Component

Human high-affinity choline transporter CHT1 / SLC5A7

Human high-affinity choline transporter CHT1 / SLC5A7. Species, exposure and limitations are retained in each linked claim.

6 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. CHT1 supports reutilization of choline liberated by synaptic acetylcholine hydrolysis, sustaining presynaptic acetylcholine synthesis.

    Human high-affinity choline transporter CHT1 / SLC5A7 → Choline source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/choline-research/38589607.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3cf951acec5056180aacccf73a96951c54fa40be5446cd778bd90eb23b43fd3a", "start_char": 0, "end_char": 1090, "text_sha256": "3cf951acec5056180aacccf73a96951c54fa40be5446cd778bd90eb23b43fd3a"}
    experimental_model
    Human CHT1 cryo-EM and functional characterization
    exposure
    Choline-bound, inhibitor-bound and apo conformations
    limitations
    Structural transport cycle; no claim of cognitive benefit from increasing intake.
    nutrient_topic
    Choline research collection; topical membership is not evidence of a direct dietary effect. · Choline
    organism
    Human CHT1 protein
    plain_language
    After acetylcholine is broken down, choline can be taken back up and reused.
    primary_references
    [choline-p38589607] Transport mechanism of presynaptic high-affinity choline uptake by CHT1. (2024). https://pubmed.ncbi.nlm.nih.gov/38589607/ DOI: 10.1038/s41594-024-01259-w
    tissue_or_cell_type
    Presynaptic uptake mechanism and experimental structures

    Choline: metabolism, signaling and nutrient connections (2026-09-17) · lines 334–345

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human CHT1 cryo-EM and functional characterization · source_derived_draft · unverified_draft

    ### choline-cht1-recycling CHT1 supports reutilization of choline liberated by synaptic acetylcholine hydrolysis, sustaining presynaptic acetylcholine synthesis. Condition category: normal nutrient_topic: Choline research collection; topical membership is not evidence of a direct dietary effect. plain_language: After acetylcholine is broken down, choline can be taken back up and reused. organism: Human CHT1 protein tissue_or_cell_type: Presynaptic uptake mechanism and experimental structures experimental_model: Human CHT1 cryo-EM and functional characterization limitations: Structural transport cycle; no claim of cognitive benefit from increasing intake. exposure: Choline-bound, inhibitor-bound and apo conformations evidence_span: {"source_cache": "artifacts/choline-research/38589607.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3cf951acec5056180aacccf73a96951c54fa40be5446cd778bd90eb23b43fd3a", "start_char": 0, "end_char": 1090, "text_sha256": "3cf951acec5056180aacccf73a96951c54fa40be5446cd778bd90eb23b43fd3a"} [choline-p38589607] Transport mechanism of presynaptic high-affinity choline uptake by CHT1. (2024). https://pubmed.ncbi.nlm.nih.gov/38589607/ DOI: 10.1038/s41594-024-01259-w
    Complete structured claim and evidence

  2. Human CHT1 expression produced high-affinity choline uptake in Xenopus oocytes.

    Human high-affinity choline transporter CHT1 / SLC5A7 → Human CHT1-mediated choline uptake in expression assays source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/choline-research/11068039.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "f9885c7f9525456b2c9eac0865a1f86cda2cf8f26cd6a8e34c212218f3a22bd5", "start_char": 0, "end_char": 1088, "text_sha256": "f9885c7f9525456b2c9eac0865a1f86cda2cf8f26cd6a8e34c212218f3a22bd5"}
    experimental_model
    Human CHT1 expression in Xenopus oocytes
    exposure
    Choline, sodium and chloride titrations; hemicholinium-3 inhibition
    limitations
    Assay EC50 values and Hill coefficients are not dietary requirements or exact ion-coupling stoichiometry.
    nutrient_topic
    Choline research collection; topical membership is not evidence of a direct dietary effect. · Choline
    organism
    Human transporter; Xenopus oocyte host
    plain_language
    This transporter supplies choline for the neuronal recycling route.
    primary_references
    [choline-p11068039] Functional characterization of the human high-affinity choline transporter. (2000). https://pubmed.ncbi.nlm.nih.gov/11068039/ DOI: 10.1016/s0014-5793(00)02134-7
    tissue_or_cell_type
    Plasma-membrane transport assay

