Proteasome-associated proteins: Regulation of a proteolytic machine

Marion Schmidt, John Hanna, Suzanne Elsasser, Daniel Finley

Research output: Contribution to journalReview article

135 Scopus citations

Abstract

The proteasome is a compartmentalized, ATP-dependent protease composed of more than 30 subunits that recognizes and degrades polyubiquitinated substrates. Despite its physiological importance, many aspects of the proteasome's structural organization and regulation remain poorly understood. In addition to the proteins that form the proteasome holocomplex, there is increasing evidence that proteasomal function is affected by a wide variety of associating proteins. A group of ubiquitin-binding proteins assist in delivery of substrates to the proteasome, whereas proteasome-associated ubiquitin ligases and deubiquitinating enzymes may alter the dynamics of ubiquitin chains already associated with the proteasome. Some proteins appear to influence the overall stability of the complex, and still others have the capacity to activate or inhibit the hydrolytic activity of the core particle. The increasing number of interacting proteins identified suggests that proteasomes, as they exist in the cell, are larger and more diverse in composition than previously assumed. Thus, the study of proteasome-associated proteins will lead to new perspectives on the dynamics of this uniquely complex proteolytic machine.

Original languageEnglish (US)
Pages (from-to)725-737
Number of pages13
JournalBiological Chemistry
Volume386
Issue number8
DOIs
StatePublished - Oct 24 2005

Keywords

  • Proteasome-associated proteins
  • Protein turnover
  • Regulation

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Clinical Biochemistry

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