The ksr-1 gene encodes a novel protein kinase involved in ras-mediated signaling in C. elegans

Article Abstract:

The Caenorhabditis elegans kinase suppressor of RAS (ksr-1) gene is a positive regulator of the let-60 ras signal transduction during vulval and larval development. The ksr-1 gene encodes a protein kinase which is structurally similar to Raf kinases. Null ksr-1 mutations have no effect in wild-type C. elegans but suppress the formation of multiple vulva by mutationally activated let-60 ras. The KSR kinase acts linear or parallel to let-60 ras. The Drosophila ksr gene encodes a protein kinase similar to KSR and inhibits the rough-eye phenotype caused by activated Ras1 gene.

Mutation (Biology), Mutation, Protein kinases

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An FGF receptor signaling pathway is required for the normal cell migrations of the sex myoblasts in C. elegans hermaphrodites

Article Abstract:

The anterior migration of sex myoblasts (SMs) in Caenorhabditis elegans hermaphrodites is controlled by an extracellular signal to the receptor tyrosine kinase encoded by the egl-15 gene. The protein is a fibroblast growth factor receptor (FGFR). The SMs of egl-15 mutants migrate posteriorly away from the gonads under repulsion from the gonadal cells. The extracellular signal to the FGFR is probably attractive and in its absence a repulsive signal dominates. The sem-5 gene produces an adaptor molecule involved in signal transduction in the FGFR pathways.

Proteins, Cell receptors, Cell migration

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clr-1 encodes a receptor tyrosine phosphatase that negatively regulates an FGF receptor signaling pathway in Caenorhabditis elegans

Article Abstract:

The protein CLR-1 in Caenorhabditis elegans, a receptor tyrosine phosphatase, apparently reduces the action of a signaling pathway mediated by fibroblast growth factor receptor (FGFR) through dephosphorylation. CLR-1 has two intracellular phosphatase domains as well as a complex extracellular area. The in vivo function of CLR-1 depends on activity in the membrane-proximal phosphatase domain. The membrane-distal domain does not appear to be essential for normal functioning.

Genetic aspects, Phosphatases, Fibroblast growth factors

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