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      Ability of Sit4p to promote K+ efflux via Nha1p is modulated by Sap155p and Sap185p.

      Eukaryotic Cell

      metabolism, Adaptor Proteins, Signal Transducing, Carrier Proteins, Cation Transport Proteins, Fungal Proteins, Gene Deletion, Hygromycin B, pharmacology, Kinetics, Membrane Proteins, Phosphoprotein Phosphatases, Phosphoproteins, Potassium, Protein Phosphatase 2, Ribonucleoprotein, U2 Small Nuclear, Rubidium, Saccharomyces cerevisiae, drug effects, genetics, growth & development, Saccharomyces cerevisiae Proteins, Sodium-Hydrogen Antiporter, Transcription Factors

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          Abstract

          We demonstrate here that SAP155 encodes a negative modulator of K+ efflux in the yeast Saccharomyces cerevisiae. Overexpression of SAP155 decreases efflux, whereas deletion increases efflux. In contrast, a homolog of SAP155, called SAP185, encodes a positive modulator of K+ efflux: overexpression of SAP185 increases efflux, whereas deletion decreases efflux. Two other homologs, SAP4 and SAP190, are without effect on K+ homeostasis. Both SAP155 and SAP185 require the presence of SIT4 for function, which encodes a PP2A-like phosphatase important for the G1-S transition through the cell cycle. Overexpression of either the outwardly rectifying K+ channel, Tok1p, or the putative plasma membrane K+/H+ antiporter, Kha1p, increases efflux in both wild-type and sit4Delta strains. However, overexpression of the Na+-K+/H+ antiporter, Nha1p, is without effect in a sit4Delta strain, suggesting that Sit4p signals to Nha1p. In summary, the combined activities of Sap155p and Sap185p appear to control the function of Nha1p in K+ homeostasis via Sit4p.

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          Author and article information

          Journal
          15947196
          1151994
          10.1128/EC.4.6.1041-1049.2005

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