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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.

Pubmed ID: 7589480

Authors

  • Hane M
  • Lowin B
  • Peitsch M
  • Becker K
  • Tschopp J

Journal

FEBS letters

Publication Data

October 16, 1995

Associated Grants

None

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