The Caenorhabditis elegans death protein Ced-4 contains a motif with similarity to the mammalian 'death effector domain'

被引:13
作者
Bauer, MKA [1 ]
Wesselborg, S [1 ]
SchulzeOsthoff, K [1 ]
机构
[1] UNIV FREIBURG,INST BIOCHEM & MOL BIOL,D-79104 FREIBURG,GERMANY
关键词
apoptosis; Ced-4; Fas; APO-1; death effector domain; FADD; FLICE;
D O I
10.1016/S0014-5793(96)01497-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In the nematode Caenorhabditis elegans apoptosis is tightly regulated by a hierarchical set of genes. Two of these, ced-3 and ced-9, possess mammalian homologues encoding executional ICE proteases and inhibitory Bcl-2-related proteins, respectively. The function of a third key player, ced-4, is however completely unknown and no mammalian counterparts have been identified. Here me report that Ced-4 protein contains a structural region with similarity to the mammalian death effector domain which has previously been demonstrated to act as an important protein interaction motif in the signaling pathway of the mammalian surface receptor Fas (APO-1, CD95). Based on this finding and previously described genetic experiments, we propose that Ced-4, similar to the mammalian proteins FADD and FLICE, may possess a function as an adaptor protein in invertebrate apoptotic pathways.
引用
收藏
页码:256 / 258
页数:3
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