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. 2010 Oct 18;191(2):237–248. doi: 10.1083/jcb.201006074

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© 2010 Lumpkin et al.

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Figure 4. — A molecular model of touch—the MEC-4 complex. The MEC-4 complex of C. elegans body-touch neurons has been the focus of three decades of research. MEC-4 and MEC-10 are Deg/ENaC isoforms that serve as pore-forming subunits. Functional channels likely contain two MEC-4 subunits and one MEC-10 subunit (Hong and Driscoll, 1994; Jasti et al., 2007). MEC-2 and MEC-6 are accessory subunits that enable channel activity. MEC-2 is a stomatin-like protein located in the inner leaflet of the membrane, whereas MEC-6 is a paraoxonase-like transmembrane protein (Chelur et al., 2002). Mechanotransduction also requires a specialized extracellular matrix, consisting of MEC-5, a collagen isoform, and MEC-1 and MEC-9, both with multiple EGF repeats. MEC-7 and MEC-12 are tubulin monomers that form 15-protofilament microtubules required for touch sensitivity.