Component

5-diphosphoinositol pentakisphosphate (5-InsP7)

5-diphosphoinositol pentakisphosphate (5-InsP7). Species, exposure and limitations are retained in each linked claim.

5 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. 5-InsP7 inhibited PDK1-dependent Akt phosphorylation and activation in the reported biochemical pathway.

    5-diphosphoinositol pentakisphosphate (5-InsP7) → AKT serine/threonine kinase family source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/inositol-research/21145457.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0de0a9c3ea11cd8ce59bccff69a41139b11e11182fd9fd66016ec72ba329a5ce", "start_char": 0, "end_char": 889, "text_sha256": "0de0a9c3ea11cd8ce59bccff69a41139b11e11182fd9fd66016ec72ba329a5ce"}
    experimental_model
    Biochemical Akt regulation and targeted mouse Ip6k1 deletion
    exposure
    5-InsP7 and Ip6k1 knockout
    limitations
    Whole-gene deletion is not equivalent to adding or withdrawing free myo-inositol; the reported therapeutic proposal is not established treatment.
    nutrient_topic
    Inositol research collection; topical membership is not evidence of a direct dietary effect. · Inositol (stereoisomer family)
    organism
    Mammalian enzymology and Mus musculus
    plain_language
    An inositol-derived signal can restrain insulin-pathway signaling rather than always increasing it.
    primary_references
    [ino-p21145457] Inositol pyrophosphates inhibit Akt signaling, thereby regulating insulin sensitivity and weight gain. (2010). https://pubmed.ncbi.nlm.nih.gov/21145457/ DOI: 10.1016/j.cell.2010.11.032
    tissue_or_cell_type
    Muscle, adipose tissue and liver

    Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 782–793

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Biochemical Akt regulation and targeted mouse Ip6k1 deletion · source_derived_draft · unverified_draft

    ### ino-ip7-akt 5-InsP7 inhibited PDK1-dependent Akt phosphorylation and activation in the reported biochemical pathway. Condition category: normal nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: An inositol-derived signal can restrain insulin-pathway signaling rather than always increasing it. organism: Mammalian enzymology and Mus musculus tissue_or_cell_type: Muscle, adipose tissue and liver experimental_model: Biochemical Akt regulation and targeted mouse Ip6k1 deletion limitations: Whole-gene deletion is not equivalent to adding or withdrawing free myo-inositol; the reported therapeutic proposal is not established treatment. exposure: 5-InsP7 and Ip6k1 knockout evidence_span: {"source_cache": "artifacts/inositol-research/21145457.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0de0a9c3ea11cd8ce59bccff69a41139b11e11182fd9fd66016ec72ba329a5ce", "start_char": 0, "end_char": 889, "text_sha256": "0de0a9c3ea11cd8ce59bccff69a41139b11e11182fd9fd66016ec72ba329a5ce"} [ino-p21145457] Inositol pyrophosphates inhibit Akt signaling, thereby regulating insulin sensitivity and weight gain. (2010). https://pubmed.ncbi.nlm.nih.gov/21145457/ DOI: 10.1016/j.cell.2010.11.032
    Complete structured claim and evidence

What acts on it

  1. IP6K enzymes form 5-InsP7 from InsP6.

    Inositol hexakisphosphate kinase family → 5-diphosphoinositol pentakisphosphate (5-InsP7) source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/inositol-research/21145457.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0de0a9c3ea11cd8ce59bccff69a41139b11e11182fd9fd66016ec72ba329a5ce", "start_char": 0, "end_char": 889, "text_sha256": "0de0a9c3ea11cd8ce59bccff69a41139b11e11182fd9fd66016ec72ba329a5ce"}
    experimental_model
    Biochemical Akt regulation and targeted mouse Ip6k1 deletion
    exposure
    5-InsP7 and Ip6k1 knockout
    limitations
    Whole-gene deletion is not equivalent to adding or withdrawing free myo-inositol; the reported therapeutic proposal is not established treatment.
    nutrient_topic
    Inositol research collection; topical membership is not evidence of a direct dietary effect. · Inositol (stereoisomer family)
    organism
    Mammalian enzymology and Mus musculus
    plain_language
    Adding a phosphate onto an existing phosphate makes an inositol pyrophosphate.
    primary_references
    [ino-p21145457] Inositol pyrophosphates inhibit Akt signaling, thereby regulating insulin sensitivity and weight gain. (2010). https://pubmed.ncbi.nlm.nih.gov/21145457/ DOI: 10.1016/j.cell.2010.11.032
    tissue_or_cell_type
    Muscle, adipose tissue and liver

    Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 769–780

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Biochemical Akt regulation and targeted mouse Ip6k1 deletion · source_derived_draft · unverified_draft

    ### ino-ip6k-ip7 IP6K enzymes form 5-InsP7 from InsP6. Condition category: normal nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: Adding a phosphate onto an existing phosphate makes an inositol pyrophosphate. organism: Mammalian enzymology and Mus musculus tissue_or_cell_type: Muscle, adipose tissue and liver experimental_model: Biochemical Akt regulation and targeted mouse Ip6k1 deletion limitations: Whole-gene deletion is not equivalent to adding or withdrawing free myo-inositol; the reported therapeutic proposal is not established treatment. exposure: 5-InsP7 and Ip6k1 knockout evidence_span: {"source_cache": "artifacts/inositol-research/21145457.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0de0a9c3ea11cd8ce59bccff69a41139b11e11182fd9fd66016ec72ba329a5ce", "start_char": 0, "end_char": 889, "text_sha256": "0de0a9c3ea11cd8ce59bccff69a41139b11e11182fd9fd66016ec72ba329a5ce"} [ino-p21145457] Inositol pyrophosphates inhibit Akt signaling, thereby regulating insulin sensitivity and weight gain. (2010). https://pubmed.ncbi.nlm.nih.gov/21145457/ DOI: 10.1016/j.cell.2010.11.032
    Complete structured claim and evidence

  2. PPIP5K kinase activity converts 5-InsP7 to 1,5-InsP8.

    Diphosphoinositol pentakisphosphate kinase family → 5-diphosphoinositol pentakisphosphate (5-InsP7) source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/inositol-research/28126903.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6f5c96ed7d02591d5fe475d0e26aa2f21dc93f0c86c12998debb417f98254d2f", "start_char": 0, "end_char": 1981, "text_sha256": "6f5c96ed7d02591d5fe475d0e26aa2f21dc93f0c86c12998debb417f98254d2f"}
    experimental_model
    Cellular phosphate withdrawal/repletion and bifunctional enzyme kinetics
    exposure
    Phosphate availability and PPIP5K kinase/phosphatase assays
    limitations
    Cell-culture nutrient withdrawal is not a measured human dietary threshold; PPIP5K isoforms are not identical.
    nutrient_topic
    Inositol research collection; topical membership is not evidence of a direct dietary effect. · Inositol (stereoisomer family)
    organism
    Human HCT116 cells and human PPIP5K proteins
    plain_language
    A further phosphorylation step creates another distinct phosphate signal.
    primary_references
    [ino-p28126903] The Significance of the Bifunctional Kinase/Phosphatase Activities of Diphosphoinositol Pentakisphosphate Kinases (PPIP5Ks) for Coupling Inositol Pyrophosphate Cell Signaling to Cellular Phosphate Homeostasis. (2017). https://pubmed.ncbi.nlm.nih.gov/28126903/ DOI: 10.1074/jbc.m116.765743
    tissue_or_cell_type
    Intestinal tumor-derived cell line; purified enzymes

    Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 808–819

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cellular phosphate withdrawal/repletion and bifunctional enzyme kinetics · source_derived_draft · unverified_draft

