Regulatory proteins of the proteasome

G. N. DeMartino, C. A. Slaughter

Research output: Contribution to journalReview article

42 Scopus citations

Abstract

The function of the proteasome is controlled by a variety of specific regulatory proteins including activators, inhibitors, and modulators. Two recently discovered activators, termed PA28 and PA700, bind to the terminal rings of the proteasome to form proteasome-regulator complexes which display greatly increased proteolytic activity. PA28 is a high-affinity activator of the proteasome's multiple peptidase activities. The carboxyl terminus of PA28 is required for its binding to the proteasome. PA700 binds to the proteasome via an ATP-dependent mechanism. PA700 has ATPase activity, and at least four of PA700's 16 subunits are members of a protein family containing a concensus sequence for ATP binding. Proteasome-PA700 complexes are activated with respect to both the hydrolysis of peptide substrates and the hydrolysis of ubiquitinated proteins.

Original languageEnglish (US)
Pages (from-to)314-324
Number of pages11
JournalEnzyme and Protein
Volume47
Issue number4-6
DOIs
StatePublished - Jan 1 1993

Keywords

  • ATPase
  • Activators
  • PA28
  • PA700
  • Proteasome
  • Regulators

ASJC Scopus subject areas

  • Biochemistry

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