Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the proteasome and in the Ino80 chromatin-remodeling complex.

@article{Yao2008DistinctMO,
  title={Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the proteasome and in the Ino80 chromatin-remodeling complex.},
  author={Tingting Yao and Ling Song and Jingji Jin and Yong Cai and Hidehisa Takahashi and Selene K Swanson and Michael P Washburn and Laurence Florens and Ronald C. Conaway and Robert E Cohen and Joan W Conaway},
  journal={Molecular cell},
  year={2008},
  volume={31 6},
  pages={909-17}
}
Deubiquitinating enzymes (DUBs) are proteases that can antagonize ubiquitin-mediated signaling by disassembling ubiquitin-protein conjugates. How DUBs are regulated in vivo and how their substrate specificities are achieved are largely unknown. The conserved DUB Uch37 is found on proteasomes in organisms ranging from fission yeast to humans. Deubiquitination by Uch37 is activated by proteasomal binding, which enables Uch37 to process polyubiquitin chains. Here we show that in the nucleus Uch37… CONTINUE READING

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