、电生理学和分子动力学模拟发现,TRPM8 抑制剂选择性地结合到通道的脱敏状态。这些抑制剂被用来揭示脱敏和抑制的重叠机制,以及冷和冷却激动剂共享共同的脱敏途径。此外,我们确定了 TRPM8 脱敏中构象变化的关键结构决定因素。我们的研究说明了受体水平构象变化如何改变冷感觉,为治疗开发提供了思路。