The novel functions of ubiquitination in signaling

Lijun Sun, Zhijian J. Chen

Research output: Contribution to journalArticle

343 Citations (Scopus)

Abstract

Ubiquitin is best known for its function in targeting proteins for degradation by the proteasome. Recent studies have revealed several new functions of ubiquitin that are independent of proteasomal degradation. These functions include the novel signaling roles of ubiquitin in DNA repair and the activation of protein kinases such as IκB kinase. In both cases, a novel form of polyubiquitin chain linked through lysine-63 of ubiquitin plays an important regulatory role. Monoubiquitination also has signaling roles that are distinct from those of polyubiquitination, as illustrated from the studies of DNA repair. Thus, polyubiquitination and monoubiquitination have emerged as important signaling mechanisms that control diverse physiological and pathological processes.

Original languageEnglish (US)
Pages (from-to)119-126
Number of pages8
JournalCurrent Opinion in Cell Biology
Volume16
Issue number2
DOIs
StatePublished - Apr 2004

Fingerprint

Ubiquitination
Ubiquitin
DNA Repair
Polyubiquitin
Physiological Phenomena
Proteasome Endopeptidase Complex
Pathologic Processes
Protein Kinases
Proteolysis
Lysine
Phosphotransferases

Keywords

  • deubiquitination enzyme
  • Dub
  • FA
  • Fanconi Anemia
  • PolyUb
  • polyubiquitin
  • TLR
  • Toll-like receptor
  • Ub
  • ubiquitin
  • ubiquitin-specific protease
  • UBP

ASJC Scopus subject areas

  • Cell Biology

Cite this

The novel functions of ubiquitination in signaling. / Sun, Lijun; Chen, Zhijian J.

In: Current Opinion in Cell Biology, Vol. 16, No. 2, 04.2004, p. 119-126.

Research output: Contribution to journalArticle

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