    Choline: metabolism, signaling and nutrient connections (2026-09-17) · lines 282–293

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human CHT1 expression in Xenopus oocytes · source_derived_draft · unverified_draft

    ### choline-cht1-uptake Human CHT1 expression produced high-affinity choline uptake in Xenopus oocytes. Condition category: normal nutrient_topic: Choline research collection; topical membership is not evidence of a direct dietary effect. plain_language: This transporter supplies choline for the neuronal recycling route. organism: Human transporter; Xenopus oocyte host tissue_or_cell_type: Plasma-membrane transport assay experimental_model: Human CHT1 expression in Xenopus oocytes limitations: Assay EC50 values and Hill coefficients are not dietary requirements or exact ion-coupling stoichiometry. exposure: Choline, sodium and chloride titrations; hemicholinium-3 inhibition evidence_span: {"source_cache": "artifacts/choline-research/11068039.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "f9885c7f9525456b2c9eac0865a1f86cda2cf8f26cd6a8e34c212218f3a22bd5", "start_char": 0, "end_char": 1088, "text_sha256": "f9885c7f9525456b2c9eac0865a1f86cda2cf8f26cd6a8e34c212218f3a22bd5"} [choline-p11068039] Functional characterization of the human high-affinity choline transporter. (2000). https://pubmed.ncbi.nlm.nih.gov/11068039/ DOI: 10.1016/s0014-5793(00)02134-7
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Human CHT1-mediated choline uptake depended on Cl− in the oocyte assay.

    Chloride ion → Human CHT1-mediated choline uptake in expression assays source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/choline-research/11068039.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "f9885c7f9525456b2c9eac0865a1f86cda2cf8f26cd6a8e34c212218f3a22bd5", "start_char": 0, "end_char": 1088, "text_sha256": "f9885c7f9525456b2c9eac0865a1f86cda2cf8f26cd6a8e34c212218f3a22bd5"}
    experimental_model
    Human CHT1 expression in Xenopus oocytes
    exposure
    Choline, sodium and chloride titrations; hemicholinium-3 inhibition
    limitations
    Assay EC50 values and Hill coefficients are not dietary requirements or exact ion-coupling stoichiometry.
    nutrient_topic
    Choline research collection; topical membership is not evidence of a direct dietary effect. · Choline
    organism
    Human transporter; Xenopus oocyte host
    plain_language
    Cl− was part of the transport requirement, not just a background nutrient.
    primary_references
    [choline-p11068039] Functional characterization of the human high-affinity choline transporter. (2000). https://pubmed.ncbi.nlm.nih.gov/11068039/ DOI: 10.1016/s0014-5793(00)02134-7
    tissue_or_cell_type
    Plasma-membrane transport assay

    Choline: metabolism, signaling and nutrient connections (2026-09-17) · lines 308–319

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human CHT1 expression in Xenopus oocytes · source_derived_draft · unverified_draft

    ### choline-cht1-chloride Human CHT1-mediated choline uptake depended on Cl− in the oocyte assay. Condition category: normal nutrient_topic: Choline research collection; topical membership is not evidence of a direct dietary effect. plain_language: Cl− was part of the transport requirement, not just a background nutrient. organism: Human transporter; Xenopus oocyte host tissue_or_cell_type: Plasma-membrane transport assay experimental_model: Human CHT1 expression in Xenopus oocytes limitations: Assay EC50 values and Hill coefficients are not dietary requirements or exact ion-coupling stoichiometry. exposure: Choline, sodium and chloride titrations; hemicholinium-3 inhibition evidence_span: {"source_cache": "artifacts/choline-research/11068039.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "f9885c7f9525456b2c9eac0865a1f86cda2cf8f26cd6a8e34c212218f3a22bd5", "start_char": 0, "end_char": 1088, "text_sha256": "f9885c7f9525456b2c9eac0865a1f86cda2cf8f26cd6a8e34c212218f3a22bd5"} [choline-p11068039] Functional characterization of the human high-affinity choline transporter. (2000). https://pubmed.ncbi.nlm.nih.gov/11068039/ DOI: 10.1016/s0014-5793(00)02134-7
    Complete structured claim and evidence

