The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1

Article Abstract:

SH3 domains of Grb2 are tied to proline-rich carboxy-terminal mSos1 tail. The mSos1 is a ligand for Grb2SH3 domains. Sos is needed for Ras signalling and has central domain connected to Ras-GNRPs. EGF stimulates binding of Grb2-mSos1 complex to autophosphorylated EGF receptor. Grb2 links tyrosine kinases to Ras-GNRP in mammalian cells. Conduction of mSos1 to a particulate fraction of a cell is brought about by binding Grb2-mSos1 complex to an autophosphorylated EGFR. Exchange of GDP for GTP results from contact of mSos1 with the membrane.

Analysis, Growth, Cytology, Cell receptors, Mammals, Epidermal growth factor, Epidermal growth factors

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Vascular system defects and neuronal apoptosis in mice lacking Ras GTPase-activating protein

Article Abstract:

Embryos of mice which lack rasGAP demonstrate neuronal apoptosis and major defects in endothelial cell organization. The Ras activity during embryonic development is controlled by the dual action of rasGAP and neurofibromin. A synergistic effect results when the Gap and Nf1 genes undergo mutations. The resulting embryo displays a deteriorated Gap phenotype. Biochemical studies show that the rasGAP complex is a substrate for Flt-1 and Flk-1 tyrosine-kinase activity.

Embryology, Experimental, Embryological research, G proteins, Ras genes, Neurofibrils

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Mad about SMADs

Article Abstract:

The family of signalling molecules, transforming growth factor-beta (TGF-beta), regulate cell proliferation. SMAD proteins are relevant to TGF-beta-mediated signalling in vertebrates. Hata and Shi and colleagues have shown how such signalling molecules could regulate their function, and how SMAD protein mutations can upset their activity in development and human cancer.

Cellular signal transduction, Transforming growth factors

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