USP8 suppresses death receptor-mediated apoptosis by enhancing FLIPL stability

@article{Jeong2017USP8SD,
  title={USP8 suppresses death receptor-mediated apoptosis by enhancing FLIPL stability},
  author={Manhyung Jeong and E-W Lee and Daehyeon Seong and Jung Youn Seo and Ji Hoon Kim and Sasker Grootjans and So-Yun Kim and Peter Vandenabeele and Jaewhan Song},
  journal={Oncogene},
  year={2017},
  volume={36},
  pages={458-470}
}
FLICE-like inhibitory protein (FLIP) is a critical regulator of death receptor-mediated apoptosis. Here, we found ubiquitin-specific peptidase 8 (USP8) to be a novel deubiquitylase of the long isoform of FLIP (FLIPL). USP8 directly deubiquitylates and stabilizes FLIPL, but not the short isoform. USP8 depletion induces FLIPL destabilization, promoting anti-Fas-, tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)- and tumor necrosis factor alpha-induced extrinsic apoptosis by… CONTINUE READING

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