Component

Human neutral amino acid transporter B0AT1 / SLC6A19

Human neutral amino acid transporter B0AT1 / SLC6A19. Species, exposure and limitations are retained in each linked claim.

7 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. Human B0AT1 D173N and P265L variants retained activation by coexpressed mouse ACE2 but not human collectrin; A69T and R240Q were not activated by either partner.

    Human neutral amino acid transporter B0AT1 / SLC6A19 → Accessory-protein response of human B0AT1 variants source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary full text
    experimental_model
    Human transporter variants in Xenopus oocytes with mouse ACE2 or human collectrin.
    limitations
    Mixed-species expression system; not a direct measurement of each patient intestine or kidney.
    nutrient_topic
    L-Isoleucine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Isoleucine
    plain_language
    The same transporter mutation can behave differently with different helper proteins.
    primary_references
    Tissue-specific amino acid transporter partners ACE2 and collectrin differentially interact with hartnup mutations. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19185582/ · DOI 10.1053/j.gastro.2008.10.055
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Isoleucine: transport, translation, catabolism and cross-nutrient mechanisms (2026-09-19) · lines 34–40

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human transporter variants in Xenopus oocytes with mouse ACE2 or human collectrin. · source_derived_draft · unverified_draft

    ## isoleucine-hartnup-partners The same transporter mutation can behave differently with different helper proteins. Human B0AT1 D173N and P265L variants retained activation by coexpressed mouse ACE2 but not human collectrin; A69T and R240Q were not activated by either partner. Model: Human transporter variants in Xenopus oocytes with mouse ACE2 or human collectrin. Limitations: Mixed-species expression system; not a direct measurement of each patient intestine or kidney. Evidence access: Primary full text Tissue-specific amino acid transporter partners ACE2 and collectrin differentially interact with hartnup mutations. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19185582/ · DOI 10.1053/j.gastro.2008.10.055
    Complete structured claim and evidence

  2. Tested Hartnup-associated SLC6A19 variants reduced neutral amino acid transport in vitro.

    Human neutral amino acid transporter B0AT1 / SLC6A19 → Intestinal and renal neutral amino acid transport source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/sodium-research/15286788.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "72277489510231d6da07dacf086404f5f069094a47d7a1a2de9a8392556c3a14", "start_char": 0, "end_char": 1040, "text_sha256": "72277489510231d6da07dacf086404f5f069094a47d7a1a2de9a8392556c3a14"}
    experimental_model
    Human genetic mapping and heterologous transport-function tests
    exposure
    Hartnup-associated variants versus normal transporter
    limitations
    Not every clinical feature of Hartnup disorder was explained; no direct test here of niacin supplementation or sodium shortage.
    nutrient_topic
    Sodium research collection; topical membership is not evidence of a direct dietary effect. · Sodium
    organism
    Human SLC6A19
    plain_language
    Even with sodium and food present, a damaged transporter can limit nutrient transport.
    primary_references
    [sodium-p15286788] Hartnup disorder is caused by mutations in the gene encoding the neutral amino acid transporter SLC6A19. (2004). https://pubmed.ncbi.nlm.nih.gov/15286788/ DOI: 10.1038/ng1406
    tissue_or_cell_type
    Kidney/intestine transporter; expression assays
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Sodium: gradients, nutrient transport, fluid regulation and loss states (2026-09-17) · lines 603–614

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human genetic mapping and heterologous transport-function tests · source_derived_draft · unverified_draft

