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Vol. 13, Issue 8, 2771-2782, August 2002





and
¶
*Department of Anatomy and Cell Biology, Faculty of Medicine,
University of Cantabria, 39011 Santander, Spain;
Nuclear bodies represent a heterogeneous class of nuclear
structures. Herein, we describe that a subset 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 the PML
protein. We propose that clastosomes are sites where proteolysis
of a variety of protein substrates is taking place.
Department of Biochemistry, Faculty of Medicine,
Autonomous University of Madrid, 28029 Madrid, Spain;
§Center for Cancer Biology, University of Rochester
Medical Center, Rochester, New York 14642; and
Institute
of Molecular Medicine, Faculty of Medicine, University of Lisbon,
Lisbon, Portugal
These authors contributed equally to this work.
¶
Corresponding author. E-mail address:
carmo.fonseca{at}fm.ul.pt.
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