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MBC in Press, published online ahead of print August 16, 2006
Mol. Biol. Cell 10.1091/mbc.E06-04-0282

A more recent version of this article appeared on November 1, 2006
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Submitted on April 7, 2006
Revised on July 5, 2006
Accepted on August 8, 2006

Actin Bodies in Yeast Quiescent Cells: An Immediately Available Actin Reserve?

Isabelle Sagot, Benoît Pinson, Bénédicte Salin, and Bertrand Daignan-Fornier

Institut de Biochimie et Génétique Cellulaires, Centre National de la Recherche Scientifique UMR 5095, Université Victor Segalen/Bordeaux II, F-33077 Bordeaux Cedex, France

Monitoring Editor: Fred Chang

Most eukaryotic cells spend most of their life in a quiescent state, poised to respond to specific signals to proliferate. In the case of S. cerevisiae, entry into and exit from quiescence are dependent only on the availability of nutrients in the environment. The transition from quiescence to proliferation requires not only drastic metabolic changes but also a complete remodeling of various cellular structures. Here, we describe an actin cytoskeleton organization specific of the yeast quiescent state. When cells cease to divide, actin is reorganized into structures that we named "actin bodies". We show that actin bodies contain F-actin and several actin binding proteins such as fimbrin and capping protein. Further, by contrast to actin patches or cables, actin bodies are mostly immobile and we could not detect any actin filament turnover. Finally, we show that upon cells refeeding, actin bodies rapidly disappear and actin cables and patches can be assembled in the absence of de novo protein synthesis. This led us to propose that actin bodies are a reserve of actin that can be immediately mobilized for actin cables and patches formation upon reentry into a proliferation cycle.

Address correspondence to: Isabelle Sagot (isabelle.sagot{at}ibgc.u-bordeaux2.fr)




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D. Laporte, B. Salin, B. Daignan-Fornier, and I. Sagot
Reversible cytoplasmic localization of the proteasome in quiescent yeast cells
J. Cell Biol., May 28, 2008; 181(5): 737 - 745.
[Abstract] [Full Text] [PDF]


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