    ### sodium-b0at1-loss Tested Hartnup-associated SLC6A19 variants reduced neutral amino acid transport in vitro. Condition category: machinery_impairment nutrient_topic: Sodium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Even with sodium and food present, a damaged transporter can limit nutrient transport. organism: Human SLC6A19 tissue_or_cell_type: Kidney/intestine transporter; expression assays experimental_model: Human genetic mapping and heterologous transport-function tests limitations: Not every clinical feature of Hartnup disorder was explained; no direct test here of niacin supplementation or sodium shortage. exposure: Hartnup-associated variants versus normal transporter evidence_span: {"source_cache": "artifacts/sodium-research/15286788.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "72277489510231d6da07dacf086404f5f069094a47d7a1a2de9a8392556c3a14", "start_char": 0, "end_char": 1040, "text_sha256": "72277489510231d6da07dacf086404f5f069094a47d7a1a2de9a8392556c3a14"} [sodium-p15286788] Hartnup disorder is caused by mutations in the gene encoding the neutral amino acid transporter SLC6A19. (2004). https://pubmed.ncbi.nlm.nih.gov/15286788/ DOI: 10.1038/ng1406
    Complete structured claim and evidence

  3. SLC6A19 functioned as a sodium-dependent, chloride-independent neutral amino acid transporter.

    Human neutral amino acid transporter B0AT1 / SLC6A19 → Neutral amino acids (assay substrates specified per claim) source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/sodium-research/15286788.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "72277489510231d6da07dacf086404f5f069094a47d7a1a2de9a8392556c3a14", "start_char": 0, "end_char": 1040, "text_sha256": "72277489510231d6da07dacf086404f5f069094a47d7a1a2de9a8392556c3a14"}
    experimental_model
    Human genetic mapping and heterologous transport-function tests
    exposure
    Hartnup-associated variants versus normal transporter
    limitations
    Not every clinical feature of Hartnup disorder was explained; no direct test here of niacin supplementation or sodium shortage.
    nutrient_topic
    Sodium research collection; topical membership is not evidence of a direct dietary effect. · Sodium
    organism
    Human SLC6A19
    plain_language
    Sodium coupling is also used to absorb or recover some amino acids.
    primary_references
    [sodium-p15286788] Hartnup disorder is caused by mutations in the gene encoding the neutral amino acid transporter SLC6A19. (2004). https://pubmed.ncbi.nlm.nih.gov/15286788/ DOI: 10.1038/ng1406
    tissue_or_cell_type
    Kidney/intestine transporter; expression assays
    transport_effect
    raises Sodium-dependent neutral amino acid transport, which is inward.
    transport_pool
    the expressing cell Sodium-dependent neutral amino acid transport, which is inward.

    Sodium: gradients, nutrient transport, fluid regulation and loss states (2026-09-17) · lines 590–601

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human genetic mapping and heterologous transport-function tests · source_derived_draft · unverified_draft

    ### sodium-b0at1-transport SLC6A19 functioned as a sodium-dependent, chloride-independent neutral amino acid transporter. Condition category: normal nutrient_topic: Sodium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Sodium coupling is also used to absorb or recover some amino acids. organism: Human SLC6A19 tissue_or_cell_type: Kidney/intestine transporter; expression assays experimental_model: Human genetic mapping and heterologous transport-function tests limitations: Not every clinical feature of Hartnup disorder was explained; no direct test here of niacin supplementation or sodium shortage. exposure: Hartnup-associated variants versus normal transporter evidence_span: {"source_cache": "artifacts/sodium-research/15286788.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "72277489510231d6da07dacf086404f5f069094a47d7a1a2de9a8392556c3a14", "start_char": 0, "end_char": 1040, "text_sha256": "72277489510231d6da07dacf086404f5f069094a47d7a1a2de9a8392556c3a14"} [sodium-p15286788] Hartnup disorder is caused by mutations in the gene encoding the neutral amino acid transporter SLC6A19. (2004). https://pubmed.ncbi.nlm.nih.gov/15286788/ DOI: 10.1038/ng1406
    Complete structured claim and evidence

