Nature Communications (Feb 2021)

Cryo-EM structural analysis of FADD:Caspase-8 complexes defines the catalytic dimer architecture for co-ordinated control of cell fate

  • Joanna L. Fox,
  • Michelle A. Hughes,
  • Xin Meng,
  • Nikola A. Sarnowska,
  • Ian R. Powley,
  • Rebekah Jukes-Jones,
  • David Dinsdale,
  • Timothy J. Ragan,
  • Louise Fairall,
  • John W. R. Schwabe,
  • Nobuhiro Morone,
  • Kelvin Cain,
  • Marion MacFarlane

DOI
https://doi.org/10.1038/s41467-020-20806-9
Journal volume & issue
Vol. 12, no. 1
pp. 1 – 17

Abstract

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The core FADD:Caspase-8 complex and its regulatory partners, such as the cell death inhibitor c-FLIP, coordinate cell fate. Here authors present the structure of full-length procaspase-8 in a complex with FADD and reveal how recruitment of c-FLIPS into this complex inhibits Caspase-8 activity.