Article Abstract:
Genetic and biochemical techniques are used to imply a Drosophila gene (drk) as an essential component of the sev receptor tyrosine kinase signal transduction pathway. The gene also encodes a protein that has a structure of SH3-SH2-SH3 and is homologous to the Sem-5 protein of C. elegans and mammalian GRB2. Moreover, the coupling of this gene with Son of sevenless, an activator of Ras guanine nucleotid exchange, leads to a conservation of signaling proteins during evolution. Thus, this approach may be a general mechanism for linking tyrosine kinases to Ras.
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Article Abstract:
A study was undertaken to investigate the biological activity of the mammalian Grb2, a subset of the SH2 domain-containing proteins of protein-tyrosine kinases, to relate it to the genetic analysis of an SH2/SH3 adaptor. The mammalian Grb2 was believed to bind phosphoproteins, docking proteins and cytoplasmic tyrosine kinases. Results revealed that Grb2 manifested multiple activities in normal and oncogenic signaling pathways. It was suggested that the Grb2 signaling pathway regulated cell differentiation in the early embryonic development.
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Article Abstract:
DOS, a product of the gene termed as daughter of sevenless (dos), contains an amino-terminally located pleckstrin homology domain and several tyrosine phosphorylation sites. It acts as a filter in signaling via the SEV (sevenless) protein in the developing eye of Drosophila. The tyrosine phosphorylation sites act as connection sites for various forms of signaling molecules. DOS acts a separate signaling pathway that is independent of the DRK SH2/SH3 protein in the SEV receptor tyrosine kinase pathway.
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