  2. Hemicholinium-3 inhibited human CHT1-mediated uptake with a reported Ki of 1.3 nM.

    Hemicholinium-3 → Human CHT1-mediated choline uptake in expression assays source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/choline-research/11068039.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "f9885c7f9525456b2c9eac0865a1f86cda2cf8f26cd6a8e34c212218f3a22bd5", "start_char": 0, "end_char": 1088, "text_sha256": "f9885c7f9525456b2c9eac0865a1f86cda2cf8f26cd6a8e34c212218f3a22bd5"}
    experimental_model
    Human CHT1 expression in Xenopus oocytes
    exposure
    Choline, sodium and chloride titrations; hemicholinium-3 inhibition
    limitations
    Assay EC50 values and Hill coefficients are not dietary requirements or exact ion-coupling stoichiometry.
    nutrient_topic
    Choline research collection; topical membership is not evidence of a direct dietary effect. · Choline
    organism
    Human transporter; Xenopus oocyte host
    plain_language
    Blocking entry can limit choline availability even when choline is outside the cell.
    primary_references
    [choline-p11068039] Functional characterization of the human high-affinity choline transporter. (2000). https://pubmed.ncbi.nlm.nih.gov/11068039/ DOI: 10.1016/s0014-5793(00)02134-7
    tissue_or_cell_type
    Plasma-membrane transport assay

    Choline: metabolism, signaling and nutrient connections (2026-09-17) · lines 321–332

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human CHT1 expression in Xenopus oocytes · source_derived_draft · unverified_draft

    ### choline-cht1-inhibitor Hemicholinium-3 inhibited human CHT1-mediated uptake with a reported Ki of 1.3 nM. Condition category: normal nutrient_topic: Choline research collection; topical membership is not evidence of a direct dietary effect. plain_language: Blocking entry can limit choline availability even when choline is outside the cell. organism: Human transporter; Xenopus oocyte host tissue_or_cell_type: Plasma-membrane transport assay experimental_model: Human CHT1 expression in Xenopus oocytes limitations: Assay EC50 values and Hill coefficients are not dietary requirements or exact ion-coupling stoichiometry. exposure: Choline, sodium and chloride titrations; hemicholinium-3 inhibition evidence_span: {"source_cache": "artifacts/choline-research/11068039.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "f9885c7f9525456b2c9eac0865a1f86cda2cf8f26cd6a8e34c212218f3a22bd5", "start_char": 0, "end_char": 1088, "text_sha256": "f9885c7f9525456b2c9eac0865a1f86cda2cf8f26cd6a8e34c212218f3a22bd5"} [choline-p11068039] Functional characterization of the human high-affinity choline transporter. (2000). https://pubmed.ncbi.nlm.nih.gov/11068039/ DOI: 10.1016/s0014-5793(00)02134-7
    Complete structured claim and evidence

  3. Tested SLC5A7 missense variants caused a near-complete loss of CHT transport activity in cell models.

    Human SLC5A7 missense variants tested in the 2016 CMS study → Human CHT1-mediated choline uptake in expression assays source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/choline-research/27569547.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8f8b3acd919795de1aa33ccb5a616ccaaffc27e619990562f1bb69add7836d3d", "start_char": 0, "end_char": 1723, "text_sha256": "8f8b3acd919795de1aa33ccb5a616ccaaffc27e619990562f1bb69add7836d3d"}
    experimental_model
    Six-family genetics, expression assays and NMJ examination
    exposure
    Eleven recessive SLC5A7 mutations; missense variants tested functionally
    limitations
    Rare inherited disease with variant-specific effects; not a dietary-deficiency diagnosis or evidence that supplements repair the transporter.
    nutrient_topic
    Choline research collection; topical membership is not evidence of a direct dietary effect. · Choline
    organism
    Human variants; cell expression systems
    plain_language
    A damaged transporter can interrupt acetylcholine supply upstream of the synthesis enzyme.
    primary_references
    [choline-p27569547] Impaired Presynaptic High-Affinity Choline Transporter Causes a Congenital Myasthenic Syndrome with Episodic Apnea. (2016). https://pubmed.ncbi.nlm.nih.gov/27569547/ DOI: 10.1016/j.ajhg.2016.06.033
    tissue_or_cell_type
    Neuromuscular junction and choline transport
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Choline: metabolism, signaling and nutrient connections (2026-09-17) · lines 347–358

