Molecular Biology of the Cell Call for Nominations: MBC Editor-in-Chief

Home Help [Feedback] [For Subscribers] [Archive] [Search] --
QUICK SEARCH:   [advanced]


     

MBC in Press, published online ahead of print August 15, 2007
Mol. Biol. Cell 10.1091/mbc.E06-12-1141

A more recent version of this article appeared on October 1, 2007
This Article
Right arrow Full Text (PDF)
Right arrow Supplemental Material
Right arrow All Versions of this Article:
E06-12-1141v1
18/10/4168    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by George, V. T.
Right arrow Articles by Humphrey, T. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by George, V. T.
Right arrow Articles by Humphrey, T. C.

Submitted on December 21, 2006
Revised on July 31, 2007
Accepted on August 6, 2007

Regulation of Cell Cycle and Stress Responses to Hydrostatic Pressure in Fission Yeast

Vinoj T. George,* Gavin Brooks,{dagger} and Timothy C. Humphrey*

*Medical Research Council Radiation Oncology and Biology Unit, Harwell, Didcot, Oxfordshire, OX11 0RD, United Kingdom; {dagger}Cardiovascular Research Group, School of Pharmacy, University of Reading, Reading, Berkshire, RG6 6AP, United Kingdom

Monitoring Editor: Daniel Lew

We have investigated the cellular responses to hydrostatic pressure using the fission yeast Schizosaccharomyces pombe as a model system. Exposure to sublethal levels of hydrostatic pressure resulted in G2 cell cycle delay. This delay resulted from Cdc2 tyrosine-15 (Y-15) phosphorylation, and was abrogated by simultaneous disruption of the Cdc2 kinase regulators, Cdc25 and Wee1. However, cell cycle delay was independent of the DNA damage, cytokinesis and cell size checkpoints, suggesting a novel mechanism of Cdc2-Y15 phosphorylation in response to hydrostatic pressure. Spc1/Sty1 mitogen activated protein (MAP) kinase, a conserved member of the eukaryotic stress-activated p38 MAP kinase family, was rapidly activated following pressure stress, and was required for cell cycle recovery under these conditions, in part through promoting polo kinase (Plo1) phosphorylation on serine 402. Moreover, the Spc1 MAP kinase pathway played a key role in maintaining cell viability under hydrostatic pressure stress through the bZip transcription factor, Atf1. Further analysis revealed that pre-stressing cells with heat increased barotolerance, suggesting adaptational cross-talk between these stress responses. These findings provide new insights into eukaryotic homeostasis following exposure to pressure stress.

Address correspondence to: Timothy C. Humphrey (T.Humphrey{at}har.mrc.ac.uk)






Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Copyright © 2007 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.