Genetics, Vol. 159, 1491-1499, December 2001, Copyright © 2001

Phosphate Transport and Sensing in Saccharomyces cerevisiae

Dennis D. Wykoffa and Erin K. O'Sheaa
a Howard Hughes Medical Institute, Department of Biochemistry and Biophysics, University of California, San Francisco, California 94143

Corresponding author: Erin K. O'Shea, Howard Hughes Medical Institute, Department of Biochemisty and Biophysics, University of California, 513 Parnassus Ave., San Francisco, CA 94143-0448., oshea{at}biochem.ucsf.edu (E-mail)

Communicating editor: M. JOHNSTON

Cellular metabolism depends on the appropriate concentration of intracellular inorganic phosphate; however, little is known about how phosphate concentrations are sensed. The similarity of Pho84p, a high-affinity phosphate transporter in Saccharomyces cerevisiae, to the glucose sensors Snf3p and Rgt2p has led to the hypothesis that Pho84p is an inorganic phosphate sensor. Furthermore, pho84{Delta} strains have defects in phosphate signaling; they constitutively express PHO5, a phosphate starvation-inducible gene. We began these studies to determine the role of phosphate transporters in signaling phosphate starvation. Previous experiments demonstrated a defect in phosphate uptake in phosphate-starved pho84{Delta} cells; however, the pho84{Delta} strain expresses PHO5 constitutively when grown in phosphate-replete media. We determined that pho84{Delta} cells have a significant defect in phosphate uptake even when grown in high phosphate media. Overexpression of unrelated phosphate transporters or a glycerophosphoinositol transporter in the pho84{Delta} strain suppresses the PHO5 constitutive phenotype. These data suggest that PHO84 is not required for sensing phosphate. We further characterized putative phosphate transporters, identifying two new phosphate transporters, PHO90 and PHO91. A synthetic lethal phenotype was observed when five phosphate transporters were inactivated, and the contribution of each transporter to uptake in high phosphate conditions was determined. Finally, a PHO84-dependent compensation response was identified; the abundance of Pho84p at the plasma membrane increases in cells that are defective in other phosphate transporters.





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