![[Feedback]](/icons/banner/feedbackACT.gif){kind=icon}
![[For Subscribers]](/icons/banner/subscriberACT.gif){kind=icon}
![[Archive]](/icons/banner/archiveACT.gif){kind=icon}
![[Search]](/icons/banner/searchACT.gif){kind=icon}
![[Contents]](/icons/banner/tocACT.gif){kind=icon}
|
|
|
|
|
||
Vol. 17, Issue 11, 4645-4655, November 2006
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Institut de Biochimie et Génétique Cellulaires, Centre National de la Recherche Scientifique Unité Mixte de Recherche 5095, Université Victor Segalen/Bordeaux II, F-33077 Bordeaux Cedex, France
Submitted April 7, 2006;
Revised July 5, 2006;
Accepted August 8, 2006
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 Saccharomyces 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. Furthermore, 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.
The online version of this contains supplemental material at MBC Online (http://www.molbiolcell.org). This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E06-04-0282) on August 16, 2006.
Address correspondence to: Isabelle Sagot (isabelle.sagot{at}ibgc.u-bordeaux2.fr)
Abbreviations used: ABP, actin-binding protein; Lat-A, lantrunculin A
This article has been cited by other articles:
|
|
 |
|
  S. L. Holland and S. V. Avery Actin-Mediated Endocytosis Limits Intracellular Cr Accumulation and Cr Toxicity during Chromate Stress Toxicol. Sci., October 1, 2009; 111(2): 437 - 446. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. Narayanaswamy, M. Levy, M. Tsechansky, G. M. Stovall, J. D. O'Connell, J. Mirrielees, A. D. Ellington, and E. M. Marcotte Widespread reorganization of metabolic enzymes into reversible assemblies upon nutrient starvation PNAS, June 23, 2009; 106(25): 10147 - 10152. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S.-W. Chiu, S.-Y. Chen, and H.-c. Wong Localization and Expression of MreB in Vibrio parahaemolyticus under Different Stresses Appl. Envir. Microbiol., November 15, 2008; 74(22): 7016 - 7022. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. Laporte, B. Salin, B. Daignan-Fornier, and I. Sagot Reversible cytoplasmic localization of the proteasome in quiescent yeast cells J. Cell Biol., October 20, 2008; 181(5): 737 - 745. [Abstract] [Full Text] [PDF]
|
|
