Ubiquitin: not just for proteasomes anymore

Curr Opin Cell Biol. 2003 Apr;15(2):184-90. doi: 10.1016/s0955-0674(03)00010-3.

Abstract

Ubiquitin is a small protein that can be covalently linked to itself or other proteins, either as single ubiquitin molecules or as chains of polyubiquitin. Addition of ubiquitin to a target protein requires a series of enzymatic activities (by ubiquitin-activating, -conjugating and -ligating enzymes). The first function attributed to ubiquitin was the covalent modification of misfolded cytoplasmic proteins, thereby directing proteasome-dependent proteolysis. More recently, additional functions have been ascribed to ubiquitin and ubiquitin-related proteins. Ubiquitin directs specific proteins through the endocytic pathway by modifying cargo proteins, and possibly also components of the cytoplasmic protein trafficking machinery.

Publication types

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

MeSH terms

  • Active Transport, Cell Nucleus / physiology
  • Animals
  • Cysteine Endopeptidases / metabolism*
  • Endocytosis / physiology
  • Eukaryotic Cells / metabolism*
  • Humans
  • Multienzyme Complexes / metabolism*
  • Peptide Hydrolases / metabolism*
  • Proteasome Endopeptidase Complex
  • Protein Transport / physiology*
  • Receptors, Cell Surface / physiology
  • Ubiquitin / metabolism*

Substances

  • Multienzyme Complexes
  • Receptors, Cell Surface
  • Ubiquitin
  • Peptide Hydrolases
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex