The SPX domain of the yeast low-affinity phosphate transporter Pho90 regulates transport activity

Yeast has two phosphate‐uptake systems that complement each other: the high‐affinity transporters (Pho84 and Pho89) are active under phosphate starvation, whereas Pho87 and Pho90 are low‐affinity transporters that function when phosphate is abundant. Here, we report new regulatory functions of the a...

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Bibliographic Details
Published in:EMBO reports 2009-09, Vol.10 (9), p.1003-1008
Main Authors: Hürlimann, Hans Caspar, Pinson, Benoît, Stadler-Waibel, Martha, Zeeman, Samuel C, Freimoser, Florian M
Format: Article
Language:English
Subjects:
Biochemistry
Biological Transport
Chemical compounds
Cyclin-Dependent Kinase Inhibitor Proteins - genetics
Cyclin-Dependent Kinase Inhibitor Proteins - metabolism
EMBO20
EMBO21
Life Sciences
Metabolism
phosphate
Phosphate Transport Proteins - chemistry
Phosphate Transport Proteins - genetics
Phosphate Transport Proteins - metabolism
Phosphates
Phosphates - metabolism
Protein Binding
Protein Structure, Tertiary
Saccharomyces cerevisiae - chemistry
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Scientific Report
Signal transduction
SPX domain
transporter
Yeast
Yeasts
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Summary:Yeast has two phosphate‐uptake systems that complement each other: the high‐affinity transporters (Pho84 and Pho89) are active under phosphate starvation, whereas Pho87 and Pho90 are low‐affinity transporters that function when phosphate is abundant. Here, we report new regulatory functions of the amino‐terminal SPX domain of Pho87 and Pho90. By studying truncated versions of Pho87 and Pho90, we show that the SPX domain limits the phosphate‐uptake velocity, suppresses phosphate efflux and affects the regulation of the phosphate signal transduction pathway. Furthermore, split‐ubiquitin assays and co‐immunoprecipitation suggest that the SPX domain of both Pho90 and Pho87 interacts physically with the regulatory protein Spl2. This work suggests that the SPX domain inhibits low‐affinity phosphate transport through a physical interaction with Spl2.
ISSN:1469-221X
1469-3178
DOI:10.1038/embor.2009.105