  4. B0AT1/SLC6A19 transports neutral amino acids including phenylalanine during intestinal absorption and renal reuptake.

    Human neutral amino acid transporter B0AT1 / SLC6A19 → L-Phenylalanine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human B0AT1 structural and transport study; established physiological role described in abstract.
    limitations
    Transporter identity does not specify a universal saturation threshold.
    nutrient_topic
    L-Phenylalanine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Phenylalanine
    plain_language
    The gut and kidney transport machinery helps determine phenylalanine availability.
    primary_references
    Structure-guided development of a potent human B0AT1 inhibitor effective in a mouse model of phenylketonuria. · 2026 · https://pubmed.ncbi.nlm.nih.gov/42350764/ · DOI 10.1038/s42003-026-10535-y
    transport_effect
    raises Recorded as acting during intestinal absorption and renal reuptake, both of which are inward.
    transport_pool
    the enterocyte and tubule cell interior Recorded as acting during intestinal absorption and renal reuptake, both of which are inward.

    L-Phenylalanine: transport, protein synthesis, cofactor recycling and cross-nutrient mechanisms (2026-09-19) · lines 166–172

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human B0AT1 structural and transport study; established physiological role described in abstract. · source_derived_draft · unverified_draft

    ## l-phenylalanine-renal-transporter The gut and kidney transport machinery helps determine phenylalanine availability. B0AT1/SLC6A19 transports neutral amino acids including phenylalanine during intestinal absorption and renal reuptake. Model: Human B0AT1 structural and transport study; established physiological role described in abstract. Limitations: Transporter identity does not specify a universal saturation threshold. Evidence access: Primary abstract Structure-guided development of a potent human B0AT1 inhibitor effective in a mouse model of phenylketonuria. · 2026 · https://pubmed.ncbi.nlm.nih.gov/42350764/ · DOI 10.1038/s42003-026-10535-y
    Complete structured claim and evidence

  5. Silencing SLC6A19 reduced citrulline uptake in human HK-2 renal cells.

    Human neutral amino acid transporter B0AT1 / SLC6A19 → Apical citrulline uptake in renal proximal tubular cells source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/citrulline-research/19322909.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "f466fcced77ee9fe7a97f010112a035332d513382d13e6187d10bc02be152ece", "start_char": 0, "end_char": 1531, "text_sha256": "f466fcced77ee9fe7a97f010112a035332d513382d13e6187d10bc02be152ece"}
    experimental_model
    Apical transport kinetics and transporter knockdown
    exposure
    Citrulline uptake on permeable supports; SLC6A19 or SLC7A9 silencing
    limitations
    Renal evidence must not be relabeled as a demonstrated human intestinal transport mechanism.
    nutrient_topic
    Citrulline research collection; topical membership is not evidence of a direct dietary effect. · L-Citrulline
    organism
    Human HK-2 cells; rat cultures studied separately
    plain_language
    A neutral-amino-acid transporter contributes to kidney uptake.
    primary_references
    [citrulline-p19322909] Transport characteristics of L-citrulline in renal apical membrane of proximal tubular cells. (2009). https://pubmed.ncbi.nlm.nih.gov/19322909/ DOI: 10.1002/bdd.653
    tissue_or_cell_type
    Renal proximal tubular epithelium

    Citrulline: arginine recycling, nitrogen disposal and nutrient connections (2026-09-17) · lines 398–409

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Apical transport kinetics and transporter knockdown · source_derived_draft · unverified_draft

    ### citrulline-renal-b0at1 Silencing SLC6A19 reduced citrulline uptake in human HK-2 renal cells. Condition category: normal nutrient_topic: Citrulline research collection; topical membership is not evidence of a direct dietary effect. plain_language: A neutral-amino-acid transporter contributes to kidney uptake. organism: Human HK-2 cells; rat cultures studied separately tissue_or_cell_type: Renal proximal tubular epithelium experimental_model: Apical transport kinetics and transporter knockdown limitations: Renal evidence must not be relabeled as a demonstrated human intestinal transport mechanism. exposure: Citrulline uptake on permeable supports; SLC6A19 or SLC7A9 silencing evidence_span: {"source_cache": "artifacts/citrulline-research/19322909.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "f466fcced77ee9fe7a97f010112a035332d513382d13e6187d10bc02be152ece", "start_char": 0, "end_char": 1531, "text_sha256": "f466fcced77ee9fe7a97f010112a035332d513382d13e6187d10bc02be152ece"} [citrulline-p19322909] Transport characteristics of L-citrulline in renal apical membrane of proximal tubular cells. (2009). https://pubmed.ncbi.nlm.nih.gov/19322909/ DOI: 10.1002/bdd.653
    Complete structured claim and evidence

What acts on it

  1. A designed inhibitor occupied an allosteric B0AT1 pocket about 17 angstroms from the substrate site, stabilized an outward-occluded state and blocked transport with submicromolar IC50.

