Component
Human XPR1-KIDINS220 complex
Human XPR1-KIDINS220 complex. Species, exposure and limitations are retained in each linked claim.
2 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
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.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
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.
What acts on it
In the presence of InsP6 and phosphate, human XPR1-KIDINS220 adopted an outward-open structure; InsP6 occupied SPX and juxtamembrane regions.
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
- An intracellular inositol phosphate helped stabilize an open exporter complex.
- 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 925–936
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-xpr1-ins-p6 In the presence of InsP6 and phosphate, human XPR1-KIDINS220 adopted an outward-open structure; InsP6 occupied SPX and juxtamembrane regions. Condition category: normal nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: An intracellular inositol phosphate helped stabilize an open exporter complex. 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
Where it participates (unsigned role)
XPR1 alone remained closed even with InsP6 and phosphate in the tested structures, whereas the KIDINS220-containing complex could open.
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
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.