Component
Phosphatidylinositol 3,4,5-trisphosphate (PIP3)
Phosphatidylinositol 3,4,5-trisphosphate (PIP3). 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
Human PTEN removed the 3-phosphate from PI(3,4,5)P3, forming PI(4,5)P2.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/inositol-research/9593664.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "118dd3dacb2fa7be09cb0258dd0f6de1193cf2553142c94a5750d82c5f00a248", "start_char": 0, "end_char": 1012, "text_sha256": "118dd3dacb2fa7be09cb0258dd0f6de1193cf2553142c94a5750d82c5f00a248"}
- experimental_model
- Phosphatase assays and human cell expression
- exposure
- Wild-type versus catalytic-mutant PTEN
- limitations
- Cellular overexpression and enzymology do not imply that inositol supplements activate PTEN.
- nutrient_topic
- Inositol research collection; topical membership is not evidence of a direct dietary effect. · Inositol (stereoisomer family)
- organism
- Human protein and HEK293 cells
- plain_language
- A phosphatase reverses a signaling-lipid phosphorylation step.
- primary_references
- [ino-p9593664] The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. (1998). https://pubmed.ncbi.nlm.nih.gov/9593664/ DOI: 10.1074/jbc.273.22.13375
- tissue_or_cell_type
- Purified enzyme and cultured cells
Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 717–728
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Phosphatase assays and human cell expression · source_derived_draft · unverified_draft
### ino-pten-pip3 Human PTEN removed the 3-phosphate from PI(3,4,5)P3, forming PI(4,5)P2. Condition category: normal nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: A phosphatase reverses a signaling-lipid phosphorylation step. organism: Human protein and HEK293 cells tissue_or_cell_type: Purified enzyme and cultured cells experimental_model: Phosphatase assays and human cell expression limitations: Cellular overexpression and enzymology do not imply that inositol supplements activate PTEN. exposure: Wild-type versus catalytic-mutant PTEN evidence_span: {"source_cache": "artifacts/inositol-research/9593664.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "118dd3dacb2fa7be09cb0258dd0f6de1193cf2553142c94a5750d82c5f00a248", "start_char": 0, "end_char": 1012, "text_sha256": "118dd3dacb2fa7be09cb0258dd0f6de1193cf2553142c94a5750d82c5f00a248"} [ino-p9593664] The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. (1998). https://pubmed.ncbi.nlm.nih.gov/9593664/ DOI: 10.1074/jbc.273.22.13375
Complete structured claim and evidence
Where it participates (unsigned role)
Human IPMK also has PI(4,5)P2 3-kinase activity, producing PI(3,4,5)P3.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/inositol-research/28882892.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "39494635d8bd1a8a8df3ac71f8aa6c5f6440bd3c6fa7cb4756e52d572a8f16db", "start_char": 0, "end_char": 1781, "text_sha256": "39494635d8bd1a8a8df3ac71f8aa6c5f6440bd3c6fa7cb4756e52d572a8f16db"}
- experimental_model
- Crystal structures and targeted human IPMK mutants
- exposure
- IP3 and PI(4,5)P2 substrate binding and phosphorylation
- limitations
- Human substrate specificity differs from yeast and plant orthologs; do not merge their regioselectivity.
- nutrient_topic
- Inositol research collection; topical membership is not evidence of a direct dietary effect. · Inositol (stereoisomer family)
- organism
- Human protein
- plain_language
- One enzyme acts on both soluble inositol phosphates and a membrane lipid.
- primary_references
- [ino-p28882892] Structural features of human inositol phosphate multikinase rationalize its inositol phosphate kinase and phosphoinositide 3-kinase activities. (2017). https://pubmed.ncbi.nlm.nih.gov/28882892/ DOI: 10.1074/jbc.m117.801845
- tissue_or_cell_type
- Purified IPMK
Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 691–702
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Crystal structures and targeted human IPMK mutants · source_derived_draft · unverified_draft
### ino-ipmk-pip3 Human IPMK also has PI(4,5)P2 3-kinase activity, producing PI(3,4,5)P3. Condition category: normal nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: One enzyme acts on both soluble inositol phosphates and a membrane lipid. organism: Human protein tissue_or_cell_type: Purified IPMK experimental_model: Crystal structures and targeted human IPMK mutants limitations: Human substrate specificity differs from yeast and plant orthologs; do not merge their regioselectivity. exposure: IP3 and PI(4,5)P2 substrate binding and phosphorylation evidence_span: {"source_cache": "artifacts/inositol-research/28882892.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "39494635d8bd1a8a8df3ac71f8aa6c5f6440bd3c6fa7cb4756e52d572a8f16db", "start_char": 0, "end_char": 1781, "text_sha256": "39494635d8bd1a8a8df3ac71f8aa6c5f6440bd3c6fa7cb4756e52d572a8f16db"} [ino-p28882892] Structural features of human inositol phosphate multikinase rationalize its inositol phosphate kinase and phosphoinositide 3-kinase activities. (2017). https://pubmed.ncbi.nlm.nih.gov/28882892/ DOI: 10.1074/jbc.m117.801845
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.