Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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DED Interaction of FADD and Caspase-8 in the Induction of Apoptotic Cell Death

  • Park, Young-Hoon (Department of Molecular Biology, College of Natural Sciences, Pusan National University) ;
  • Han, Chang Woo (Department of Molecular Biology, College of Natural Sciences, Pusan National University) ;
  • Jeong, Mi Suk (Department of Molecular Biology, College of Natural Sciences, Pusan National University) ;
  • Jang, Se Bok (Department of Molecular Biology, College of Natural Sciences, Pusan National University)
  • Received : 2022.06.06
  • Accepted : 2022.07.19
  • Published : 2022.08.28
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Abstract

Fas-associated death domain (FADD) is an adapter molecule that bridges the interaction between receptor-interacting protein 1 (RIP1) and aspartate-specific cysteine protease-8 (caspase-8). As the primary mediator of apoptotic cell death, caspase-8 has two N-terminal death-effector domains (DEDs) and it interacts with other proteins in the DED subfamily through several conserved residues. In the tumor necrosis receptor-1 (TNFR-1)-dependent signaling pathway, apoptosis is triggered by the caspase-8/FADD complex by stimulating receptor internalization. However, the molecular mechanism of complex formation by the DED proteins remains poorly understood. Here, we found that direct DED-DED interaction between FADD and caspase-8 and the structure-based mutations (Y8D/I128A, E12A/I128A, E12R/I128A, K39A/I128A, K39D/I128A, F122A/I128A, and L123A/I128A) of caspase-8 disrupted formation of the stable DED complex with FADD. Moreover, the monomeric crystal structure of the caspase-8 DEDs (F122A/I128A) was solved at 1.7 Å. This study will provide new insight into the interaction mechanism and structural characteristics between FADD and caspase-8 DED subfamily proteins.

Keywords

Acknowledgement

Diffraction data were collected at the Pohang Light Source (PLS-7A), Republic of Korea. This study was supported by the Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science and Technology (2018R1D1A1B07043701) to S.B.J. and (2016R1D1A1B02011142) to M.S.J. This work was also supported by a National Research Foundation of Korea (NRF) grant funded by the Korean government (MSIT) (Grant No. 2021R1C1C2004755 to C. W. H.)

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