Ubiquitin-like proteins: new wines in new bottles

Gene. 2000 May 2;248(1-2):1-14. doi: 10.1016/s0378-1119(00)00139-6.


Ubiquitin is a small polypeptide that covalently modifies other cellular proteins and targets them to the proteasome for degradation. In recent years, ubiquitin-dependent proteolysis has been demonstrated to play a critical role in the regulation of many cellular processes, such as cell cycle progression, cell signaling, and immune recognition. The recent discovery of three new ubiquitin-like proteins, NEDD8, Sentrin/SUMO, and Apg12, has further broadened the horizon of this type of post-translational protein modification. This review will focus on the biology and biochemistry of the Sentrin/SUMO and NEDD8 modification pathways, which are clearly distinct from the ubiquitination pathway and have unique biological functions.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Cysteine Endopeptidases
  • Endopeptidases / metabolism
  • Humans
  • Molecular Sequence Data
  • NEDD8 Protein
  • Peptide Hydrolases*
  • Protein Processing, Post-Translational
  • SUMO-1 Protein
  • Sequence Homology, Amino Acid
  • Ubiquitins / genetics
  • Ubiquitins / metabolism*


  • NEDD8 Protein
  • NEDD8 protein, human
  • Nedd8 protein, mouse
  • SUMO-1 Protein
  • Ubiquitins
  • Endopeptidases
  • Peptide Hydrolases
  • SENP1 protein, human
  • Cysteine Endopeptidases
  • Senp3 protein, mouse