    ### ino-ppip5k-ip8 PPIP5K kinase activity converts 5-InsP7 to 1,5-InsP8. Condition category: normal nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: A further phosphorylation step creates another distinct phosphate signal. organism: Human HCT116 cells and human PPIP5K proteins tissue_or_cell_type: Intestinal tumor-derived cell line; purified enzymes experimental_model: Cellular phosphate withdrawal/repletion and bifunctional enzyme kinetics limitations: Cell-culture nutrient withdrawal is not a measured human dietary threshold; PPIP5K isoforms are not identical. exposure: Phosphate availability and PPIP5K kinase/phosphatase assays evidence_span: {"source_cache": "artifacts/inositol-research/28126903.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6f5c96ed7d02591d5fe475d0e26aa2f21dc93f0c86c12998debb417f98254d2f", "start_char": 0, "end_char": 1981, "text_sha256": "6f5c96ed7d02591d5fe475d0e26aa2f21dc93f0c86c12998debb417f98254d2f"} [ino-p28126903] The Significance of the Bifunctional Kinase/Phosphatase Activities of Diphosphoinositol Pentakisphosphate Kinases (PPIP5Ks) for Coupling Inositol Pyrophosphate Cell Signaling to Cellular Phosphate Homeostasis. (2017). https://pubmed.ncbi.nlm.nih.gov/28126903/ DOI: 10.1074/jbc.m116.765743
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Phosphate starvation lowered ATP and 5-InsP7, while InsP8 showed a larger and more sensitive response; levels recovered with phosphate replenishment.

    Inorganic phosphate → 1,5-bisdiphosphoinositol tetrakisphosphate (1,5-InsP8) source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    nutrient_deficiency Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/inositol-research/28126903.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6f5c96ed7d02591d5fe475d0e26aa2f21dc93f0c86c12998debb417f98254d2f", "start_char": 0, "end_char": 1981, "text_sha256": "6f5c96ed7d02591d5fe475d0e26aa2f21dc93f0c86c12998debb417f98254d2f"}
    experimental_model
    Cellular phosphate withdrawal/repletion and bifunctional enzyme kinetics
    exposure
    Phosphate availability and PPIP5K kinase/phosphatase assays
    limitations
    Cell-culture nutrient withdrawal is not a measured human dietary threshold; PPIP5K isoforms are not identical.
    nutrient_topic
    Inositol research collection; topical membership is not evidence of a direct dietary effect. · Inositol (stereoisomer family)
    organism
    Human HCT116 cells and human PPIP5K proteins
    plain_language
    The signaling network detects phosphate supply instead of depending only on the amount of free inositol.
    primary_references
    [ino-p28126903] The Significance of the Bifunctional Kinase/Phosphatase Activities of Diphosphoinositol Pentakisphosphate Kinases (PPIP5Ks) for Coupling Inositol Pyrophosphate Cell Signaling to Cellular Phosphate Homeostasis. (2017). https://pubmed.ncbi.nlm.nih.gov/28126903/ DOI: 10.1074/jbc.m116.765743
    tissue_or_cell_type
    Intestinal tumor-derived cell line; purified enzymes
    trigger_kind
    nutrient_deficiency Imported condition classification; unverified.

    Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 860–871

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cellular phosphate withdrawal/repletion and bifunctional enzyme kinetics · source_derived_draft · unverified_draft

