Ubiquitin and ubiquitin-like proteins in protein regulation

Research output: Contribution to journalArticle

201 Citations (Scopus)

Abstract

The discovery of the ubiquitin system was awarded with the Nobel Prize in Chemistry in 2004. Labeling of intracellular proteins for degradation by a multienzymatic complex, called the proteasome, was identified as the main function of this system. Subsequently, it was discovered that the attachment of ubiquitin to proteins can modify their function without degradation. Finally, a number of other molecules were recognized to be conjugated to proteins in a manner similar to ubiquitin and were henceforth called ubiquitin-like proteins. This review provides an overview of this class of molecules and its implication for function, subcellular location, and half-life of proteins.

Original languageEnglish (US)
Pages (from-to)1276-1291
Number of pages16
JournalCirculation Research
Volume100
Issue number9
DOIs
StatePublished - May 2007

Fingerprint

Ubiquitins
Ubiquitin
Nobel Prize
Proteins
Proteasome Endopeptidase Complex
Proteolysis
Half-Life

Keywords

  • Cell cycle
  • Inflammation
  • Metabolism
  • Protein
  • Ubiquitin
  • Ubiquitin-like proteins

ASJC Scopus subject areas

  • Physiology
  • Cardiology and Cardiovascular Medicine

Cite this

Ubiquitin and ubiquitin-like proteins in protein regulation. / Herrmann, Joerg; Lerman, Lilach O; Lerman, Amir.

In: Circulation Research, Vol. 100, No. 9, 05.2007, p. 1276-1291.

Research output: Contribution to journalArticle

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