Current View of Ligand and Lipid Recognition by the Menthol Receptor TRPM8.

Trends in Biochemical Sciences
Ying Yin, Seok-Yong Lee

Abstract

Transient receptor potential (TRP) melastatin member 8 (TRPM8), which is a calcium-permeable ion channel, functions as the primary molecular sensor of cold and menthol in humans. Recent cryoelectron microscopy (cryo-EM) studies of TRPM8 have shown distinct structural features in its architecture and domain assembly compared with the capsaicin receptor TRP vanilloid member 1 (TRPV1). Moreover, ligand-bound TRPM8 structures have uncovered unforeseen binding sites for both cooling agonists and membrane lipid phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2]. These complex structures unveil the molecular basis of cooling agonist sensing by TRPM8 and the allosteric role of PI(4,5)P2 in agonist binding for TRPM8 activation. Here, we review the recent advances in TRPM8 structural biology and investigate the molecular principles governing the distinguishing role of TRPM8 as the evolutionarily conserved menthol receptor.

Citations

Jan 22, 2021·Biochimica Et Biophysica Acta. Molecular Basis of Disease·Bruno StiegerKaspar P Locher
Mar 7, 2021·International Journal of Molecular Sciences·María Ángeles BonacheRosario González-Muñiz
Jul 14, 2021·Journal of Cell Science·Lixia Yue, Haoxing Xu
Aug 28, 2021·International Journal of Molecular Sciences·Carolina IzquierdoRosario González-Muñiz

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