    ### ino-phosphate-ip8 Phosphate starvation lowered ATP and 5-InsP7, while InsP8 showed a larger and more sensitive response; levels recovered with phosphate replenishment. Condition category: nutrient_deficiency nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: The signaling network detects phosphate supply instead of depending only on the amount of free inositol. organism: Human HCT116 cells and human PPIP5K proteins tissue_or_cell_type: Intestinal tumor-derived cell line; purified enzymes experimental_model: Cellular phosphate withdrawal/repletion and bifunctional enzyme kinetics limitations: Cell-culture nutrient withdrawal is not a measured human dietary threshold; PPIP5K isoforms are not identical. exposure: Phosphate availability and PPIP5K kinase/phosphatase assays evidence_span: {"source_cache": "artifacts/inositol-research/28126903.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6f5c96ed7d02591d5fe475d0e26aa2f21dc93f0c86c12998debb417f98254d2f", "start_char": 0, "end_char": 1981, "text_sha256": "6f5c96ed7d02591d5fe475d0e26aa2f21dc93f0c86c12998debb417f98254d2f"} [ino-p28126903] The Significance of the Bifunctional Kinase/Phosphatase Activities of Diphosphoinositol Pentakisphosphate Kinases (PPIP5Ks) for Coupling Inositol Pyrophosphate Cell Signaling to Cellular Phosphate Homeostasis. (2017). https://pubmed.ncbi.nlm.nih.gov/28126903/ DOI: 10.1074/jbc.m116.765743
    Complete structured claim and evidence

  2. PPIP5K proteins also possess InsP8 phosphatase activity, opposing their kinase reaction.

    Diphosphoinositol pentakisphosphate kinase family → 1,5-bisdiphosphoinositol tetrakisphosphate (1,5-InsP8) source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/inositol-research/28126903.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6f5c96ed7d02591d5fe475d0e26aa2f21dc93f0c86c12998debb417f98254d2f", "start_char": 0, "end_char": 1981, "text_sha256": "6f5c96ed7d02591d5fe475d0e26aa2f21dc93f0c86c12998debb417f98254d2f"}
    experimental_model
    Cellular phosphate withdrawal/repletion and bifunctional enzyme kinetics
    exposure
    Phosphate availability and PPIP5K kinase/phosphatase assays
    limitations
    Cell-culture nutrient withdrawal is not a measured human dietary threshold; PPIP5K isoforms are not identical.
    nutrient_topic
    Inositol research collection; topical membership is not evidence of a direct dietary effect. · Inositol (stereoisomer family)
    organism
    Human HCT116 cells and human PPIP5K proteins
    plain_language
    The same protein family can build and break down the signal.
    primary_references
    [ino-p28126903] The Significance of the Bifunctional Kinase/Phosphatase Activities of Diphosphoinositol Pentakisphosphate Kinases (PPIP5Ks) for Coupling Inositol Pyrophosphate Cell Signaling to Cellular Phosphate Homeostasis. (2017). https://pubmed.ncbi.nlm.nih.gov/28126903/ DOI: 10.1074/jbc.m116.765743
    tissue_or_cell_type
    Intestinal tumor-derived cell line; purified enzymes

    Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 821–832

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cellular phosphate withdrawal/repletion and bifunctional enzyme kinetics · source_derived_draft · unverified_draft

    ### ino-ppip5k-reverse PPIP5K proteins also possess InsP8 phosphatase activity, opposing their kinase reaction. Condition category: normal nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: The same protein family can build and break down the signal. organism: Human HCT116 cells and human PPIP5K proteins tissue_or_cell_type: Intestinal tumor-derived cell line; purified enzymes experimental_model: Cellular phosphate withdrawal/repletion and bifunctional enzyme kinetics limitations: Cell-culture nutrient withdrawal is not a measured human dietary threshold; PPIP5K isoforms are not identical. exposure: Phosphate availability and PPIP5K kinase/phosphatase assays evidence_span: {"source_cache": "artifacts/inositol-research/28126903.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6f5c96ed7d02591d5fe475d0e26aa2f21dc93f0c86c12998debb417f98254d2f", "start_char": 0, "end_char": 1981, "text_sha256": "6f5c96ed7d02591d5fe475d0e26aa2f21dc93f0c86c12998debb417f98254d2f"} [ino-p28126903] The Significance of the Bifunctional Kinase/Phosphatase Activities of Diphosphoinositol Pentakisphosphate Kinases (PPIP5Ks) for Coupling Inositol Pyrophosphate Cell Signaling to Cellular Phosphate Homeostasis. (2017). https://pubmed.ncbi.nlm.nih.gov/28126903/ DOI: 10.1074/jbc.m116.765743
    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