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Solution structure of c-FLIP death effector domains.

Zhi-Qiang Bai1, Xiaofang Ma2, Bin Liu3

  • 1State Key Laboratory of Phytochemistry and Plant Resources in West China, Kunming Institute of Botany, Chinese Academy of Sciences, 132 Lanhei Road, Heilongtan, Kunming, 650201, Yunnan, China; Innovative Institute of Chinese Medicine and Pharmacy, Chengdu University of Traditional Chinese Medicine, Chengdu, 611137, China; University of Chinese Academy of Sciences, Beijing, 100049, China.

Biochemical and Biophysical Research Communications
|June 10, 2022
PubMed
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We determined the structure of c-FLIP tandem death effector domains (tDED) using NMR. This structure is similar to procaspase-8 tDED, revealing how c-FLIP regulates cell death signaling.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Cell Death Research

Background:

  • Extrinsic apoptosis is initiated by the death-inducing signaling complex (DISC) and death effector domain (DED) filament.
  • Cellular FLICE-inhibitory protein (c-FLIP) regulates procaspase-8 recruitment and activation at the DISC via its tandem DEDs (tDED).
  • The structural basis for c-FLIP's interaction with procaspase-8 and its mechanism of inhibiting apoptosis remain unclear.

Purpose of the Study:

  • To elucidate the structure of c-FLIPtDED.
  • To understand the molecular mechanisms by which c-FLIP regulates procaspase-8 activation and extrinsic apoptosis.

Main Methods:

  • Solution nuclear magnetic resonance (NMR) spectroscopy was used to determine the monomeric structure of c-FLIPtDED (F114G).
  • Structural superimposition was performed to compare c-FLIPtDED with procaspase-8tDED.

Main Results:

  • The monomeric structure of c-FLIPtDED (F114G) was solved at near physiological pH.
  • Structural analysis revealed that c-FLIPtDED shares a similar structural topology with procaspase-8tDED.

Conclusions:

  • The determined structure provides a structural basis for understanding the interaction between c-FLIP and procaspase-8.
  • These findings offer insights into the molecular mechanisms of c-FLIP in modulating cell death pathways.