    Experimental B0AT1 inhibitor from the 2026 structure-guided study → Human neutral amino acid transporter B0AT1 / SLC6A19 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human transporter cryo-EM and human/mouse transport inhibition assays.
    limitations
    Compound identity is not resolved in the accessed abstract; this is experimental pharmacology, not a supplement recommendation.
    nutrient_topic
    L-Phenylalanine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Phenylalanine
    plain_language
    Transport can be blocked at a site away from where the amino acid binds.
    primary_references
    Structure-guided development of a potent human B0AT1 inhibitor effective in a mouse model of phenylketonuria. · 2026 · https://pubmed.ncbi.nlm.nih.gov/42350764/ · DOI 10.1038/s42003-026-10535-y

    L-Phenylalanine: transport, protein synthesis, cofactor recycling and cross-nutrient mechanisms (2026-09-19) · lines 174–180

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human transporter cryo-EM and human/mouse transport inhibition assays. · source_derived_draft · unverified_draft

    ## l-phenylalanine-renal-inhibition Transport can be blocked at a site away from where the amino acid binds. A designed inhibitor occupied an allosteric B0AT1 pocket about 17 angstroms from the substrate site, stabilized an outward-occluded state and blocked transport with submicromolar IC50. Model: Human transporter cryo-EM and human/mouse transport inhibition assays. Limitations: Compound identity is not resolved in the accessed abstract; this is experimental pharmacology, not a supplement recommendation. Evidence access: Primary abstract Structure-guided development of a potent human B0AT1 inhibitor effective in a mouse model of phenylketonuria. · 2026 · https://pubmed.ncbi.nlm.nih.gov/42350764/ · DOI 10.1038/s42003-026-10535-y
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Oral experimental B0AT1 inhibition increased urinary phenylalanine and lowered plasma phenylalanine in PKU-model mice.

    Experimental B0AT1 inhibitor from the 2026 structure-guided study → Mouse urinary phenylalanine excretion source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    PKU-model mice; oral dosing, dose not specified in accessed abstract.
    limitations
    Human efficacy and effects on other neutral amino acids are not established here.
    nutrient_topic
    L-Phenylalanine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Phenylalanine
    plain_language
    A transporter intervention can lower blood levels by increasing urinary loss.
    primary_references
    Structure-guided development of a potent human B0AT1 inhibitor effective in a mouse model of phenylketonuria. · 2026 · https://pubmed.ncbi.nlm.nih.gov/42350764/ · DOI 10.1038/s42003-026-10535-y

    L-Phenylalanine: transport, protein synthesis, cofactor recycling and cross-nutrient mechanisms (2026-09-19) · lines 182–188

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · PKU-model mice; oral dosing, dose not specified in accessed abstract. · source_derived_draft · unverified_draft

    ## l-phenylalanine-renal-excretion A transporter intervention can lower blood levels by increasing urinary loss. Oral experimental B0AT1 inhibition increased urinary phenylalanine and lowered plasma phenylalanine in PKU-model mice. Model: PKU-model mice; oral dosing, dose not specified in accessed abstract. Limitations: Human efficacy and effects on other neutral amino acids are not established here. Evidence access: Primary abstract Structure-guided development of a potent human B0AT1 inhibitor effective in a mouse model of phenylketonuria. · 2026 · https://pubmed.ncbi.nlm.nih.gov/42350764/ · DOI 10.1038/s42003-026-10535-y
    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.

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