The novel functions of ubiquitination in signaling

Curr Opin Cell Biol. 2004 Apr;16(2):119-26. doi: 10.1016/j.ceb.2004.02.005.

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 IkappaB 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • DNA Repair / genetics
  • Humans
  • I-kappa B Kinase
  • Polymers / metabolism
  • Protein Processing, Post-Translational / physiology*
  • Protein-Serine-Threonine Kinases / metabolism
  • Proteins / metabolism*
  • Signal Transduction / physiology*
  • Ubiquitin / metabolism*

Substances

  • Polymers
  • Proteins
  • Ubiquitin
  • Protein-Serine-Threonine Kinases
  • CHUK protein, human
  • I-kappa B Kinase
  • IKBKB protein, human
  • IKBKE protein, human