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Resources » Paper

SE George et al. (1999) International C. elegans Meeting "Still Searching for components of the VAB-1 pathways"

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    Publication type:
    Meeting_abstract
    WormBase ID:
    WBPaper00023155

    SE George, & AD Chisholm (1999). Still Searching for components of the VAB-1 pathways presented in International C. elegans Meeting. Unpublished information; cite only with author permission.

    We are identifying the mechanisms by which the C. elegans Eph receptor tyrosine kinase, VAB-1, signals in neural and epithelial morphogenesis. VAB-1 has both kinase-dependent and kinase-independent functions during C. elegans development (George et al, Cell 92:633). The kinase-dependent (forward signaling) function of VAB-1 is mediated by its cytoplasmic kinase domain, possibly through tyrosine phosphorylation of the juxtamembrane domain. Proteins that interact with the cytoplasmic domain of Eph receptors have been identified in vertebrates using the yeast two-hybrid system. Candidate molecules include a low molecular weight protein tyrosine phosphatase and adaptor proteins such as Nck, Grb2, and Grb10. We are using a modified yeast two-hybrid screen to identify genes that function in VAB-1 forward signaling. Initial progress and methodology of the screen will be presented. The nature of the VAB-1 kinase-independent function is unknown but may involve the extracellular domain. Our genetic and biochemical studies indicate that VAB-2 (a C. elegans ephrin) is a ligand for VAB-1 and that it appears to mediate the kinase-independent function of VAB-1 (see Chin-Sang et al abstract). vab-2 mutations display synthetic lethality with vab-1 kinase mutations. We also observe synthetic lethality between vab-1 kinase mutations and a mutation in the receptor protein tyrosine phosphatase, PTP-1, suggesting that PTP-1 may be acting in a parallel pathway to the VAB-1 kinase activity (see Harrington et al abstract). To identify genes that are acting in the VAB-1 kinase-independent pathway or in parallel pathways we are performing screens to identify mutations that are synthetic lethal with vab-1 . Progress of the screen will be presented.


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