Association of human fas (CD95) with a ubiquitin-conjugating enzyme (UBC-FAP).
A novel human ubiquitin conjugating enzyme (UBC) was found to associate with Fas (CD95). The mRNA for this UBC Fas-associated protein (FAP) was widely expressed in human tissues, and the protein was identified in several mammalian cell lines. UBC-FAP shows strong homology to two recently identified UBCs, Hus5 and Ubc9, which control yeast cell cycle progression. UBC-FAP, but not an active site mutant, complemented ubc9-1(ts) mutants. This suggests that UBC-FAP is a human homologue of Ubc9, possesses ubiquitin conjugating activity, and may play an important role in mammalian cell cycle regulation. A single amino acid substitution in the death domain of Fas that abolishes Fas-mediated apoptosis also abolished Fas association with UBC-FAP, suggesting that UBC-FAP may play a role in Fas signal transduction. The sequence of UBC-FAP is identical to that of HsUbc9, a UBC recently shown to interact with Rad51.
Wright
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DA
Department of Medicine, Division of Immunology, Children's Hospital, and Department of Pediatrics, Harvard Medical School, Boston, Massachusetts 02115, USA.
Futcher
B
B
Ghosh
P
P
Geha
R S
RS
D000818:Animals; D015152:Blotting, Northern; D015153:Blotting, Western; D019556:COS Cells; D002874:Chromosome Mapping; D006801:Humans; D008025:Ligases / Q000378:metabolism*; D016297:Mutagenesis, Site-Directed; D017384:Sequence Deletion; D014407:Tumor Cells, Cultured; D044763:Ubiquitin-Conjugating Enzymes; D019014:fas Receptor / Q000378:metabolism*; D000098843:Ubiquitin-Conjugating Enzyme UBC9
D019014:fas Receptor; D044763:Ubiquitin-Conjugating Enzymes; D008025:Ligases; D000098843:Ubiquitin-Conjugating Enzyme UBC9