Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Apoptosis / genetics
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Computer Graphics
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Cytoplasm / metabolism
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Fas Ligand Protein
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Humans
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Immunoblotting
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Membrane Glycoproteins / chemistry
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Membrane Glycoproteins / metabolism*
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Membrane Proteins / chemistry
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Membrane Proteins / metabolism
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Mice
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Models, Molecular
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Molecular Sequence Data
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Peptide Fragments / chemistry
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Peptide Fragments / metabolism
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Proline / chemistry
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Proline / metabolism
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Protein-Tyrosine Kinases / chemistry
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Protein-Tyrosine Kinases / metabolism*
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Proto-Oncogene Proteins / chemistry
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Proto-Oncogene Proteins / metabolism*
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Proto-Oncogene Proteins c-fyn
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Recombinant Fusion Proteins / metabolism
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Sequence Alignment
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src Homology Domains*
Substances
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FASLG protein, human
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Fas Ligand Protein
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Fasl protein, mouse
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Membrane Glycoproteins
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Membrane Proteins
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Peptide Fragments
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Proto-Oncogene Proteins
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Recombinant Fusion Proteins
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Proline
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Protein-Tyrosine Kinases
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FYN protein, human
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Fyn protein, mouse
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Proto-Oncogene Proteins c-fyn