Scientific Report
- EMBO reports (2009) 10, 1003 - 1008
- doi:10.1038/embor.2009.105
Published online: 10 July 2009
Subject Categories:
The SPX domain of the yeast low-affinity phosphate transporter Pho90 regulates transport activityEMBO Open
Hans Caspar Hürlimann1,*, Benoît Pinson2,3,*, Martha Stadler-Waibel1, Samuel C Zeeman1 & Florian M Freimoser1
- Institute of Plant Sciences, ETH Zurich, Universitätstrasse 2, 8092 Zurich, Switzerland
- Institut de Biochimie et Génétique Cellulaires, 1 Rue C. Saint-Saëns, Université Victor Segalen/Bordeaux 2, 33077 Bordeaux, France
- CNRS—UMR5095, Bordeaux, France
Correspondence to:
Florian M Freimoser,
Tel: +41 44 632 38 44; Fax: +41 44 632 10 44;
E-mail: ffreimoser@ethz.ch
*These authors contributed equally to this work
Received 17 November 2008; Revised 9 April 2009; Accepted 20 April 2009
Abstract
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.
Keywords:
- metabolism,
- phosphate,
- SPX domain,
- transporter,
- yeast
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