Dimerization and ubiquitin mediated recruitment of A20, a complex deubiquitinating enzyme.

@article{Lu2013DimerizationAU,
  title={Dimerization and ubiquitin mediated recruitment of A20, a complex deubiquitinating enzyme.},
  author={Timothy T Lu and Michio Onizawa and Gianna Elena Hammer and Emre E. Turer and Qian Yin and Ermelinda Damko and Alexander Agelidis and Nataliya Shifrin and Rommel Advincula and Julio Barrera and Barbara A Malynn and Hao Wu and Averil Ma},
  journal={Immunity},
  year={2013},
  volume={38 5},
  pages={
          896-905
        }
}
A20 is an anti-inflammatory protein linked to multiple human autoimmune diseases and lymphomas. A20 possesses a deubiquitinating motif and a zinc finger, ZF4, that binds ubiquitin and supports its E3 ubiquitin ligase activity. To understand how these activities mediate A20's physiological functions, we generated two lines of gene-targeted mice, abrogating either A20's deubiquitinating activity (Tnfaip3(OTU) mice) or A20's ZF4 (Tnfaip3(ZF4) mice). Both Tnfaip3(OTU) and Tnfaip3(ZF4) mice… CONTINUE READING

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Dimerization and Ubiquitin Mediated Recruitment of A20, a Complex Deubiquitinating Enzyme, Immunity

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  • 2013