title: Molecules that mediate touch transduction in the nematode Caenorhabditis elegans.
abstract: Despite the widespread importance of mechanotransduction in biology, remarkably little is known about the nature of the molecules that mediate mechanical signaling. Mechanosensation in the nematode Caenorhabditis elegans is mediated by six mechanosensory neurons called touch receptor cells. Genetic analysis has resulted in the identification of over 400 mutations that disrupt the function of the touch receptors. Molecular characterization of the genes revealed has identified subunits of a candidate mechanosensory ion channel, tubulins expressed specifically in the touch receptors, and extracellular matrix proteins needed for mechanotransduction. mec-4 and mec-10 encode members of a C. elegans gene family related to the vertebrate epithelial Na+ channel that are hypothesized to encode subunits of a mechanosensory channel. mec-6 may encode another channel subunit. Inside the cell, alpha-tubulin MEC-12, beta-tubulin MEC-7 and a candidate linker protein MEC-2 may interact with the mechanotransducing channel to deliver gating tension. In the extracelluar matrix, collagen MEC-5 and MEC-9 and MEC-1 may interact with extracellular channel domains. A molecular model for mechanotransduction is discussed.
authors.affiliation: Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, NJ 08855, USA.
authors.forename: M
authors.initials: M
authors.lastname: Driscoll
authors.forename: N
authors.initials: N
authors.lastname: Tavernarakis
mesh_terms: D000818:Animals; D017173:Caenorhabditis elegans / Q000166:cytology / Q000235:genetics* / Q000502:physiology; D004252:DNA Mutational Analysis; D017238:Genes, Helminth; D007473:Ion Channels / Q000502:physiology*; D008465:Mechanoreceptors / Q000502:physiology* / Q000648:ultrastructure; D009154:Mutation; D009475:Neurons, Afferent / Q000502:physiology*; D015398:Signal Transduction / Q000235:genetics* / Q000502:physiology; D014110:Touch; D014404:Tubulin / Q000235:genetics / Q000502:physiology
chemical_list: D007473:Ion Channels; D014404:Tubulin