Inorganic phosphate export by the retrovirus receptor XPR1 in metazoans

Cell Rep. 2013 Jun 27;3(6):1866-73. doi: 10.1016/j.celrep.2013.05.035. Epub 2013 Jun 20.

Abstract

Inorganic phosphate uptake is a universal function accomplished by transporters that are present across the living world. In contrast, no phosphate exporter has ever been identified in metazoans. Here, we show that depletion of XPR1, a multipass membrane molecule initially identified as the cell-surface receptor for xenotropic and polytropic murine leukemia retroviruses (X- and P-MLV), induced a decrease in phosphate export and that reintroduction of various XPR1 proteins, from fruit fly to human, rescued this defect. Inhibition of phosphate export was also obtained with a soluble ligand generated from the envelope-receptor-binding domain of X-MLV in all human cell lines tested, as well as in diverse stem cells and epithelial cells derived from renal proximal tubules, the main site of phosphate homeostasis regulation. These results provide new insights on phosphate export in metazoans and the role of Xpr1 in this function.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • CHO Cells
  • Caco-2 Cells
  • Cricetulus
  • HEK293 Cells
  • HeLa Cells
  • Humans
  • Jurkat Cells
  • Mice
  • Models, Biological
  • Molecular Sequence Data
  • NIH 3T3 Cells
  • Phosphates / metabolism*
  • Receptors, G-Protein-Coupled / genetics
  • Receptors, G-Protein-Coupled / metabolism*
  • Receptors, Virus / genetics
  • Receptors, Virus / metabolism*
  • Species Specificity
  • Transfection
  • Xenotropic and Polytropic Retrovirus Receptor

Substances

  • Phosphates
  • Receptors, G-Protein-Coupled
  • Receptors, Virus
  • XPR1 protein, human
  • Xenotropic and Polytropic Retrovirus Receptor
  • Xpr1 protein, mouse

Associated data

  • GENBANK/KF007921