The putative polyamine transporter Shp2 facilitates phosphate export in an Xpr1-independent manner and contributes to high phosphate tolerance.

ABSTRACT: Phosphate (Pi) homeostasis at the cellular level is crucial, requiring coordinated Pi uptake, storage, and export. However, the regulatory mechanisms, particularly those governing Pi export, remain elusive, despite their relevance to human diseases like primary familial brain calcification. While Xpr1, conserved across eukaryotes, is the only known Pi exporter, the existence of additional Pi exporting factors is evident; however, these factors have been poorly characterized. Using the fission yeast Schizosaccharomyces pombe as a model, we have aimed to better understand cellular Pi homeostasis mechanisms. Previously, we showed three Pi regulators with SPX domains to be critical: Pqr1 (Pi uptake restrictor), Xpr1/Spx2, and the VTC complex (polyphosphate synthase). SPX domains bind to inosit

SUBMITTER: Komamura T 

PROVIDER: S-EPMC11742622 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature