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The Ubiquitin Code

Annual Review of Biochemistry · 2012 · Vol. 81(1) · pp. 203–229
David KomanderMichael Rapé

Abstract

The posttranslational modification with ubiquitin, a process referred to as ubiquitylation, controls almost every process in cells. Ubiquitin can be attached to substrate proteins as a single moiety or in the form of polymeric chains in which successive ubiquitin molecules are connected through specific isopeptide bonds. Reminiscent of a code, the various ubiquitin modifications adopt distinct conformations and lead to different outcomes in cells. Here, we discuss the structure, assembly, and function of this ubiquitin code.

Ubiquitin and proteasome pathwaysAutophagy in Disease and TherapyCancer-related Molecular PathwaysUbiquitinMoietyFunction (biology)ChemistryDeubiquitinating enzymeUbiquitin-Protein LigasesUbiquitin ligaseCell biologyBiochemistryComputational biology

MeSH terms

AnimalsHumansProtein Processing, Post-TranslationalProteinsUbiquitin-Conjugating EnzymesUbiquitin-Activating EnzymesUbiquitin-Protein LigasesUbiquitination

Funding

  • Harvard University
  • National Institutes of Health
  • Medical Research Council
Citations
3,574
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References
Mechanisms Underlying Ubiquitination
Annual Review of Biochemistry · 2001 · 3,700 citations
Recognition of the polyubiquitin proteolytic signal
The EMBO Journal · 2000 · 1,686 citations
PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
Nature Cell Biology · 2010 · 2,752 citations
Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome
Annual Review of Biochemistry · 2009 · 1,764 citations
Breaking the chains: structure and function of the deubiquitinases
Nature Reviews Molecular Cell Biology · 2009 · 2,081 citations
RING Domain E3 Ubiquitin Ligases
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