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The Intracellular Localization of the Proteasome

  • C. Gordon
Part of the Current Topics in Microbiology and Immunology book series (CT MICROBIOLOGY, volume 268)

Abstract

Proteasomes are large multiprotein complexes which constitute the main non-lysosomal (non-vacuolar in yeast) mechanism to degrade intracellular proteins. One major function of proteasomes is to degrade proteins that have been targeted for destruction by the ubiquitin pathway. By determining the levels of key regulatory proteins the proteasome plays a critical role in many different biological processes, such as cell cycle proliferation, development, apoptosis and antigen presentation (Hershko and Ciechanover 1998; Voges et al. 1999). The proteasome is also responsible for degrading other proteins independently of the ubiquitin pathway. Misfolded proteins and ornithine decarboxylase are examples of proteins that do not require the addition of a polyubiquitin signal for proteolysis by the proteasome to occur (Strickland et al. 2000; Coffino 2001).

Keywords

Green Fluorescent Protein Fission Yeast Nuclear Periphery Green Fluorescent Protein Signal Ubiquitin Pathway 
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

  • C. Gordon
    • 1
  1. 1.MRC Human Genetics UnitWestern General HospitalEdinburghUK

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