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Interaction of the widely expressed Fas with its membrane-bound ligand (FasL) leads to rapid cell death via apoptosis. To avoid pathological tissue damage, the activity of FasL requires tight regulation. Here, we report that the Src homology 3 (SH3) domain of Fyn binds to the proline-rich cytoplasmic region of FasL. Binding of the SH3 domain occurs between amino acid residues 44-71 which contains several potential SH3 interaction sites. This binding is specific, as SH3 domains of Lck, Grb2 and ras-GAP bind only weakly or not at all. We suggest that FasL activity may be modulated by SH3 domains of the src-like Fyn kinase.
Pubmed ID: 7589480 RIS Download
Mesh terms: Amino Acid Sequence | Animals | Apoptosis | Computer Graphics | Cytoplasm | Fas Ligand Protein | Humans | Immunoblotting | Membrane Glycoproteins | Membrane Proteins | Mice | Models, Molecular | Molecular Sequence Data | Peptide Fragments | Proline | Protein-Tyrosine Kinases | Proto-Oncogene Proteins | Proto-Oncogene Proteins c-fyn | Recombinant Fusion Proteins | Sequence Alignment | src Homology Domains
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