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Published online May 26, 2008
doi:10.1083/jcb.200711154
The Journal of Cell Biology, Vol. 181, No. 5, 737-745
The Rockefeller University Press, 0021-9525 $30.00
© 2008 Laporte et al.
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 Reversible cytoplasmic localization of the proteasome in quiescent yeast cells

Damien Laporte1,2, Bénédicte Salin1,2, Bertrand Daignan-Fornier1,2, and Isabelle Sagot1,2

1 Institut de Biochimie et Génétique Cellulaires, Université Victor Segalen Bordeaux II, 33077 Bordeaux, France
2 Centre National de la Recherche Scientifique, UMR5095 Bordeaux, France

Correspondence to Isabelle Sagot: isabelle.sagot{at}ibgc.u-bordeaux2.fr

The 26S proteasome is responsible for the controlled proteolysis of a vast number of proteins, including crucial cell cycle regulators. Accordingly, in Saccharomyces cerevisiae, 26S proteasome function is mandatory for cell cycle progression. In budding yeast, the 26S proteasome is assembled in the nucleus, where it is localized throughout the cell cycle. We report that upon cell entry into quiescence, proteasome subunits massively relocalize from the nucleus into motile cytoplasmic structures. We further demonstrate that these structures are proteasome cytoplasmic reservoirs that are rapidly mobilized upon exit from quiescence. Therefore, we have named these previously unknown structures proteasome storage granules (PSGs). Finally, we observe conserved formation and mobilization of these PSGs in the evolutionary distant yeast Schizosaccharomyces pombe. This conservation implies a broad significance for these proteasome reserves.

Abbreviations used in this paper: CP, core particle; PSG, proteasome storage granule; RP, regulatory particle.


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