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The predator becomes the prey: regulating the ubiquitin system by ubiquitylation and degradation

Journal

NATURE REVIEWS MOLECULAR CELL BIOLOGY
Volume 12, Issue 9, Pages 605-620

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/nrm3173

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Funding

  1. US National Institutes of Health National Cancer Institute and Center for Cancer Research
  2. Miriam and Sheldon Adelson Foundation for Medical Research
  3. Israel Science Foundation
  4. German-Israeli Foundation for Research and Scientific Development
  5. Deutsch-Israelische Projektkooperation
  6. Rubicon - the European Union Network of Excellence

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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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