Molecular modeling of mechanotransduction in the nematode Caenorhabditis elegans.
Genetic and molecular studies of touch avoidance in the nematode Caenorhabditis elegans have resulted in a molecular model for a mechanotransducing complex. mec-4 and mec-10 encode proteins hypothesized to be subunits of a mechanically gated ion channel that are related to subunits of the vertebrate amiloride-sensitive epithelial Na+ channel. Products of mec-5, a novel collagen, and mec-9, a protein that includes multiple Kunitz-type protease inhibitor repeats and EGF repeats, may interact with the channel in the extracellular matrix. Inside the cell, specialized 15-protofilament microtubules composed of mec-12 alpha-tubulin and mec-7 beta-tubulin may be linked to the mechanosensitive channel by stomatin-homologous MEC-2. MEC-4 and MEC-10 are members of a large family of C. elegans proteins, the degenerins. Two other degenerins, UNC-8 and DEL-1, are candidate components of a stretch-sensitive channel in motor neurons. Implications for advancing understanding of mechanotransduction in other systems are discussed.
Tavernarakis
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Department of Molecular Biology and Biochemistry, Rutgers University, New Brunswick, New Jersey 08855, USA.
Driscoll
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D000818:Animals; D017173:Caenorhabditis elegans / Q000502:physiology*; D006801:Humans; D008465:Mechanoreceptors / Q000502:physiology*; D008958:Models, Molecular; D010812:Physical Stimulation; D015398:Signal Transduction; D014110:Touch / Q000502:physiology