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Interaction of peptides derived from the Fas ligand with the Fyn‐SH3 domain
Author(s) -
Hane Michael,
Lowin Bente,
Peitsch Manuel,
Becker Karin,
Tschopp Jürg
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01051-f
Subject(s) - sh3 domain , fyn , proto oncogene tyrosine protein kinase src , fas ligand , microbiology and biotechnology , grb2 , chemistry , ligand (biochemistry) , biology , apoptosis , kinase , biochemistry , programmed cell death , receptor
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.