Voltage- and cold-dependent gating of single TRPM8 ion channels

International audienceTransient receptor potential (TRP) channels are nonselective cation channels, most of which are Ca 2+ permeable. When activated, they produce calcium influx and membrane depolarization in virtually all cell types by responding to diverse stimuli in a multimodal manner (Venkatachalam and Montell, 2007). Their membrane topology is similar to voltage-dependent K + channels (K v) with six transmembrane domains (S1-S6). TRP channels are tetrameric, with S5 and S6 domains lining the pore. However, compared with other classical voltageand ligand-gated ion channels, the fundamental singlechannel properties of TRPs remain largely unexplored. TRPM8, a member of the melastatin TRP subfamily, functions primarily as a neuronal cold receptor and has been characterized as the principal detector of environmental cold in the range of 15 to 30°C based on both biophysical and behavioral studies with TRPM8 knockout mice