The ubiquitin-proteasome system
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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.
KeywordsCellular proteolysis proteasomes protein degradation ubiquitination
ATPases associated with various cellular activities-ATPase
branched chain amino acids preferring
homologous to E6-AP carboxyl terminus
major histocompatibility complex
proteasome assembling chaperone
proteasome maturing protein
really interesting new gene
regulatory particle non-ATPase
regulatory particle tripleA-ATPase
small neutral amino acids preferring
ubiquitin mediated proteolysis-1
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