Binding of OTULIN to the PUB domain of HOIP controls NF-κB signaling.

@article{Schaeffer2014BindingOO,
  title={Binding of OTULIN to the PUB domain of HOIP controls NF-κB signaling.},
  author={V{\'e}ronique Schaeffer and Masato Akutsu and Michael Hans Olma and Ligia C. Gomes and Masato Kawasaki and Ivan Dikic},
  journal={Molecular cell},
  year={2014},
  volume={54 3},
  pages={349-61}
}
Linear ubiquitin chains are implicated in the regulation of the NF-κB pathway, immunity, and inflammation. They are synthesized by the LUBAC complex containing the catalytic subunit HOIL-1-interacting protein (HOIP) and are disassembled by the linear ubiquitin-specific deubiquitinase OTULIN. Little is known about the regulation of these opposing activities. Here we demonstrate that HOIP and OTULIN interact and act as a bimolecular editing pair for linear ubiquitin signals in vivo. The HOIP PUB… CONTINUE READING
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