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

  1. Author:
    Weissman, A. M.
    Shabek, N.
    Ciechanover, A.

  2. Author Address

    [Weissman, AM] NCI, Lab Prot Dynam & Signalling, Frederick, MD 21702 USA. [Shabek, N; Ciechanover, A] Technion Israel Inst Technol, Canc & Vasc Biol Res Ctr, Rappaport Fac Med, IL-31096 Haifa, Israel. [Shabek, N; Ciechanover, A] Technion Israel Inst Technol, Res Inst, IL-31096 Haifa, Israel.;Weissman, AM (reprint author), NCI, Lab Prot Dynam & Signalling, Frederick, MD 21702 USA;amw@nih.gov c_tzachy@netvision.net.il
    1. Year: 2011
    2. Date: Sep
  2. Journal: Nature Reviews Molecular Cell Biology
    1. 12
    2. 9
    3. Pages: 605-620
  4. Type of Article: Review
  5. ISSN: 1471-0072
  1. 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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External Sources

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  2. DOI: 10.1038/nrm3173
  3. View record in Web of Science®
  4. WOS: 000294164700014

Library Notes

  1. Fiscal Year: FY2011-2012
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