ArticleScientific reports2019
Characterization of XPR1/SLC53A1 variants located outside of the SPX domain in patients with primary familial brain calcification.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 31 citations in OpenAlex.
- The SLC-ome of membrane transport: from molecular discovery to physiology and clinical applications.Physiological reviews · 2026Review
- Primary Brain Calcification Associated with a Novel XPR1 In-Frame Deletion: Clinical Characterization and Insights into Cerebellar and Basal Ganglia Contributions.Cerebellum (London, England) · 2026Article
- Structural insights into the gating mechanism of the fission yeast phosphate exporter SpXpr1.Cell discovery · 2026Article
- KIDINS220 and InsP8 safeguard the stepwise regulation of phosphate exporter XPR1.Molecular cell · 2025Article
- The identification of XPR1 as a voltage- and phosphate-activated phosphate-permeable ion channel.Nature communications · 2025Article
- Structure and function of human XPR1 in phosphate export.Nature communications · 2025Article
- Synergistic activation of the human phosphate exporter XPR1 by KIDINS220 and inositol pyrophosphate.Nature communications · 2025Article
- Transport and InsPNature communications · 2025Article
- Structural mechanism underlying PHO1;H1-mediated phosphate transport in Arabidopsis.Nature plants · 2025Article
- Structural basis of phosphate export by human XPR1.Nature communications · 2025Article
- Structural insights into the mechanism of phosphate recognition and transport by XPR1.Nature communications · 2025Article
- Article
- Upstream open reading frame-introducing variants in patients with primary familial brain calcification.European journal of human genetics : EJHG · 2024Article
- Primary Familial Brain Calcification WithJournal of clinical neurology (Seoul, Korea) · 2024Article
- The Genetics of Primary Familial Brain Calcification: A Literature Review.International journal of molecular sciences · 2023Review
- Inositol pyrophosphates activate the vacuolar transport chaperone complex in yeast by disrupting a homotypic SPX domain interaction.Nature communications · 2023Article
- Interplay between primary familial brain calcification-associated SLC20A2 and XPR1 phosphate transporters requires inositol polyphosphates for control of cellular phosphate homeostasis.The Journal of biological chemistry · 2020Article
- Control of XPR1-dependent cellular phosphate efflux by InsPProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Phosphate Transporter Profiles in Murine and Human Thymi Identify Thymocytes at Distinct Stages of Differentiation.Frontiers in immunology · 2020Article
- Basal ganglia calcifications (Fahr's syndrome): related conditions and clinical features.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2019Review
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11 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Primary familial brain calcification (PFBC) is a rare neurological disease characterized by deposits of calcium phosphate in the basal ganglia and other regions of the brain. Pathogenic variants in the XPR1/SLC53A1 gene, which encodes the only known inorganic phosphate exporter, cause an autosomal dominant form of PFBC. These variants are typically located in the SPX N-terminal domain of the protein. Here, we characterize three XPR1 variants outside of SPX in three PFBC patients with an apparently sporadic presentation: c.1375C > T p.(R459C), c.1855A > G p.(N619D) and c.1886T > G p.(I629S), with the latter identified as the first XPR1/SLC53A1 de novo mutation to occur in a PFBC proband. When tested in an in vitro physiological complementation assay, the three XPR1 variants were impaired in phosphate export function, although they were normally expressed at the cell surface and could serve as functional receptors for retrovirus entry. Moreover, peripheral blood cells from the p.N619D patient could be assayed ex vivo and displayed significantly impaired phosphate export. Our results establish for the first time the clinical and molecular characteristics of XPR1 variants located outside the SPX domain and assert a direct link between these variants, deficient phosphate export, and PFBC. Moreover, we unveiled new structural features in XPR1 C-terminal domain that play a role in phosphate export and disease.
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