DEDD, a novel death effector domain-containing protein, targeted to the nucleolus.
The CD95 signaling pathway comprises proteins that contain one or two death effector domains (DED), such as FADD/ Mort1 or caspase-8. Here we describe a novel 37 kDa protein, DEDD, that contains an N-terminal DED. DEDD is highly conserved between human and mouse (98. 7% identity) and is ubiquitously expressed. Overexpression of DEDD in 293T cells induced weak apoptosis, mainly through its DED by which it interacts with FADD and caspase-8. Endogenous DEDD was found in the cytoplasm and translocated into the nucleus upon stimulation of CD95. Immunocytological studies revealed that overexpressed DEDD directly translocated into the nucleus, where it co-localizes in the nucleolus with UBF, a basal factor required for RNA polymerase I transcription. Consistent with its nuclear localization, DEDD contains two nuclear localization signals and the C-terminal part shares sequence homology with histones. Recombinant DEDD binds to both DNA and reconstituted mononucleosomes and inhibits transcription in a reconstituted in vitro system. The results suggest that DEDD is a final target of a chain of events by which the CD95-induced apoptotic signal is transferred into the nucleolus to shut off cellular biosynthetic activities.[1]References
- DEDD, a novel death effector domain-containing protein, targeted to the nucleolus. Stegh, A.H., Schickling, O., Ehret, A., Scaffidi, C., Peterhänsel, C., Hofmann, T.G., Grummt, I., Krammer, P.H., Peter, M.E. EMBO J. (1998) [Pubmed]
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