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Resources » Paper

Minor, Paul et al. (2011) International Worm Meeting "FGF signaling cooperates with WNT signaling in C. elegans vulval cell lineage polarity."

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  • Comments on Minor, Paul et al. (2011) International Worm Meeting "FGF signaling cooperates with WNT signaling in C. elegans vulval cell lineage polarity." (0)

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    Status:
    Publication type:
    Meeting_abstract
    WormBase ID:
    WBPaper00038598

    Minor, Paul, Asthagiri, Anand, & Sternberg, Paul (2011). FGF signaling cooperates with WNT signaling in C. elegans vulval cell lineage polarity presented in International Worm Meeting. Unpublished information; cite only with author permission.

    The C. elegans vulva is formed from divisions of three vulval precursor cells (VPCs): P5.p, P6.p, and P7.p. P5.p and P7.p are induced and divide to form a 2 deg lineage pattern in which the daughter cells of P5.p and P7.p display mirror symmetry about the vulval center. Previous data shows the orientation of these cells is determined by the interaction of multiple Wnt signals. Two separate signal cascades beginning with Wnts from the anchor cell promote the wild-type, anterior-facing P7.p, vulval lineage, whereas the Wnt/EGL-20 signal from the tail promotes the daughter cells of P7.p to face the posterior. Here we show that EGL-20 acts through a member of the LDL receptor superfamily, LRP-2, in addtion to Ror/CAM-1, Van Gogh/VANG-1. All three proteins act together to control vulval polarity through the localization of the beta-catenin-like transcriptional coactivator SYS-1. We also show that the FGF/EGL-17 pathway acting through Raf/LIN-45 is also required for the P7.p wild-type lineage orientation. The role of FGF in the P7.p orientation decision presents the first evidence that the 1 deg daughter cells of P6.p influence the polarity of the neighboring 2 deg cells. Finally by observing SYS-1 localization we show that the FGF pathway converges with Wnt in determining P7.p orientation.

    Affiliations:
    - HHMI/Biology Division, Caltech, Pasadena, CA
    - Department of Chemical Engineering, Northeastern University, Boston, MA


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