Redefining the Caenorhabditis elegans DEG/ENaC Mechanosensory Channel Complex

Mechanosensation underlies multiple senses, such as touch, pain, hearing, and proprioception. The molecules that mediate most of the mechanical senses have not been identified. Genetic and molecular methods have identified several putative mechanosensitive proteins. However, how the mechanotransduction machineries organize and function remains largely unknown. To understand the organization of the mechanotransduction complex, I studied the DEG/ENaC mechanosensory channel that detects gentle touch in the six touch receptor neurons (TRNs) of C. elegans. Previous studies from our lab have suggested that this channel complex contains two pore-forming subunits MEC-4 and MEC-10 (DEG/ENaC proteins) and two auxiliary subunits MEC-6 (paraoxonase-like protein) and MEC-2 (stomatin-like protein). However, questions remain about what molecules really constitute this mechanosensory channel complex. Studying this particular DEG/ENaC channel in C. elegans will not only elucidate the organization of one major mechanosensory complex, but also improve our knowledge of other DEG/ENaC proteins, which are found in both vertebrates and invertebrates, and involved in various functions, e.g. mechanosensati