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ABIN-1 is a ubiquitin sensor that restricts cell death and sustains embryonic development

Shigeru Oshima1, Emre E Turer, Joseph A Callahan

  • 1Department of Medicine, University of California at San Francisco, 513 Parnassus Avenue, S-1057, San Francisco, California 94143-0451, USA.

Nature
|December 9, 2008
PubMed

Insights

ABIN-1 protein deficiency causes embryonic death by increasing sensitivity to tumor necrosis factor (TNF)-induced cell death. ABIN-1

Area of Science:

  • Molecular Biology
  • Immunology
  • Developmental Biology

Background:

  • Tumor necrosis factor receptor (TNFR) signaling proteins are crucial for cellular activation and survival.
  • ABIN-1 (A20 binding and inhibitor of NF-kappaB) is a protein implicated in inhibiting NF-kappaB signaling.

Purpose of the Study:

  • To investigate the in vivo function of ABIN-1 in embryonic development and cellular survival.
  • To elucidate the mechanism by which ABIN-1 regulates tumor necrosis factor (TNF)-induced programmed cell death.

Main Methods:

  • Generation and analysis of ABIN-1 deficient mice.
  • Assessment of cellular sensitivity to TNF-induced apoptosis.
  • Investigation of ABIN-1's role in TNF signaling complexes and caspase 8 recruitment.
  • Analysis of ABIN-1's interaction with polyubiquitin chains.

Main Results:

  • ABIN-1 deficient mice exhibit embryonic lethality due to fetal liver apoptosis, anemia, and hypoplasia.
  • ABIN-1 deficient cells show hypersensitivity to TNF-induced programmed cell death, which is rescued by TNF deficiency.
  • ABIN-1 inhibits caspase 8 recruitment to FADD in TNF signaling complexes, preventing apoptosis.
  • ABIN-1's anti-apoptotic activity depends on its ability to bind polyubiquitin chains.

Conclusions:

  • ABIN-1 is essential for embryonic survival, regulating TNF-induced apoptosis.
  • ABIN-1 acts by preventing caspase 8 activation through polyubiquitin binding.
  • These findings highlight the critical role of ubiquitination and ubiquitin sensing in organismal survival.

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