Interaction of peptides derived from the Fas ligand with the Fyn-SH3 domain
Détails
ID Serval
serval:BIB_E1B81EED523A
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Interaction of peptides derived from the Fas ligand with the Fyn-SH3 domain
Périodique
FEBS Letters
ISSN
0014-5793 (Print)
Statut éditorial
Publié
Date de publication
10/1995
Volume
373
Numéro
3
Pages
265-8
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Oct 16
Research Support, Non-U.S. Gov't --- Old month value: Oct 16
Résumé
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.
Mots-clé
Amino Acid Sequence
Animals
Apoptosis/genetics
Computer Graphics
Cytoplasm/metabolism
Fas Ligand Protein
Humans
Immunoblotting
Membrane Glycoproteins/chemistry/*metabolism
Membrane Proteins/chemistry/metabolism
Mice
Models, Molecular
Molecular Sequence Data
Peptide Fragments/chemistry/metabolism
Proline/chemistry/metabolism
Protein-Tyrosine Kinases/chemistry/*metabolism
Proto-Oncogene Proteins/chemistry/*metabolism
Proto-Oncogene Proteins c-fyn
Recombinant Fusion Proteins/metabolism
Sequence Alignment
*src Homology Domains
Pubmed
Web of science
Création de la notice
24/01/2008 16:18
Dernière modification de la notice
20/08/2019 17:05