Differential affinity of FLIP and procaspase 8 for FADD’s DED binding surfaces regulates DISC assembly

@inproceedings{Majkut2014DifferentialAO,
  title={Differential affinity of FLIP and procaspase 8 for FADD’s DED binding surfaces regulates DISC assembly},
  author={Joanna Majkut and Miriam Sgobba and Caitriona Holohan and Nyree T. Crawford and AE Logan and Elizabeth Kerr and CA Higgins and KL Redmond and JS Riley and Izabela Stasik and DA Fennell and Sandra van Schaeybroeck and Shozeb M. Haider and P G Johnston and David Haigh and DB Longley},
  booktitle={Nature communications},
  year={2014}
}
Death receptor activation triggers recruitment of FADD, which via its death effector domain (DED) engages the DEDs of procaspase 8 and its inhibitor FLIP to form death-inducing signalling complexes (DISCs). The DEDs of FADD, FLIP and procaspase 8 interact with one another using two binding surfaces defined by α1/α4 and α2/α5 helices, respectively. Here we report that FLIP has preferential affinity for the α1/α4 surface of FADD, whereas procaspase 8 has preferential affinity for FADD's α2/α5… CONTINUE READING

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