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Significance The molecular organization of eukaryotic mechanosensory channels is largely uncharacterized. This characterization, having the correct parts list, is a necessary beginning step toward understanding how the channel transduces mechanical signals. Here we investigate the organization of the degenerin/epithelial sodium channel (DEG/ENaC) mechanosensory transduction channel in the six touch receptor neurons ofCaenorhabditis elegan s. Previous work has suggested that four membrane proteins formed a channel complex: the DEG/ENaC proteins MEC-4 and MEC-10 form the channel pore and the stomatin-like protein MEC-2 and paraoxonase-like protein MEC-6 act as auxiliary proteins. Using single molecule imaging, we find that the transduction complex is simpler, being a MEC-4:MEC-4:MEC-10 trimer. In contrast to the previous suggestion, this trimer does not appear to associate substantially with MEC-2 or MEC-6.

Subunit composition of a DEG/ENaC mechanosensory channel of Caenorhabditis elegans