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Resources » Paper

Bojun Chen et al. (2007) International Worm Meeting "UNC-1 is required for the function of UNC-9-based gap junctions in C. elegans."

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    Status:
    Publication type:
    Meeting_abstract
    WormBase ID:
    WBPaper00030626

    Bojun Chen, Qiang Liu, Qian Ge, Jia Xie, & Zhao-Wen Wang (2007). UNC-1 is required for the function of UNC-9-based gap junctions in C. elegans presented in International Worm Meeting. Unpublished information; cite only with author permission.

    The unc-1 gene encodes a close homologue of the mammalian protein stomatin. Recent studies suggest that stomatin or stomatin-like proteins modulate mechno- and acid-sensitive ion channels. In C. elegans, loss-of-function mutation (lf) of unc-1 causes the kinked locomotion defect and suppresses the hypersensitivity to volatile anesthetics caused by mutations of unc-79 or unc-80. These phenotypes are similar to those exhibited by unc-9(lf) mutants. We have previously determined that the innexin UNC-9 is a key component of gap junctions mediating electrical coupling of body-wall muscle cells. In this study, we found that UNC-1 was also involved in electrical coupling of body-wall muscle cells. unc-1(lf) inhibited electrical coupling to a similar degree as unc-9(lf), and unc-1(lf);unc-9(lf) double mutant did not further inhibit the coupling compared with the unc-9 single mutant, suggesting that the coupling defect observed in the unc-1 mutant was primarily, if not exclusively, due to inhibition of UNC-9-based gap junctions. unc-1 was expressed in body-wall muscle cells as well as many neurons, which is similar to the expression pattern of unc-9. Coexpression of Myc-tagged UNC-9 and HA-tagged UNC-1 showed that the two fusion proteins co-localized at body-wall muscle intercellular junctions and along neuronal processes. Furthermore, locomotion defects of the unc-1(lf);unc-9(lf) double mutant were similar to those of either single mutant, while the coiled phenotype of an unc-1 dominant gain-of-function mutant was suppressed by unc-9(lf), suggesting that unc-1 genetically interacts with unc-9. These results show that UNC-1 is required for the function of UNC-9-based gap junctions in C. elegans. Because there is no similar report in the literature, this study has revealed a novel mechanism of gap junction regulation.


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