Pyrophosphate Stimulates the Phosphate-Sodium Symporter of <italic toggle="yes">Trypanosoma brucei</italic> Acidocalcisomes and <italic toggle="yes">Saccharomyces cerevisiae</italic> Vacuoles

ABSTRACT Inorganic pyrophosphate (PPi) is a by-product of biosynthetic reactions and has bioenergetic and regulatory roles in a variety of cells. Here we show that PPi and other pyrophosphate-containing compounds, including polyphosphate (polyP), can stimulate sodium-dependent depolarization of the...

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Autores principales: Evgeniy Potapenko, Ciro D. Cordeiro, Guozhong Huang, Roberto Docampo
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Publicado: American Society for Microbiology 2019
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spelling oai:doaj.org-article:8406d6ebc9084f0c9049b7819072ecab2021-11-15T15:22:21ZPyrophosphate Stimulates the Phosphate-Sodium Symporter of <italic toggle="yes">Trypanosoma brucei</italic> Acidocalcisomes and <italic toggle="yes">Saccharomyces cerevisiae</italic> Vacuoles10.1128/mSphere.00045-192379-5042https://doaj.org/article/8406d6ebc9084f0c9049b7819072ecab2019-04-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mSphere.00045-19https://doaj.org/toc/2379-5042ABSTRACT Inorganic pyrophosphate (PPi) is a by-product of biosynthetic reactions and has bioenergetic and regulatory roles in a variety of cells. Here we show that PPi and other pyrophosphate-containing compounds, including polyphosphate (polyP), can stimulate sodium-dependent depolarization of the membrane potential and Pi conductance in Xenopus oocytes expressing a Saccharomyces cerevisiae or Trypanosoma brucei Na+/Pi symporter. PPi is not taken up by Xenopus oocytes, and deletion of the TbPho91 SPX domain abolished its depolarizing effect. PPi generated outward currents in Na+/Pi-loaded giant vacuoles prepared from wild-type or pho91Δ yeast strains expressing TbPHO91 but not from the pho91Δ strains. Our results suggest that PPi, at physiological concentrations, can function as a signaling molecule releasing Pi from S. cerevisiae vacuoles and T. brucei acidocalcisomes. IMPORTANCE Acidocalcisomes, first described in trypanosomes and known to be present in a variety of cells, have similarities with S. cerevisiae vacuoles in their structure and composition. Both organelles share a Na+/Pi symporter involved in Pi release to the cytosol, where it is needed for biosynthetic reactions. Here we show that PPi, at physiological cytosolic concentrations, stimulates the symporter expressed in either Xenopus oocytes or yeast vacuoles via its SPX domain, revealing a signaling role of this molecule.Evgeniy PotapenkoCiro D. CordeiroGuozhong HuangRoberto DocampoAmerican Society for MicrobiologyarticleSPX domainSaccharomyces cerevisiaeTrypanosoma bruceiXenopus laevisacidocalcisomephosphate-sodium symporterMicrobiologyQR1-502ENmSphere, Vol 4, Iss 2 (2019)
institution DOAJ
collection DOAJ
language EN
topic SPX domain
Saccharomyces cerevisiae
Trypanosoma brucei
Xenopus laevis
acidocalcisome
phosphate-sodium symporter
Microbiology
QR1-502
spellingShingle SPX domain
Saccharomyces cerevisiae
Trypanosoma brucei
Xenopus laevis
acidocalcisome
phosphate-sodium symporter
Microbiology
QR1-502
Evgeniy Potapenko
Ciro D. Cordeiro
Guozhong Huang
Roberto Docampo
Pyrophosphate Stimulates the Phosphate-Sodium Symporter of <italic toggle="yes">Trypanosoma brucei</italic> Acidocalcisomes and <italic toggle="yes">Saccharomyces cerevisiae</italic> Vacuoles
description ABSTRACT Inorganic pyrophosphate (PPi) is a by-product of biosynthetic reactions and has bioenergetic and regulatory roles in a variety of cells. Here we show that PPi and other pyrophosphate-containing compounds, including polyphosphate (polyP), can stimulate sodium-dependent depolarization of the membrane potential and Pi conductance in Xenopus oocytes expressing a Saccharomyces cerevisiae or Trypanosoma brucei Na+/Pi symporter. PPi is not taken up by Xenopus oocytes, and deletion of the TbPho91 SPX domain abolished its depolarizing effect. PPi generated outward currents in Na+/Pi-loaded giant vacuoles prepared from wild-type or pho91Δ yeast strains expressing TbPHO91 but not from the pho91Δ strains. Our results suggest that PPi, at physiological concentrations, can function as a signaling molecule releasing Pi from S. cerevisiae vacuoles and T. brucei acidocalcisomes. IMPORTANCE Acidocalcisomes, first described in trypanosomes and known to be present in a variety of cells, have similarities with S. cerevisiae vacuoles in their structure and composition. Both organelles share a Na+/Pi symporter involved in Pi release to the cytosol, where it is needed for biosynthetic reactions. Here we show that PPi, at physiological cytosolic concentrations, stimulates the symporter expressed in either Xenopus oocytes or yeast vacuoles via its SPX domain, revealing a signaling role of this molecule.
format article
author Evgeniy Potapenko
Ciro D. Cordeiro
Guozhong Huang
Roberto Docampo
author_facet Evgeniy Potapenko
Ciro D. Cordeiro
Guozhong Huang
Roberto Docampo
author_sort Evgeniy Potapenko
title Pyrophosphate Stimulates the Phosphate-Sodium Symporter of <italic toggle="yes">Trypanosoma brucei</italic> Acidocalcisomes and <italic toggle="yes">Saccharomyces cerevisiae</italic> Vacuoles
title_short Pyrophosphate Stimulates the Phosphate-Sodium Symporter of <italic toggle="yes">Trypanosoma brucei</italic> Acidocalcisomes and <italic toggle="yes">Saccharomyces cerevisiae</italic> Vacuoles
title_full Pyrophosphate Stimulates the Phosphate-Sodium Symporter of <italic toggle="yes">Trypanosoma brucei</italic> Acidocalcisomes and <italic toggle="yes">Saccharomyces cerevisiae</italic> Vacuoles
title_fullStr Pyrophosphate Stimulates the Phosphate-Sodium Symporter of <italic toggle="yes">Trypanosoma brucei</italic> Acidocalcisomes and <italic toggle="yes">Saccharomyces cerevisiae</italic> Vacuoles
title_full_unstemmed Pyrophosphate Stimulates the Phosphate-Sodium Symporter of <italic toggle="yes">Trypanosoma brucei</italic> Acidocalcisomes and <italic toggle="yes">Saccharomyces cerevisiae</italic> Vacuoles
title_sort pyrophosphate stimulates the phosphate-sodium symporter of <italic toggle="yes">trypanosoma brucei</italic> acidocalcisomes and <italic toggle="yes">saccharomyces cerevisiae</italic> vacuoles
publisher American Society for Microbiology
publishDate 2019
url https://doaj.org/article/8406d6ebc9084f0c9049b7819072ecab
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