Plasma-membrane hyperpolarization diminishes the cation efflux via Nha1 antiporter and Ena ATPase under potassium-limiting conditions
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F12%3A00377369" target="_blank" >RIV/67985823:_____/12:00377369 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1111/j.1567-1364.2012.00793.x" target="_blank" >http://dx.doi.org/10.1111/j.1567-1364.2012.00793.x</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1111/j.1567-1364.2012.00793.x" target="_blank" >10.1111/j.1567-1364.2012.00793.x</a>
Alternative languages
Result language
angličtina
Original language name
Plasma-membrane hyperpolarization diminishes the cation efflux via Nha1 antiporter and Ena ATPase under potassium-limiting conditions
Original language description
A series of experiments with strains lacking various combinations of potassium efflux and uptake systems revealed that all three potassium exporting systems, the Nha1 antiporter, Ena ATPase and Tok1 channel contribute to potassium homeostasis and are active upon potassium limitation in wild-type cells. In trk1 delta trk2 delta mutants, the potassium efflux via potassium exporters Nha1 and Ena1 is diminished and can be restored either by the expression of TRK1 or deletion of TOK1. In both cases, the relative hyperpolarization of trk1 delta trk2 delta cells is decreased. Thus it is the plasma-membrane potential which serves as the common mechanism regulating the activity of K+ exporting systems
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EE - Microbiology, virology
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2012
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
FEMS Yeast Research
ISSN
1567-1356
e-ISSN
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Volume of the periodical
12
Issue of the periodical within the volume
4
Country of publishing house
US - UNITED STATES
Number of pages
8
Pages from-to
439-446
UT code for WoS article
000306187400006
EID of the result in the Scopus database
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