The Fas–FADD death domain complex structure reveals the basis of DISC assembly and disease mutations

@inproceedings{Wang2010TheFD,
  title={The Fas–FADD death domain complex structure reveals the basis of DISC assembly and disease mutations},
  author={Liwei Wang and Jin Kuk Yang and Venkataraman Kabaleeswaran and Amanda J. Rice and Anthony C. Cruz and Ah Young Park and Qian Yin and Ermelinda Damko and Se Bok Jang and Stefan Raunser and Carol V Robinson and Richard M Siegel and Thomas Walz and Hao Wu},
  booktitle={Nature Structural &Molecular Biology},
  year={2010}
}
The death-inducing signaling complex (DISC) formed by the death receptor Fas, the adaptor protein FADD and caspase-8 mediates the extrinsic apoptotic program. Mutations in Fas that disrupt the DISC cause autoimmune lymphoproliferative syndrome (ALPS). Here we show that the Fas–FADD death domain (DD) complex forms an asymmetric oligomeric structure composed of 5–7 Fas DD and 5 FADD DD, whose interfaces harbor ALPS-associated mutations. Structure-based mutations disrupt the Fas–FADD interaction… CONTINUE READING

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Membrane-bound Fas ligand only is essential for Fas-induced apoptosis

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