Evidence of complex formation between FADD and c-FLIP death effector domains for the death inducing signaling complex

@inproceedings{Hwang2014EvidenceOC,
  title={Evidence of complex formation between FADD and c-FLIP death effector domains for the death inducing signaling complex},
  author={Eun Young Hwang and Mi Suk Jeong and So Young Park and Se Bok Jang},
  booktitle={BMB reports},
  year={2014}
}
Adaptor protein FADD forms the death inducing signaling complex (DISC) by recruiting the initiating caspases-8 and -10 through homotypic death effector domain (DED) interactions. Cellular FLICE-inhibitory protein (c-FLIP) is an inhibitor of death ligand-induced apoptosis downstream of death receptors, and FADD competes with procaspase-8/10 for recruitment for DISC. However, the mechanism of action of FADD and c-FLIP proteins remain poorly understood at the molecular level. In this study, we… CONTINUE READING