Abstract
Channels are typically gated by several factors, including voltage, ligand and mechanical force. Most members of the calcium homeostasis modulator (CALHM) protein family, large-pore ATP release channels, exist in different oligomeric states. Dynamic conversions between CALHM1 heptamers and octamers to gate the channel were proposed. Meanwhile, the latest study observed that the transient receptor potential vanilloid 3 (TRPV3) channel adopts a dynamic transition between pentamers and canonical tetramers in response to small molecule treatment. These results suggest that oligomeric rearrangement may add a new layer to regulate the channel activities.