Interaction of peptides derived from the Fas ligand with the Fyn-SH3 domain.
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.
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
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
FEBS Lett.
Date: Oct. 16, 1995
PubMed ID: 7589480
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