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.
Mesh Terms:
Animals, Antigens, CD95, Blotting, Northern, Blotting, Western, COS Cells, Chromosome Mapping, Humans, Ligases, Mutagenesis, Site-Directed, Sequence Deletion, Tumor Cells, Cultured, Ubiquitin-Conjugating Enzymes
Animals, Antigens, CD95, Blotting, Northern, Blotting, Western, COS Cells, Chromosome Mapping, Humans, Ligases, Mutagenesis, Site-Directed, Sequence Deletion, Tumor Cells, Cultured, Ubiquitin-Conjugating Enzymes
J. Biol. Chem.
Date: Dec. 06, 1996
PubMed ID: 8940097
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