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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Hane M,Lowin B,Peitsch M,Becker K,Tschopp Jdoi
10.1016/0014-5793(95)01051-fsubject
Has Abstractpub_date
1995-10-16 00:00:00pages
265-8issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(95)01051-Fjournal_volume
373pub_type
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