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Cleavage of the C-terminus of NEDD8 by UCH-L3.

NEDD8 is a novel ubiquitin-like protein that has been shown to conjugate to nuclear proteins in a manner analogous to ubiquitination and sentrinization. To identify proteins that are involved in the NEDD8-conjugation and de-conjugation pathway, the yeast two-hybrid system was used to screen a human heart cDNA library using NEDD8 as a bait. Seven strongly positive clones were found to contain a cDNA insert encoding the ubiquitin C-terminal hydrolase, UCH-L3. In vitro GST pull-down assay demonstrated that UCH-L3 bound to both NEDD8 and ubiquitin. In contrast, UCH-L3 did not bind to sentrin-1, sentrin-2, or sentrin-3. Recombinant UCH-L3, but not UCH-L1, was able to cleave the C-terminus of NEDD8. Thus, UCH-L3 can function as a C-terminal hydrolase for both NEDD8 and ubiquitin. UCH-L3 may play a physiologically significant role in the cleavage of the C-terminus of NEDD8, which is required for NEDD8 to conjugate to target proteins.

Pubmed ID: 9790970


  • Wada H
  • Kito K
  • Caskey LS
  • Yeh ET
  • Kamitani T


Biochemical and biophysical research communications

Publication Data

October 29, 1998

Associated Grants

  • Agency: NHLBI NIH HHS, Id: HL-45851

Mesh Terms

  • Down-Regulation
  • Gene Library
  • Humans
  • Hydrolysis
  • Peptide Fragments
  • Protein Binding
  • Protein Processing, Post-Translational
  • Saccharomyces cerevisiae
  • Selection, Genetic
  • Thiolester Hydrolases
  • Tissue Distribution
  • Ubiquitin Thiolesterase
  • Ubiquitins