Component

XPR1 (human phosphate exporter)

XPR1 (human phosphate exporter). Species, exposure and limitations are retained in each linked claim.

8 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

How nutrients influence it

Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.

How nutrients reach it in more than one step

Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.

Tracing routes…

What it does

Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.

Recorded relationships

What it acts on

  1. XPR1 or PPIP5K knockout reduced phosphate export and accelerated the mineralization endpoint in Saos-2 cells.

    XPR1 (human phosphate exporter) → Saos-2 cell mineralization source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/inositol-research/32019887.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bb7637b9a327b1cba07716bbed5da8a3f32a3ac00c9fff70d23ada1a736d3d18", "start_char": 0, "end_char": 2004, "text_sha256": "bb7637b9a327b1cba07716bbed5da8a3f32a3ac00c9fff70d23ada1a736d3d18"}
    experimental_model
    Binding, knockout and rescue experiments
    exposure
    PPIP5K or XPR1 deletion, kinase rescue and pyrophosphate analog delivery
    limitations
    Cell assays establish a transport-regulation mechanism, not benefits of oral inositol or increased bone mineralization.
    nutrient_topic
    Inositol research collection; topical membership is not evidence of a direct dietary effect. · Inositol (stereoisomer family)
    organism
    Human cultured cells including Saos-2 osteosarcoma cells
    plain_language
    Retaining phosphate changed mineral deposition in a bone-tumor cell model.
    primary_references
    [ino-p32019887] Control of XPR1-dependent cellular phosphate efflux by InsP8 is an exemplar for functionally-exclusive inositol pyrophosphate signaling. (2020). https://pubmed.ncbi.nlm.nih.gov/32019887/ DOI: 10.1073/pnas.1908830117
    tissue_or_cell_type
    Cellular phosphate transport
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 912–923

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Binding, knockout and rescue experiments · source_derived_draft · unverified_draft

    ### ino-xpr1-mineralization XPR1 or PPIP5K knockout reduced phosphate export and accelerated the mineralization endpoint in Saos-2 cells. Condition category: machinery_impairment nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: Retaining phosphate changed mineral deposition in a bone-tumor cell model. organism: Human cultured cells including Saos-2 osteosarcoma cells tissue_or_cell_type: Cellular phosphate transport experimental_model: Binding, knockout and rescue experiments limitations: Cell assays establish a transport-regulation mechanism, not benefits of oral inositol or increased bone mineralization. exposure: PPIP5K or XPR1 deletion, kinase rescue and pyrophosphate analog delivery evidence_span: {"source_cache": "artifacts/inositol-research/32019887.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bb7637b9a327b1cba07716bbed5da8a3f32a3ac00c9fff70d23ada1a736d3d18", "start_char": 0, "end_char": 2004, "text_sha256": "bb7637b9a327b1cba07716bbed5da8a3f32a3ac00c9fff70d23ada1a736d3d18"} [ino-p32019887] Control of XPR1-dependent cellular phosphate efflux by InsP8 is an exemplar for functionally-exclusive inositol pyrophosphate signaling. (2020). https://pubmed.ncbi.nlm.nih.gov/32019887/ DOI: 10.1073/pnas.1908830117
    Complete structured claim and evidence

  2. The study reported later XPR1-dependent modulation of PiT1 turnover, resetting phosphate uptake after the earlier efflux response.

    XPR1 (human phosphate exporter) → Human PiT1 protein turnover source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/phosphorus-research/38833370.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5c093accfcc7194268c0fbd19d3ee39aae4206e9b2feed48b76b2a95eee33b78", "start_char": 0, "end_char": 1103, "text_sha256": "5c093accfcc7194268c0fbd19d3ee39aae4206e9b2feed48b76b2a95eee33b78"}
    experimental_model
    Protein interaction, localization and phosphate-challenge cell experiments
    exposure
    Genetic manipulation and pharmacological mimic of phosphate homeostatic challenge
    limitations
    Temporal regulatory model in cultured cells; endogenous InsP8 signaling is not equivalent to taking an inositol or phytate supplement.
    nutrient_topic
    Phosphorus research collection; topical membership is not evidence of a direct dietary effect. · Phosphorus
    organism
    Human cultured HCT116, U2OS and Saos-2 systems
    plain_language
    Changing transporter turnover adjusted how much phosphate entered later.
    primary_references
    [phosphorus-p38833370] Homeostatic coordination of cellular phosphate uptake and efflux requires an organelle-based receptor for the inositol pyrophosphate IP8. (2024). https://pubmed.ncbi.nlm.nih.gov/38833370/ DOI: 10.1016/j.celrep.2024.114316
    tissue_or_cell_type
    Cellular phosphate uptake/export and LAMP1-positive puncta