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Six-family genetics, expression assays and NMJ examination · source_derived_draft · unverified_draft

    ### choline-cht1-mutants Tested SLC5A7 missense variants caused a near-complete loss of CHT transport activity in cell models. Condition category: machinery_impairment nutrient_topic: Choline research collection; topical membership is not evidence of a direct dietary effect. plain_language: A damaged transporter can interrupt acetylcholine supply upstream of the synthesis enzyme. organism: Human variants; cell expression systems tissue_or_cell_type: Neuromuscular junction and choline transport experimental_model: Six-family genetics, expression assays and NMJ examination limitations: Rare inherited disease with variant-specific effects; not a dietary-deficiency diagnosis or evidence that supplements repair the transporter. exposure: Eleven recessive SLC5A7 mutations; missense variants tested functionally evidence_span: {"source_cache": "artifacts/choline-research/27569547.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8f8b3acd919795de1aa33ccb5a616ccaaffc27e619990562f1bb69add7836d3d", "start_char": 0, "end_char": 1723, "text_sha256": "8f8b3acd919795de1aa33ccb5a616ccaaffc27e619990562f1bb69add7836d3d"} [choline-p27569547] Impaired Presynaptic High-Affinity Choline Transporter Causes a Congenital Myasthenic Syndrome with Episodic Apnea. (2016). https://pubmed.ncbi.nlm.nih.gov/27569547/ DOI: 10.1016/j.ajhg.2016.06.033
    Complete structured claim and evidence

  4. Human CHT1-mediated choline uptake depended on Na+ in the oocyte assay.

    Sodium ion → Human CHT1-mediated choline uptake in expression assays source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/choline-research/11068039.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "f9885c7f9525456b2c9eac0865a1f86cda2cf8f26cd6a8e34c212218f3a22bd5", "start_char": 0, "end_char": 1088, "text_sha256": "f9885c7f9525456b2c9eac0865a1f86cda2cf8f26cd6a8e34c212218f3a22bd5"}
    experimental_model
    Human CHT1 expression in Xenopus oocytes
    exposure
    Choline, sodium and chloride titrations; hemicholinium-3 inhibition
    limitations
    Assay EC50 values and Hill coefficients are not dietary requirements or exact ion-coupling stoichiometry.
    nutrient_topic
    Choline research collection; topical membership is not evidence of a direct dietary effect. · Choline
    organism
    Human transporter; Xenopus oocyte host
    plain_language
    Na+ was part of the transport requirement, not just a background nutrient.
    primary_references
    [choline-p11068039] Functional characterization of the human high-affinity choline transporter. (2000). https://pubmed.ncbi.nlm.nih.gov/11068039/ DOI: 10.1016/s0014-5793(00)02134-7
    tissue_or_cell_type
    Plasma-membrane transport assay

    Choline: metabolism, signaling and nutrient connections (2026-09-17) · lines 295–306

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human CHT1 expression in Xenopus oocytes · source_derived_draft · unverified_draft

    ### choline-cht1-sodium Human CHT1-mediated choline uptake depended on Na+ in the oocyte assay. Condition category: normal nutrient_topic: Choline research collection; topical membership is not evidence of a direct dietary effect. plain_language: Na+ was part of the transport requirement, not just a background nutrient. organism: Human transporter; Xenopus oocyte host tissue_or_cell_type: Plasma-membrane transport assay experimental_model: Human CHT1 expression in Xenopus oocytes limitations: Assay EC50 values and Hill coefficients are not dietary requirements or exact ion-coupling stoichiometry. exposure: Choline, sodium and chloride titrations; hemicholinium-3 inhibition evidence_span: {"source_cache": "artifacts/choline-research/11068039.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "f9885c7f9525456b2c9eac0865a1f86cda2cf8f26cd6a8e34c212218f3a22bd5", "start_char": 0, "end_char": 1088, "text_sha256": "f9885c7f9525456b2c9eac0865a1f86cda2cf8f26cd6a8e34c212218f3a22bd5"} [choline-p11068039] Functional characterization of the human high-affinity choline transporter. (2000). https://pubmed.ncbi.nlm.nih.gov/11068039/ DOI: 10.1016/s0014-5793(00)02134-7
    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