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Updated: May 10, 2026

Reporter-based Growth Assay for Systematic Analysis of Protein Degradation
Published on: November 6, 2014
The predator becomes the prey: regulating the ubiquitin system by ubiquitylation and degradation
Allan M Weissman1, Nitzan Shabek, Aaron Ciechanover
1Laboratory of Protein Dynamics and Signalling, National Cancer Institute, Frederick, Maryland 21702, USA. amw@nih.gov
Abstract:
Ubiquitylation (also known as ubiquitination) regulates essentially all of the intracellular processes in eukaryotes through highly specific modification of numerous cellular proteins, which is often tightly regulated in a spatial and temporal manner. Although most often associated with proteasomal degradation, ubiquitylation frequently serves non-proteolytic functions. In light of its central roles in cellular regulation, it has not been surprising to find that many of the components of the ubiquitin system itself are regulated by ubiquitylation. This observation has broad implications for pathophysiology.
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