    Phosphorus: metabolism, signaling and nutrient connections (2026-09-17) · lines 763–774

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Protein interaction, localization and phosphate-challenge cell experiments · source_derived_draft · unverified_draft

    ### phosphorus-ip8-uptake The study reported later XPR1-dependent modulation of PiT1 turnover, resetting phosphate uptake after the earlier efflux response. Condition category: normal nutrient_topic: Phosphorus research collection; topical membership is not evidence of a direct dietary effect. plain_language: Changing transporter turnover adjusted how much phosphate entered later. organism: Human cultured HCT116, U2OS and Saos-2 systems tissue_or_cell_type: Cellular phosphate uptake/export and LAMP1-positive puncta experimental_model: Protein interaction, localization and phosphate-challenge cell experiments limitations: Temporal regulatory model in cultured cells; endogenous InsP8 signaling is not equivalent to taking an inositol or phytate supplement. exposure: Genetic manipulation and pharmacological mimic of phosphate homeostatic challenge evidence_span: {"source_cache": "artifacts/phosphorus-research/38833370.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5c093accfcc7194268c0fbd19d3ee39aae4206e9b2feed48b76b2a95eee33b78", "start_char": 0, "end_char": 1103, "text_sha256": "5c093accfcc7194268c0fbd19d3ee39aae4206e9b2feed48b76b2a95eee33b78"} [phosphorus-p38833370] Homeostatic coordination of cellular phosphate uptake and efflux requires an organelle-based receptor for the inositol pyrophosphate IP8. (2024). https://pubmed.ncbi.nlm.nih.gov/38833370/ DOI: 10.1016/j.celrep.2024.114316
    Complete structured claim and evidence

  3. XPR1 localized to a subset of intracellular LAMP1-positive puncta designated XLPVs.

    XPR1 (human phosphate exporter) → Human XPR1 localization in LAMP1-positive intracellular puncta source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/phosphorus-research/38833370.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5c093accfcc7194268c0fbd19d3ee39aae4206e9b2feed48b76b2a95eee33b78", "start_char": 0, "end_char": 1103, "text_sha256": "5c093accfcc7194268c0fbd19d3ee39aae4206e9b2feed48b76b2a95eee33b78"}
    experimental_model
    Protein interaction, localization and phosphate-challenge cell experiments
    exposure
    Genetic manipulation and pharmacological mimic of phosphate homeostatic challenge
    limitations
    Temporal regulatory model in cultured cells; endogenous InsP8 signaling is not equivalent to taking an inositol or phytate supplement.
    nutrient_topic
    Phosphorus research collection; topical membership is not evidence of a direct dietary effect. · Phosphorus
    organism
    Human cultured HCT116, U2OS and Saos-2 systems
    plain_language
    Some of the control system operated in an intracellular compartment.
    primary_references
    [phosphorus-p38833370] Homeostatic coordination of cellular phosphate uptake and efflux requires an organelle-based receptor for the inositol pyrophosphate IP8. (2024). https://pubmed.ncbi.nlm.nih.gov/38833370/ DOI: 10.1016/j.celrep.2024.114316
    tissue_or_cell_type
    Cellular phosphate uptake/export and LAMP1-positive puncta

    Phosphorus: metabolism, signaling and nutrient connections (2026-09-17) · lines 737–748

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Protein interaction, localization and phosphate-challenge cell experiments · source_derived_draft · unverified_draft

