The Lysine48-Based polyubiquitin chain proteasomal signal

Not a single child anymore

Yelena Kravtsova-Ivantsiv, Thomas Sommer, Aaron Ciechanover

Research output: Contribution to journalReview articleResearchpeer-review

30 Citations (Scopus)

Abstract

The conjugation of ubiquitin (Ub) to proteins is involved in the regulation of many processes. The modification serves as a recognition element in trans, in which downstream effectors bind to the modified protein and determine its fate and/or function. A polyUb chain that is linked through internal lysine(Lys)-48 of Ub and anchored to an internal Lys residue of the substrate has become the accepted "canonical" signal for proteasomal targeting and degradation. However, recent studies show that the signal is far more diverse and that chains based on other internal linkages, as well as linear or heterologous chains made of Ub and Ub-like proteins and even monoUb, are recognized by the proteasome. In addition, chains linked to residues other than internal Lys were described, all challenging the current paradigm.

Original languageEnglish
Pages (from-to)192-198
Number of pages7
JournalAngewandte Chemie - International Edition
Volume52
Issue number1
DOIs
StatePublished - 2 Jan 2013

Fingerprint

Polyubiquitin
Ubiquitin
Lysine
Proteins
Ubiquitins
Proteasome Endopeptidase Complex
Degradation
Substrates

Keywords

  • Monoubiquitination
  • Polyubiquitin chains
  • Proteasome
  • Protein degradation
  • Ubiquitin

Cite this

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The Lysine48-Based polyubiquitin chain proteasomal signal : Not a single child anymore. / Kravtsova-Ivantsiv, Yelena; Sommer, Thomas; Ciechanover, Aaron.

In: Angewandte Chemie - International Edition, Vol. 52, No. 1, 02.01.2013, p. 192-198.

Research output: Contribution to journalReview articleResearchpeer-review

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