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Regulating the 26S Proteasome

  • M. H. Glickman
  • V. Maytal
Part of the Current Topics in Microbiology and Immunology book series (CT MICROBIOLOGY, volume 268)

Abstract

Numerous regulatory pathways are regulated by timely removal of critical proteins. These include proteins involved in the cell cycle, transcriptional regulation, DNA repair, development and differentiation, long-term memory, circadian rhythms, stress response, transcriptional silencing, cell-surface signaling, antigen presentation, and in combating cancer or viral infection (Hershko and Ciechanover 1998; Spataro et al. 1998; Ciechanover et al. 2000). Other proteins that must be degraded properly are damaged, abnormal, or foreign (viral) proteins. Remarkably, in eukaryotes, almost all such proteins are degraded in an ATP-dependent manner by a single, highly conserved, 2.5MDa multisubunit enzyme, the proteasome (Voges et al. 1999; Ferrell et al. 2000; Glickman 2000). The majority of substrates for degradation are first covalently attached to a chain of multiple ubiquitin molecules — a highly conserved 76 amino acid protein — recognized by the proteasome, and hydrolyzed into short peptides (Hershko and Ciechanover 1998; Ciechanover et al. 2000; Kornitzer and Ciechanover 2000; Wilkinson 2000).

Keywords

Major Histocompatibility Complex Class Core Particle Polyubiquitin Chain Regulatory Particle Multiubiquitin Chain 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 2002

Authors and Affiliations

  • M. H. Glickman
    • 1
  • V. Maytal
    • 2
  1. 1.Department of BiologyThe Technion, Israel Institute of TechnologyHaifaIsrael
  2. 2.Institute for Catalysis (ICST)The Technion, Israel Institute of TechnologyHaifaIsrael

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