    ### phosphorus-xpr1-location XPR1 localized to a subset of intracellular LAMP1-positive puncta designated XLPVs. Condition category: normal nutrient_topic: Phosphorus research collection; topical membership is not evidence of a direct dietary effect. plain_language: Some of the control system operated in an intracellular compartment. organism: Human cultured HCT116, U2OS and Saos-2 systems tissue_or_cell_type: Cellular phosphate uptake/export and LAMP1-positive puncta experimental_model: Protein interaction, localization and phosphate-challenge cell experiments limitations: Temporal regulatory model in cultured cells; endogenous InsP8 signaling is not equivalent to taking an inositol or phytate supplement. exposure: Genetic manipulation and pharmacological mimic of phosphate homeostatic challenge evidence_span: {"source_cache": "artifacts/phosphorus-research/38833370.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5c093accfcc7194268c0fbd19d3ee39aae4206e9b2feed48b76b2a95eee33b78", "start_char": 0, "end_char": 1103, "text_sha256": "5c093accfcc7194268c0fbd19d3ee39aae4206e9b2feed48b76b2a95eee33b78"} [phosphorus-p38833370] Homeostatic coordination of cellular phosphate uptake and efflux requires an organelle-based receptor for the inositol pyrophosphate IP8. (2024). https://pubmed.ncbi.nlm.nih.gov/38833370/ DOI: 10.1016/j.celrep.2024.114316
    Complete structured claim and evidence

  4. XPR1 was identified as a binding partner of the phosphate-uptake transporter PiT1.

    XPR1 (human phosphate exporter) → Human phosphate transporter PiT-1 / SLC20A1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/phosphorus-research/38833370.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5c093accfcc7194268c0fbd19d3ee39aae4206e9b2feed48b76b2a95eee33b78", "start_char": 0, "end_char": 1103, "text_sha256": "5c093accfcc7194268c0fbd19d3ee39aae4206e9b2feed48b76b2a95eee33b78"}
    experimental_model
    Protein interaction, localization and phosphate-challenge cell experiments
    exposure
    Genetic manipulation and pharmacological mimic of phosphate homeostatic challenge
    limitations
    Temporal regulatory model in cultured cells; endogenous InsP8 signaling is not equivalent to taking an inositol or phytate supplement.
    nutrient_topic
    Phosphorus research collection; topical membership is not evidence of a direct dietary effect. · Phosphorus
    organism
    Human cultured HCT116, U2OS and Saos-2 systems
    plain_language
    The phosphate exit system can physically connect to the entry system.
    primary_references
    [phosphorus-p38833370] Homeostatic coordination of cellular phosphate uptake and efflux requires an organelle-based receptor for the inositol pyrophosphate IP8. (2024). https://pubmed.ncbi.nlm.nih.gov/38833370/ DOI: 10.1016/j.celrep.2024.114316
    tissue_or_cell_type
    Cellular phosphate uptake/export and LAMP1-positive puncta

    Phosphorus: metabolism, signaling and nutrient connections (2026-09-17) · lines 724–735

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Protein interaction, localization and phosphate-challenge cell experiments · source_derived_draft · unverified_draft

    ### phosphorus-xpr1-pit1 XPR1 was identified as a binding partner of the phosphate-uptake transporter PiT1. Condition category: normal nutrient_topic: Phosphorus research collection; topical membership is not evidence of a direct dietary effect. plain_language: The phosphate exit system can physically connect to the entry system. organism: Human cultured HCT116, U2OS and Saos-2 systems tissue_or_cell_type: Cellular phosphate uptake/export and LAMP1-positive puncta experimental_model: Protein interaction, localization and phosphate-challenge cell experiments limitations: Temporal regulatory model in cultured cells; endogenous InsP8 signaling is not equivalent to taking an inositol or phytate supplement. exposure: Genetic manipulation and pharmacological mimic of phosphate homeostatic challenge evidence_span: {"source_cache": "artifacts/phosphorus-research/38833370.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5c093accfcc7194268c0fbd19d3ee39aae4206e9b2feed48b76b2a95eee33b78", "start_char": 0, "end_char": 1103, "text_sha256": "5c093accfcc7194268c0fbd19d3ee39aae4206e9b2feed48b76b2a95eee33b78"} [phosphorus-p38833370] Homeostatic coordination of cellular phosphate uptake and efflux requires an organelle-based receptor for the inositol pyrophosphate IP8. (2024). https://pubmed.ncbi.nlm.nih.gov/38833370/ DOI: 10.1016/j.celrep.2024.114316
    Complete structured claim and evidence

