Journal of Biosciences

, Volume 31, Issue 1, pp 137–155 | Cite as

The ubiquitin-proteasome system

  • Dipankar NandiEmail author
  • Pankaj Tahiliani
  • Anujith Kumar
  • Dilip Chandu


The 2004 Nobel Prize in chemistry for the discovery of protein ubiquitination has led to the recognition of cellular proteolysis as a central area of research in biology. Eukaryotic proteins targeted for degradation by this pathway are first ‘tagged’ by multimers of a protein known as ubiquitin and are later proteolyzed by a giant enzyme known as the proteasome. This article recounts the key observations that led to the discovery of ubiquitin-proteasome system (UPS). In addition, different aspects of proteasome biology are highlighted. Finally, some key roles of the UPS in different areas of biology and the use of inhibitors of this pathway as possible drug targets are discussed.


Cellular proteolysis proteasomes protein degradation ubiquitination 

Abbreviations used


ATPases associated with various cellular activities-ATPase


branched chain amino acids preferring


COP9 signalosome


endoplasmic reticulum


homologous to E6-AP carboxyl terminus




major histocompatibility complex


N-terminal nucleophile


proteasome activator


proteasome assembling chaperone


proteasome-activating nucleotidase


proteasome inhibitor


proteasome maturing protein


really interesting new gene


regulatory particle non-ATPase


regulatory particle tripleA-ATPase


Skp-Cullin-F box


small neutral amino acids preferring


ubiquitin hydrolase


ubiqutin processing


ubiquitin mediated proteolysis-1


ubiquitin-proteasome system


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Copyright information

© Indian Academy of Sciences 2006

Authors and Affiliations

  • Dipankar Nandi
    • 1
    Email author
  • Pankaj Tahiliani
    • 1
  • Anujith Kumar
    • 1
  • Dilip Chandu
    • 1
  1. 1.Department of BiochemistryIndian Institute of ScienceBangaloreIndia

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