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A unified mechanism of phosphate export across eukaryotes through EXS domain-containing proteins.

Created on 07 Jul 2026

Authors

Ghazanfar Abbas Khan, Elycia Calvet, Jean-Luc Battini, Yves Poirier

Published in

Trends in biochemical sciences. Jul 06, 2026. Epub Jul 06, 2026.

Abstract

Inorganic phosphate (Pi) is an essential macronutrient, and tight regulation of Pi import and export is required to maintain Pi homeostasis. Although Pi import mechanisms have been extensively characterized, the molecular basis of Pi export has only recently begun to emerge. Arabidopsis PHOSPHATE 1 (PHO1) and its homologue PHO1;H1 are prototypical members of the SPX [Syg1/PHO81/xenotropic and polytropic retrovirus receptor 1 (XPR1)]-EXS (ERD1/XPR1/SYG1) family of Pi exporters conserved throughout eukaryotes, including the metazoan orthologue XPR1 and fungal SYG1. We review recent structural studies redefining XPR1 and PHO1;H1 Pi transporters as channel-like proteins using a double-lock gating mechanism controlled by inositol pyrophosphates. This new knowledge enhances our ability to modulate the activity of SPX-EXS proteins involved in human diseases, such as cancer, as well as enhance phosphate-use efficiency in crops.

PMID:
42409659
Bibliographic data and abstract were imported from PubMed on 07 Jul 2026.

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