What acts on it

  1. XPR1 alone remained closed even with InsP6 and phosphate in the tested structures, whereas the KIDINS220-containing complex could open.

    KIDINS220 (human kinase D-interacting substrate 220) → XPR1 (human phosphate exporter) source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/inositol-research/40128258.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4765253840f684d5dafa834980e3fea9edc5d7419379b4a27ccf1090f081ce00", "start_char": 0, "end_char": 1071, "text_sha256": "4765253840f684d5dafa834980e3fea9edc5d7419379b4a27ccf1090f081ce00"}
    experimental_model
    Cryo-EM and functional mutagenesis
    exposure
    InsP6 and phosphate binding
    limitations
    This paper tests InsP6 despite pyrophosphate wording in its title. It does not establish that dietary phytate reaches this intracellular site or overrides InsP8 selectivity in other assays.
    nutrient_topic
    Inositol research collection; topical membership is not evidence of a direct dietary effect. · Inositol (stereoisomer family)
    organism
    Human proteins
    plain_language
    A partner protein mattered as well as the chemical signal.
    primary_references
    [ino-p40128258] Synergistic activation of the human phosphate exporter XPR1 by KIDINS220 and inositol pyrophosphate. (2025). https://pubmed.ncbi.nlm.nih.gov/40128258/ DOI: 10.1038/s41467-025-58200-y
    tissue_or_cell_type
    XPR1-KIDINS220 transport complex

    Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 938–949

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cryo-EM and functional mutagenesis · source_derived_draft · unverified_draft

    ### ino-kidins-xpr1 XPR1 alone remained closed even with InsP6 and phosphate in the tested structures, whereas the KIDINS220-containing complex could open. Condition category: normal nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: A partner protein mattered as well as the chemical signal. organism: Human proteins tissue_or_cell_type: XPR1-KIDINS220 transport complex experimental_model: Cryo-EM and functional mutagenesis limitations: This paper tests InsP6 despite pyrophosphate wording in its title. It does not establish that dietary phytate reaches this intracellular site or overrides InsP8 selectivity in other assays. exposure: InsP6 and phosphate binding evidence_span: {"source_cache": "artifacts/inositol-research/40128258.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4765253840f684d5dafa834980e3fea9edc5d7419379b4a27ccf1090f081ce00", "start_char": 0, "end_char": 1071, "text_sha256": "4765253840f684d5dafa834980e3fea9edc5d7419379b4a27ccf1090f081ce00"} [ino-p40128258] Synergistic activation of the human phosphate exporter XPR1 by KIDINS220 and inositol pyrophosphate. (2025). https://pubmed.ncbi.nlm.nih.gov/40128258/ DOI: 10.1038/s41467-025-58200-y
    Complete structured claim and evidence

  2. InsP8 bound the XPR1 N-terminal region with a reported dissociation constant of 180 nM.

    1,5-bisdiphosphoinositol tetrakisphosphate (1,5-InsP8) → XPR1 (human phosphate exporter) source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/inositol-research/32019887.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bb7637b9a327b1cba07716bbed5da8a3f32a3ac00c9fff70d23ada1a736d3d18", "start_char": 0, "end_char": 2004, "text_sha256": "bb7637b9a327b1cba07716bbed5da8a3f32a3ac00c9fff70d23ada1a736d3d18"}
    experimental_model
    Binding, knockout and rescue experiments
    exposure
    PPIP5K or XPR1 deletion, kinase rescue and pyrophosphate analog delivery
    limitations
    Cell assays establish a transport-regulation mechanism, not benefits of oral inositol or increased bone mineralization.
    nutrient_topic
    Inositol research collection; topical membership is not evidence of a direct dietary effect. · Inositol (stereoisomer family)
    organism
    Human cultured cells including Saos-2 osteosarcoma cells
    plain_language
    A specific inositol pyrophosphate binds the phosphate-export machinery.
    primary_references
    [ino-p32019887] Control of XPR1-dependent cellular phosphate efflux by InsP8 is an exemplar for functionally-exclusive inositol pyrophosphate signaling. (2020). https://pubmed.ncbi.nlm.nih.gov/32019887/ DOI: 10.1073/pnas.1908830117
    tissue_or_cell_type
    Cellular phosphate transport

    Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 873–884

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Binding, knockout and rescue experiments · source_derived_draft · unverified_draft

    ### ino-xpr1-ip8 InsP8 bound the XPR1 N-terminal region with a reported dissociation constant of 180 nM. Condition category: normal nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: A specific inositol pyrophosphate binds the phosphate-export machinery. organism: Human cultured cells including Saos-2 osteosarcoma cells tissue_or_cell_type: Cellular phosphate transport experimental_model: Binding, knockout and rescue experiments limitations: Cell assays establish a transport-regulation mechanism, not benefits of oral inositol or increased bone mineralization. exposure: PPIP5K or XPR1 deletion, kinase rescue and pyrophosphate analog delivery evidence_span: {"source_cache": "artifacts/inositol-research/32019887.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bb7637b9a327b1cba07716bbed5da8a3f32a3ac00c9fff70d23ada1a736d3d18", "start_char": 0, "end_char": 2004, "text_sha256": "bb7637b9a327b1cba07716bbed5da8a3f32a3ac00c9fff70d23ada1a736d3d18"} [ino-p32019887] Control of XPR1-dependent cellular phosphate efflux by InsP8 is an exemplar for functionally-exclusive inositol pyrophosphate signaling. (2020). https://pubmed.ncbi.nlm.nih.gov/32019887/ DOI: 10.1073/pnas.1908830117
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. PPIP5K knockout reduced XPR1-dependent phosphate efflux; wild-type PPIP5K1 rescued efflux whereas kinase-dead PPIP5K1 did not.

    Diphosphoinositol pentakisphosphate kinase family → Cellular inorganic phosphate export source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/inositol-research/32019887.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bb7637b9a327b1cba07716bbed5da8a3f32a3ac00c9fff70d23ada1a736d3d18", "start_char": 0, "end_char": 2004, "text_sha256": "bb7637b9a327b1cba07716bbed5da8a3f32a3ac00c9fff70d23ada1a736d3d18"}
    experimental_model
    Binding, knockout and rescue experiments
    exposure
    PPIP5K or XPR1 deletion, kinase rescue and pyrophosphate analog delivery
    limitations
    Cell assays establish a transport-regulation mechanism, not benefits of oral inositol or increased bone mineralization.
    nutrient_topic
    Inositol research collection; topical membership is not evidence of a direct dietary effect. · Inositol (stereoisomer family)
    organism
    Human cultured cells including Saos-2 osteosarcoma cells
    plain_language
    The exporter needed the signal-generating activity, not simply the presence of the protein.
    primary_references
    [ino-p32019887] Control of XPR1-dependent cellular phosphate efflux by InsP8 is an exemplar for functionally-exclusive inositol pyrophosphate signaling. (2020). https://pubmed.ncbi.nlm.nih.gov/32019887/ DOI: 10.1073/pnas.1908830117
    tissue_or_cell_type
    Cellular phosphate transport
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 886–897

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Binding, knockout and rescue experiments · source_derived_draft · unverified_draft

