4.6 Review

RIP1 comes back to life as a cell death regulator in TNFR1 signaling

Journal

FEBS JOURNAL
Volume 278, Issue 6, Pages 877-887

Publisher

WILEY-BLACKWELL
DOI: 10.1111/j.1742-4658.2011.08016.x

Keywords

apoptosis; caspase; IAP; necrosis; NEMO; NF-kappa B; RIP; TNF; TRAF; ubiquitin

Funding

  1. NIH [AI052417]
  2. Crohn's and Colitis Foundation of America

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Cell death induction by tumor necrosis factor has been an intensively studied area for the last two decades. Although it may appear that the skeleton should have been picked clean by now, new secrets about tumor necrosis factor death signaling are still being uncovered. In particular, the recent evidence that ubiquitination of the death kinase receptor-interacting protein 1 regulates its participation in apoptotic and necrotic cell death is opening up unexplored avenues in the catacombs of tumor necrosis factor death signaling. In this minireview, we focus on two major cell-death checkpoints that determine whether receptor-interacting protein 1 functions as a pro-survival or pro-death molecule.

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