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A more recent version of this article appeared on August 1, 2002
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Submitted on March 4, 2002
Revised on April 7, 2002
Accepted on May 7, 2002
1 Department of Anatomy and Cell Biology, Faculty of Medicine, University of Cantabria, 39011 Santander, Spain
2 Department of Biochemistry, Faculty of Medicine, Autonomous University of Madrid, 28029 Madrid, Spain
3 Center for Cancer Biology, University of Rochester Medical Center, Rochester, NY 14642, USA
4 Institute of Molecular Medicine, Faculty of Medicine, University of Lisbon, Portugal
* Corresponding author. E-mail address: carmo.fonseca{at}fm.ul.pt.
Nuclear bodies represent a heterogeneous class of nuclear structures. Here we describe that a sub-set of nuclear bodies is highly enriched in components of the ubiquitin-proteasome pathway of proteolysis. We coined the term clastosome (from the Greek Klastos, broken and Soma, body) to refer to this type of nuclear body. Clastosomes contain a high concentration of (1) ubiquitin conjugates, (2) the proteolytically active 20S core and the 19S regulatory complexes of the 26S proteasome, and (3) protein substrates of the proteasome. Although detected in a variety of cell types, clastosomes are scarce under normal conditions; however, they become more abundant when proteasomal activity is stimulated. In contrast, clastosomes disappear when cells are treated with proteasome inhibitors. Protein substrates of the proteasome that are found concentrated in clastosomes include the short-lived transcription factors c-Fos and c-Jun, adenovirus E1A proteins, and PML. We propose that clastosomes are sites where proteolysis of a variety of protein substrates is taking place.
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