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Interaction between Gab1 and the c-Met receptor tyrosine kinase is responsible for epithelial morphogenesis

Item Type:Article
Title:Interaction between Gab1 and the c-Met receptor tyrosine kinase is responsible for epithelial morphogenesis
Creators Name:Weidner, K.M. and Dicesare, S. and Sachs, M. and Brinkmann, V. and Behrens, J. and Birchmeier, W.
Abstract:The proteins Gab1 and the related DOS (for 'daughter of sevenless') each bind to substrates of tyrosine kinases like Grb2 or Corkscrew, and act in signalling pathways downstream of tyrosine kinase receptors. Here we show that Gab1 interacts directly with the c-met-encoded receptor tyrosine kinase but not with a number of other tyrosine kinases from different subfamilies. A newly identified proline-rich domain of Gab1 is responsible for the binding of this protein to the tyrosine-phosphorylated bidentate docking site in c-Met. Expression of Gab1 in epithelial cells is sufficient to induce the c-Met-specific activities, including branching morphogenesis. Thus we have discovered a new phosphotyrosine interaction domain in Gab1 and shown that Gab1 is the substrate of the c-Met receptor tyrosine kinase that mediates epithelial morphogenesis.
Keywords:Amino Acid Sequence, Binding Sites, Cell Line, Epithelium, Molecular Sequence Data, Morphogenesis, Phosphoproteins, Precipitin Tests, Proline, Protein Binding, Proto-Oncogene Proteins c-met, Receptor Protein-Tyrosine Kinases, Recombinant Fusion Proteins, Saccharomyces Cerevisiae, Signal Transducing Adaptor Proteins, Signal Transduction, Substrate Specificity, Animals, Mice
Publisher:Nature Publishing Group
Page Range:173-176
Date:14 November 1996
Official Publication:https://doi.org/10.1038/384173a0
PubMed:View item in PubMed

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