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Eukaryotic Cell, October 2006, p. 1611-1621, Vol. 5, No. 10
1535-9778/06/$08.00+0     doi:10.1128/EC.00215-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Gis4, a New Component of the Ion Homeostasis System in the Yeast Saccharomyces cerevisiae{dagger}

Tian Ye,1 Raúl García-Salcedo,2 José Ramos,2 and Stefan Hohmann1*

Department of Cell and Molecular Biology/Microbiology, Göteborg University, Box 462, S-40530 Göteborg, Sweden,1 Departamento de Microbiología, Universidad de Córdoba, Campus Universitario de Rabanales, Edif. Severo Ochoa, 14071 Córdoba, Spain2

Received 10 July 2006/ Accepted 22 July 2006

Gis4 is a new component of the system required for acquisition of salt tolerance in Saccharomyces cerevisiae. The gis4{Delta} mutant is sensitive to Na+ and Li+ ions but not to osmotic stress. Genetic evidence suggests that Gis4 mediates its function in salt tolerance, at least partly, together with the Snf1 protein kinase and in parallel with the calcineurin protein phosphatase. When exposed to salt stress, mutants lacking gis4{Delta} display a defect in maintaining low intracellular levels of Na+ and Li+ ions and exporting those ions from the cell. This defect is due to diminished expression of the ENA1 gene, which encodes the Na+ and Li+ export pump. The protein sequence of Gis4 is poorly conserved and does not reveal any hints to its molecular function. Gis4 is enriched at the cell surface, probably due to C-terminal farnesylation. The CAAX box at the C terminus is required for cell surface localization but does not seem to be strictly essential for the function of Gis4 in salt tolerance. Gis4 and Snf1 seem to share functions in the control of ion homeostasis and ENA1 expression but not in glucose derepression, the best known role of Snf1. Together with additional evidence that links Gis4 genetically and physically to Snf1, it appears that Gis4 may function in a pathway in which Snf1 plays a specific role in controlling ion homeostasis. Hence, it appears that the conserved Snf1 kinase plays roles in different pathways controlling nutrient as well as stress response.

* Corresponding author. Mailing address: Department of Cell and Molecular Biology/Microbiology, Göteborg University, Box 462, S-40530 Göteborg, Sweden. Phone: 46 31 360 8488. Fax: 46 31 773 2599. E-mail: hohmann{at}gmm.gu.se.

{dagger} Supplemental material for this article may be found at http://ec.asm.org/.

Eukaryotic Cell, October 2006, p. 1611-1621, Vol. 5, No. 10
1535-9778/06/$08.00+0     doi:10.1128/EC.00215-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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  • Melamed, D., Pnueli, L., Arava, Y. (2008). Yeast translational response to high salinity: Global analysis reveals regulation at multiple levels. RNA 14: 1337-1351 [Abstract] [Full Text]  
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