Characterization of Gas6, a member of the superfamily of G domain-containing proteins, as a ligand for Rse and Axl
Autor: | Jian Chen, P. J. Godowsk, Michael D. Sadick, Melanie R. Mark, R. G. Hammonds |
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Rok vydání: | 1996 |
Předmět: |
Molecular Sequence Data
Kidney Ligands Transfection Biochemistry Polymerase Chain Reaction Receptor tyrosine kinase Cell Line Laminin Proto-Oncogene Proteins Humans Molecular Biology DNA Primers Sequence Deletion Sequence Tagged Sites Gla domain Oncogene Proteins Binding Sites biology AXL receptor tyrosine kinase Base Sequence GAS6 Brain Genetic Variation Proteins Receptor Protein-Tyrosine Kinases Cell Biology Axl Receptor Tyrosine Kinase Recombinant Proteins Dystroglycan complex Kinetics Liver G-domain Mutagenesis Protein Biosynthesis biology.protein Mutagenesis Site-Directed Phosphorylation Intercellular Signaling Peptides and Proteins |
Zdroj: | The Journal of biological chemistry. 271(16) |
ISSN: | 0021-9258 |
Popis: | Rse, Ax1, and c-Mer comprise a family of cell adhesion molecule-related tyrosine kinase receptors. Human Gas6 was recently shown to act as a ligand for both human Rse (Godowski et al., 1995) and human Ax1 (Varnum et al., 1995). Gas6 contains an NH2-terminal Gla domain followed by four epidermal growth factor-like repeats and tandem globular (G) domains. The G domains are related to those found in sex hormone-binding globulin and to those utilized by laminin and agrin for binding to the dystroglycan complex. A series of Gas6 variants were tested for their ability to bind to Rse and Ax1. The Gla domain and epidermal growth factor-like repeats were not required for receptor binding, as deletion variants of Gas6 which lacked these domains bound to the extracellular domains of both Rse and Axl. A deletion variant of Gas6 containing just the G domain region was shown to activate Rse phosphorylation. These results provide evidence that G domains can act as signaling molecules by activating transmembrane receptor tyrosine kinases. Furthermore, they provide a structural link between the activation of cell adhesion related receptors and the control of cell growth and differentiation by the G domain-containing superfamily of proteins. |
Databáze: | OpenAIRE |
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