Premium
Interaction of Fas(Apo‐1/CD95) with proteins implicated in the ubiquitination pathway
Author(s) -
Becker Karin,
Schneider Pascal,
Hofmann Kay,
Mattmann Chantal,
Tschopp Jürg
Publication year - 1997
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/s0014-5793(97)00758-8
Subject(s) - fas receptor , death domain , fas ligand , ubiquitin , ubiquitin conjugating enzyme , apoptosis , microbiology and biotechnology , cytoplasm , signal transduction , hela , biology , receptor , chemistry , programmed cell death , ubiquitin ligase , biochemistry , gene , in vitro
Fas(Apo‐1/CD95), a receptor belonging to the tumor necrosis factor receptor family, induces apoptosis when triggered by Fas ligand. Upon its activation, the cytoplasmic domain of Fas binds several proteins which transmit the death signal. We used the yeast two‐hybrid screen to isolate Fas‐associated proteins. Here we report that the ubiquitin‐conjugating enzyme UBC9 binds to Fas at the interface between the death domain and the membrane‐proximal region of Fas. This interaction is also seen in vivo. UBC9 transiently expressed in HeLa cells bound to the co‐expressed cytoplasmic segment of Fas. FAF1, a Fas‐associated protein that potentiates apoptosis (Chu et al. (1996) Proc. Natl. Acad. Sci. USA 92, 11894–11898), was found to contain sequences similar to ubiquitin. These results suggest that proteins related to the ubiquitination pathway may modulate the Fas signaling pathway.