Phosphorylation-dependent activity of the deubiquitinase DUBA

  title={Phosphorylation-dependent activity of the deubiquitinase DUBA},
  author={Oscar W. Huang and Xiaolei Ma and Jianping Yin and Jeremy Flinders and Till Maurer and Nobuhiko Kayagaki and Qui T. Phung and Ivan Bosanac and David Arnott and Vishva M. Dixit and Sarah G. Hymowitz and Melissa A. Starovasnik and Andrea G Cochran},
  journal={Nature Structural &Molecular Biology},
Addition and removal of ubiquitin or ubiquitin chains to and from proteins is a tightly regulated process that contributes to cellular signaling and protein stability. Here we show that phosphorylation of the human deubiquitinase DUBA (OTUD5) at a single residue, Ser177, is both necessary and sufficient to activate the enzyme. The crystal structure of the ubiquitin aldehyde adduct of active DUBA reveals a marked cooperation between phosphorylation and substrate binding. An intricate web of… CONTINUE READING


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