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.[1]References
- Association of human fas (CD95) with a ubiquitin-conjugating enzyme (UBC-FAP). Wright, D.A., Futcher, B., Ghosh, P., Geha, R.S. J. Biol. Chem. (1996) [Pubmed]
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