Interaction of peptides derived from the Fas ligand with the Fyn‐SH3 domain

FEBS Letters

Hane, Michael²  Lowin, Bente²  Tschopp, Jürg²  Becker, Karin²  Peitsch, Manuel¹ 

[1] Glaxo Institute for Molecular Biology, CH-1028 Plan les-Ouates, Switzerland;Institute of Biochemistry, University of Lausanne, Chemin des Boveresses 155, CH-1066 Epalinges, Switzerland

关键词: Fyn;    SH3 domain;    Fas ligand;    Apo-1;    Apoptosis;   

DOI  :  10.1016/0014-5793(95)01051-F

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown