Hane M Lowin B Peitsch M Becker K Tschopp J 1995 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. https://sonar.ch/global/documents/93690 eng info:eu-repo/semantics/altIdentifier/doi/10.1016/0014-5793(95)01051-f info:eu-repo/semantics/altIdentifier/pmid/7589480 FEBS letters. - 1995 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 Interaction of peptides derived from the Fas ligand with the Fyn-SH3 domain. http://purl.org/coar/resource_type/c_6501