Proteasomes: destruction as a programme

Trends Biochem Sci. 1996 Mar;21(3):96-102.

Abstract

Proteasomes are large multi-subunit protease complexes that selectively degrade intracellular proteins. Most of the proteins removed by these proteases are tagged for destruction by ubiquitination. Proteasomes have a role to play in controlling cellular processes, such as metabolism and the cell cycle, through signal-mediated proteolysis of key enzymes and regulatory proteins. They also operate in the stress response, by removing abnormal proteins, and in the immune response, by generating antigenic peptides.

Publication types

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

MeSH terms

  • Animals
  • Antigen Presentation
  • Cell Cycle
  • Cysteine Endopeptidases / chemistry
  • Cysteine Endopeptidases / genetics
  • Cysteine Endopeptidases / metabolism
  • Cysteine Endopeptidases / physiology*
  • Humans
  • Immunity
  • Models, Molecular
  • Multienzyme Complexes / chemistry
  • Multienzyme Complexes / genetics
  • Multienzyme Complexes / metabolism
  • Multienzyme Complexes / physiology*
  • Proteasome Endopeptidase Complex
  • Proteins / metabolism*
  • Stress, Physiological
  • Ubiquitins / metabolism

Substances

  • Multienzyme Complexes
  • Proteins
  • Ubiquitins
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex