Interaction of peptides derived from the Fas ligand with the Fyn-SH3 domain
Details
Serval ID
serval:BIB_E1B81EED523A
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Interaction of peptides derived from the Fas ligand with the Fyn-SH3 domain
Journal
FEBS Letters
ISSN
0014-5793 (Print)
Publication state
Published
Issued date
10/1995
Volume
373
Number
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
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.
Keywords
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
Create date
24/01/2008 16:18
Last modification date
20/08/2019 17:05