Constructing and decoding unconventional ubiquitin chains

Nat Struct Mol Biol. 2011 May;18(5):520-8. doi: 10.1038/nsmb.2066.


One of the most notable discoveries in the ubiquitin system during the past decade is the extensive use of diverse chain linkages to control signaling networks. Although the utility of Lys48- and Lys63-linked chains in protein turnover and molecular assembly, respectively, are well known, we are only beginning to understand how unconventional chain linkages are formed on target proteins and how such linkages are decoded by specific binding proteins. In this review, we summarize recent efforts to elucidate the machinery and mechanisms controlling assembly of Lys11-linked and linear (or Met1-linked) ubiquitin chains, and describe current models for how these chain types function in immune signaling and cell-cycle control.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Anaphase-Promoting Complex-Cyclosome
  • Animals
  • Cell Cycle
  • Humans
  • Lysine / chemistry
  • Mice
  • Models, Molecular
  • NF-kappa B / metabolism
  • Protein Structure, Tertiary
  • Signal Transduction*
  • Ubiquitin / chemistry*
  • Ubiquitin / metabolism
  • Ubiquitin / physiology
  • Ubiquitin-Conjugating Enzymes / chemistry
  • Ubiquitin-Conjugating Enzymes / physiology
  • Ubiquitin-Protein Ligase Complexes / chemistry
  • Ubiquitin-Protein Ligase Complexes / physiology
  • Ubiquitination


  • NF-kappa B
  • Ubiquitin
  • Ubiquitin-Conjugating Enzymes
  • Ubiquitin-Protein Ligase Complexes
  • Anaphase-Promoting Complex-Cyclosome
  • Lysine