| dc.creator |
Yenush, Lynne |
|
| dc.creator |
Mulet, José M. |
|
| dc.creator |
Ariño, Joaquín |
|
| dc.creator |
Serrano, Ramón |
|
| dc.date |
2008-04-16T09:33:20Z |
|
| dc.date |
2008-04-16T09:33:20Z |
|
| dc.date |
2002 |
|
| dc.date.accessioned |
2017-01-31T01:02:26Z |
|
| dc.date.available |
2017-01-31T01:02:26Z |
|
| dc.identifier |
EMBO J. 2002 March 1; 21(5): 920–929 |
|
| dc.identifier |
1460-2075 |
|
| dc.identifier |
http://hdl.handle.net/10261/3612 |
|
| dc.identifier |
10.1093/emboj/21.5.920 |
|
| dc.identifier.uri |
http://dspace.mediu.edu.my:8181/xmlui/handle/10261/3612 |
|
| dc.description |
Final full-text version of the paper available at: http://www.nature.com/emboj/index.html |
|
| dc.description |
The yeast Ppz protein phosphatases and the Hal3p inhibitory subunit are important determinants of salt tolerance, cell wall integrity and cell cycle progression. We present several lines of evidence showing that these disparate phenotypes are connected by the fact that Ppz regulates K+ transport. First, salt tolerance, cell wall integrity and cell cycle phenotypes of Ppz mutants are dependent on the Trk K+ transporters. Secondly, Ppz mutants exhibit altered activity of the Trk system, as measured by rubidium uptake. Thirdly, Ppz mutants exhibit altered intracellular K+ and pH, as expected from H+ efflux providing electrical balance during K+ uptake. Our unifying picture of Ppz phenotypes contends that activation of Trk by decreased Ppz activity results in plasma membrane depolarization (reducing uptake of toxic cations), increased intracellular K+ and turgor (compromising cell integrity), and increased intracellular pH (augmenting the expression of pH-regulated genes and facilitating α-factor recovery). In addition to providing a coherent explanation for all Ppz-dependent phenotypes, our results provide evidence for a causal relationship between intracellular cation homeostasis and a potential cell cycle checkpoint. |
|
| dc.description |
L.Y. was supported by postdoctoral fellowships from the European Molecular Biology Organization and the National Science Foundation. J.M.M. was supported by a fellowship from the Conselleria de Educacio i Ciencia (Valencia). This work was supported by grants PB98-0565-C04-01 and PB98-0565-C04-02 from the Spanish Ministerio de Ciencia y Tecnología (Madrid). |
|
| dc.description |
Peer reviewed |
|
| dc.format |
314784 bytes |
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| dc.format |
application/pdf |
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| dc.language |
eng |
|
| dc.publisher |
Nature Publishing Group |
|
| dc.rights |
closedAccess |
|
| dc.subject |
Cell cycle |
|
| dc.subject |
Halotolerance |
|
| dc.subject |
pH |
|
| dc.subject |
Phosphatase |
|
| dc.subject |
Potassium |
|
| dc.title |
The Ppz protein phosphatases are key regulators of K+ and pH homeostasis: implications for salt tolerance, cell wall integrity and cell cycle progression |
|
| dc.type |
Artículo |
|