    ### ino-ppip5k-export PPIP5K knockout reduced XPR1-dependent phosphate efflux; wild-type PPIP5K1 rescued efflux whereas kinase-dead PPIP5K1 did not. Condition category: machinery_impairment nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: The exporter needed the signal-generating activity, not simply the presence of the protein. organism: Human cultured cells including Saos-2 osteosarcoma cells tissue_or_cell_type: Cellular phosphate transport experimental_model: Binding, knockout and rescue experiments limitations: Cell assays establish a transport-regulation mechanism, not benefits of oral inositol or increased bone mineralization. exposure: PPIP5K or XPR1 deletion, kinase rescue and pyrophosphate analog delivery evidence_span: {"source_cache": "artifacts/inositol-research/32019887.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bb7637b9a327b1cba07716bbed5da8a3f32a3ac00c9fff70d23ada1a736d3d18", "start_char": 0, "end_char": 2004, "text_sha256": "bb7637b9a327b1cba07716bbed5da8a3f32a3ac00c9fff70d23ada1a736d3d18"} [ino-p32019887] Control of XPR1-dependent cellular phosphate efflux by InsP8 is an exemplar for functionally-exclusive inositol pyrophosphate signaling. (2020). https://pubmed.ncbi.nlm.nih.gov/32019887/ DOI: 10.1073/pnas.1908830117
    Complete structured claim and evidence

  2. In the challenge model, InsP8-dependent XPR1 regulation first adjusted phosphate efflux.

    1,5-bisdiphosphoinositol tetrakisphosphate (1,5-InsP8) → Cellular inorganic phosphate export source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/phosphorus-research/38833370.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5c093accfcc7194268c0fbd19d3ee39aae4206e9b2feed48b76b2a95eee33b78", "start_char": 0, "end_char": 1103, "text_sha256": "5c093accfcc7194268c0fbd19d3ee39aae4206e9b2feed48b76b2a95eee33b78"}
    experimental_model
    Protein interaction, localization and phosphate-challenge cell experiments
    exposure
    Genetic manipulation and pharmacological mimic of phosphate homeostatic challenge
    limitations
    Temporal regulatory model in cultured cells; endogenous InsP8 signaling is not equivalent to taking an inositol or phytate supplement.
    nutrient_topic
    Phosphorus research collection; topical membership is not evidence of a direct dietary effect. · Phosphorus
    organism
    Human cultured HCT116, U2OS and Saos-2 systems
    plain_language
    An inositol pyrophosphate signal changed phosphate export.
    primary_references
    [phosphorus-p38833370] Homeostatic coordination of cellular phosphate uptake and efflux requires an organelle-based receptor for the inositol pyrophosphate IP8. (2024). https://pubmed.ncbi.nlm.nih.gov/38833370/ DOI: 10.1016/j.celrep.2024.114316
    tissue_or_cell_type
    Cellular phosphate uptake/export and LAMP1-positive puncta

    Phosphorus: metabolism, signaling and nutrient connections (2026-09-17) · lines 750–761

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Protein interaction, localization and phosphate-challenge cell experiments · source_derived_draft · unverified_draft

    ### phosphorus-ip8-export In the challenge model, InsP8-dependent XPR1 regulation first adjusted phosphate efflux. Condition category: normal nutrient_topic: Phosphorus research collection; topical membership is not evidence of a direct dietary effect. plain_language: An inositol pyrophosphate signal changed phosphate export. organism: Human cultured HCT116, U2OS and Saos-2 systems tissue_or_cell_type: Cellular phosphate uptake/export and LAMP1-positive puncta experimental_model: Protein interaction, localization and phosphate-challenge cell experiments limitations: Temporal regulatory model in cultured cells; endogenous InsP8 signaling is not equivalent to taking an inositol or phytate supplement. exposure: Genetic manipulation and pharmacological mimic of phosphate homeostatic challenge evidence_span: {"source_cache": "artifacts/phosphorus-research/38833370.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5c093accfcc7194268c0fbd19d3ee39aae4206e9b2feed48b76b2a95eee33b78", "start_char": 0, "end_char": 1103, "text_sha256": "5c093accfcc7194268c0fbd19d3ee39aae4206e9b2feed48b76b2a95eee33b78"} [phosphorus-p38833370] Homeostatic coordination of cellular phosphate uptake and efflux requires an organelle-based receptor for the inositol pyrophosphate IP8. (2024). https://pubmed.ncbi.nlm.nih.gov/38833370/ DOI: 10.1016/j.celrep.2024.114316
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards