This gene encodes a protein that contains a death effector domain (DED). DED is a protein–protein interaction domain shared by adaptors, regulators and executors of the programmed cell death pathway. Overexpression of this gene was shown to induce weak apoptosis. Upon stimulation, this protein was found to translocate from cytoplasm to nucleus and colocalize with UBTF, a basal factor required for RNA polymerase I transcription, in the nucleolus. At least three transcript variants encoding the same protein have been found for this gene.[3]
↑ 4.04.1Zhan Y, Hegde R, Srinivasula SM, Fernandes-Alnemri T, Alnemri ES (Apr 2002). "Death effector domain-containing proteins DEDD and FLAME-3 form nuclear complexes with the TFIIIC102 subunit of human transcription factor IIIC". Cell Death Differ. 9 (4): 439–47. doi:10.1038/sj/cdd/4401038. PMID11965497.
↑ 5.05.1Roth W, Stenner-Liewen F, Pawlowski K, Godzik A, Reed JC (Mar 2002). "Identification and characterization of DEDD2, a death effector domain-containing protein". J. Biol. Chem. 277 (9): 7501–8. doi:10.1074/jbc.M110749200. PMID11741985.
↑Alcivar A, Hu S, Tang J, Yang X (Jan 2003). "DEDD and DEDD2 associate with caspase-8/10 and signal cell death". Oncogene. 22 (2): 291–7. doi:10.1038/sj.onc.1206099. PMID12527898.
Further reading
Park MY, Ryu SW, Kim KD, Lim JS, Lee ZW, Kim E (2005). "Fas-associated factor-1 mediates chemotherapeutic-induced apoptosis via death effector filament formation". Int. J. Cancer. 115 (3): 412–8. doi:10.1002/ijc.20857. PMID15688372.
Alcivar A, Hu S, Tang J, Yang X (2003). "DEDD and DEDD2 associate with caspase-8/10 and signal cell death". Oncogene. 22 (2): 291–7. doi:10.1038/sj.onc.1206099. PMID12527898.
Zhan Y, Hegde R, Srinivasula SM, Fernandes-Alnemri T, Alnemri ES (2002). "Death effector domain-containing proteins DEDD and FLAME-3 form nuclear complexes with the TFIIIC102 subunit of human transcription factor IIIC". Cell Death Differ. 9 (4): 439–47. doi:10.1038/sj/cdd/4401038. PMID11965497.
Schickling O, Stegh AH, Byrd J, Peter ME (2002). "Nuclear localization of DEDD leads to caspase-6 activation through its death effector domain and inhibition of RNA polymerase I dependent transcription". Cell Death Differ. 8 (12): 1157–68. doi:10.1038/sj.cdd.4400928. PMID11753564.
Roth W, Stenner-Liewen F, Pawlowski K, Godzik A, Reed JC (2002). "Identification and characterization of DEDD2, a death effector domain-containing protein". J. Biol. Chem. 277 (9): 7501–8. doi:10.1074/jbc.M110749200. PMID11741985.
