Encyclopedia of Cancer

Living Edition
| Editors: Manfred Schwab


  • Joseph F. Maher
Living reference work entry
DOI: https://doi.org/10.1007/978-3-642-27841-9_4788-2



The proteasome is a large molecular proteolytic machine, responsible for most regulated protein degradation within cells. The proteasome functions, along with protein ubiquitination, within the ubiquitin-proteasome system (UPS), although there are also ubiquitin-independent functions of the proteasome.

The proteasome performs ATP-dependent protein degradation in the contexts of protein turnover, in quality control of misfolded proteins, and in the tight control of key regulatory proteins for important cellular processes. The proteasome can also perform more discrete, regulatory protease cleavages of target proteins, rather than degradation, modifying the activity of the cleaved protein. There is a...


Proteasomal Degradation Cancer Cachexia Skeletal Muscle Protein Regulatory Particle Hereditary Cancer Syndrome 
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  1. Archer TK (ed) (2011) The 26S proteasome: when degradation is just not enough! Biochimica et Biophysica Acta (BBA) – Gene Regulatory Mechanisms. 1809(2):65–156 (multiple review articles on non-degradative functions of the proteasome)Google Scholar
  2. Bader M, Steller H (2009) Regulation of cell death by the ubiquitin-proteasome system. Curr Opin Cell Biol 21:878–884CrossRefPubMedPubMedCentralGoogle Scholar
  3. Ebstein F, Kloetzel PM, Krüger E, Seifert U (2012) Emerging roles of immunoproteasomes beyond MHC class I antigen processing. Cell Mol Life Sci 69:2543–2558CrossRefPubMedGoogle Scholar
  4. Erales J, Coffino P (2014) Ubiquitin-independent proteasomal degradation. Biochim Biophys Acta 1843:216–221CrossRefPubMedGoogle Scholar
  5. Fearon KC, Glass DJ, Guttridge DC (2012) Cancer cachexia: mediators, signaling, and metabolic pathways. Cell Metab 16:153–166CrossRefPubMedGoogle Scholar
  6. Grigoreva TA, Tribulovich VG, Garabadzhiu AV, Melino G, Barlev NA (2015) The 26S proteasome is a multifaceted target for anti-cancer therapies. Oncotarget 6:24733–24749CrossRefPubMedPubMedCentralGoogle Scholar
  7. Hanahan D, Weinberg RA (2011) Hallmarks of cancer: the next generation. Cell 144:646–674CrossRefPubMedGoogle Scholar
  8. Kouranti I, Peyroche A (2012) Protein degradation in DNA damage response. Semin Cell Dev Biol 23:538–545CrossRefPubMedGoogle Scholar
  9. Navon A, Ciechanover A (2009) The 26S proteasome: from basic mechanisms to drug targeting. J Biol Chem 284:33713–33718CrossRefPubMedPubMedCentralGoogle Scholar
  10. Voutsadakis IA (2012) The ubiquitin-proteasome system and signal transduction pathways regulating Epithelial Mesenchymal transition of cancer. J Biomed Sci 19:67 (pp 1–13)CrossRefPubMedPubMedCentralGoogle Scholar
  11. Yang Y, Li CC, Weissman AM (2004) Regulating the p53 system through ubiquitination. Oncogene 23:2096–2106CrossRefPubMedGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2015

Authors and Affiliations

  1. 1.Cancer InstituteUniversity of Mississippi Medical CenterJacksonUSA