Gene or accession: CG4319
Gene annotation error
Gene rpr and fas not homologs has a mistake in the supporting evidence or
functional assignment.
Comments: The report states that reaper and fas are homologs. This is highly
unlikely.
The proposition that RPR might represent an ancestral member of 'death
domain' containing proteins and, as such, could share functions in common with
death receptors (Cleveland and Ihle, 1995; Golstein et al., 1995; Golstein et
al., 1995) was not supported by studies in vivo (Chen et al., 1996; Vucic et
al., 1997). The lack of a homologous relationship between REAPER and of
'death domain' containing proteins was further bolstered by the recent
structural determination of a death domain (Huang et al., 1996; Liang and
Fesik, 1997).
References
Chen, P., Lee, P., Otto, L., and Abrams, J. M. (1996). Apoptotic activity of
REAPER is distinct from signalling by the tumor necrosis factor receptor 1
death domain. J. Biol. Chem. 271, 25735-25737.
Cleveland, J. L., and Ihle, J. N. (1995). Contenders in FasL/TNF death
signaling. Cell 81, 479-82.
Golstein, P., Marguet, D., and Depraetere, V. (1995). Fas bridging cell death
and cytotoxicity: the reaper connection. Immunol. Rev. 146, 45-56.
Golstein, P., Marguet, D., and Depraetere, V. (1995). Homology between Reaper
and the cell death domains of Fas and TNFR1. Cell 81, 185-186.
Huang, B., Eberstadt, M., Olejniczak, E. T., Meadows, R. P., and Fesik, S. W.
(1996). NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain.
Nature 384, 638-41.
Liang, H., and Fesik, S. W. (1997). THREE-DIMENSIONAL STRUCTURES OF PROTEINS
INVOLVED IN PROGRAMMED CELL DEATH Review. Journal of Molecular Biology 274,
291-302.
Vucic, D., Seshagiri, S., and Miller, L. K. (1997). Characterization of
reaper- and fadd-induced apoptosis in a lepidopteran cell line. Molecular &
Cellular Biology 17, 667-676.