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Resources » Paper

RJ Harrington et al. (1999) International C. elegans Meeting "Genetic interaction of the VAB-1 receptor tyrosine kinase with the PTP-1 receptor tyrosine phosphatase"

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  • Comments on RJ Harrington et al. (1999) International C. elegans Meeting "Genetic interaction of the VAB-1 receptor tyrosine kinase with the PTP-1 receptor tyrosine phosphatase" (0)

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    Status:
    Publication type:
    Meeting_abstract
    WormBase ID:
    WBPaper00023204

    RJ Harrington, MJ Gutch, MO Hengartner, NK Tonks, I Grinberg, & AD Chisholm (1999). Genetic interaction of the VAB-1 receptor tyrosine kinase with the PTP-1 receptor tyrosine phosphatase presented in International C. elegans Meeting. Unpublished information; cite only with author permission.

    Mutations in the C. elegans Eph receptor tyrosine kinase, VAB-1, and the ephrin, VAB-2, cause defects in neural and epidermal morphogenesis. Mutations in the VAB-1 kinase domain do not cause complete loss of function, suggesting that vab-1 may have kinase dependent and kinase independent functions (George et al ., Cell 92: 633). vab-1 null mutations cause incompletely penetrant defects, suggesting that VAB-1 signaling might be redundant with parallel pathways. To identify components of such parallel pathways we investigated whether vab-1 mutations displayed synthetic lethality with other morphogenetic mutants. A mutation in a C. elegans receptor tyrosine phosphatase, ptp-1(op147) , was isolated by M. Gutch, M. Hengartner, and N. Tonks, and was reported to cause mild morphogenetic defects similar to those of weak vab-1 alleles. We have found that ptp-1(op147) strongly synergizes with mutations affecting the VAB-1 kinase domain but not with mutations affecting the VAB-1 extracellular domain or with mutations in the VAB-2 ephrin. These data suggest that PTP-1 and the VAB-1 kinase activity function in parallel redundant pathways to regulate morphogenesis. We are characterizing ptp-1 genetically and molecularly to understand the basis for this synergistic interaction with VAB-1. PTP-1 is most similar to LAR-like receptor protein tyrosine phosphatases, characterized by globular domains and multiple fibronectin type III repeats in the extracellular domain and two tyrosine phosphatase domains in the cytoplasmic domain. We have found that the ptp-1 locus encodes two to four different transcripts. Studies are in progress to define the ptp-1 gene structure, determine the ptp-1 expression pattern, and characterize the ptp-1 ; vab-1 interaction.


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