Component
y+LAT1-4F2hc complex
Independent protein complex record; interpretation is limited by each linked claim and its study context.
1 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 it acts on
SLC7A7-SLC3A2 exchanges intracellular cationic amino acids including lysine for extracellular neutral amino acids with sodium.
Experimental context and source evidence
- experimental_model
- Human/mouse heterodimer expression and exchange assays
- limitations
- Neutral-substrate transport is sodium-dependent; lysine binding itself should not be mislabeled a sodium cotransport step.
- organism
- Homo sapiens
- plain_language
- This route helps lysine leave epithelial cells toward blood.
- primary_references
- [pfeiffer1999yl] Amino acid transport of y+L-type by heterodimers of 4F2hc/CD98 and members of the glycoprotein-associated amino acid transporter family. (1999). https://pubmed.ncbi.nlm.nih.gov/9878049/ DOI: 10.1093/emboj/18.1.49
- tissue_or_cell_type
- Basolateral intestinal and renal epithelial membranes
- transport_effect
- lowers Exchanges intracellular cationic amino acids including lysine for extracellular neutral amino acids, so lysine leaves the cell.
- transport_pool
- the enterocyte interior Exchanges intracellular cationic amino acids including lysine for extracellular neutral amino acids, so lysine leaves the cell.
L-Lysine: mechanism-first literature curation (2026-09-17) · lines 34–42
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human/mouse heterodimer expression and exchange assays · source_derived_draft · unverified_draft
### basolateral-lysine-exchange SLC7A7-SLC3A2 exchanges intracellular cationic amino acids including lysine for extracellular neutral amino acids with sodium. Plain language: This route helps lysine leave epithelial cells toward blood. Condition category: normal organism: Homo sapiens tissue_or_cell_type: Basolateral intestinal and renal epithelial membranes experimental_model: Human/mouse heterodimer expression and exchange assays limitations: Neutral-substrate transport is sodium-dependent; lysine binding itself should not be mislabeled a sodium cotransport step. [pfeiffer1999yl] Amino acid transport of y+L-type by heterodimers of 4F2hc/CD98 and members of the glycoprotein-associated amino acid transporter family. (1999). https://pubmed.ncbi.nlm.nih.gov/9878049/ DOI: 10.1093/emboj/18.1.49
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.