Component
Human AXL receptor tyrosine kinase
Human AXL receptor tyrosine kinase. Species, exposure and limitations are retained in each linked claim.
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 acts on it
Functional AXL activation by GAS6 in the reporter system depended on vitamin K-mediated carboxylation and phosphatidylserine engagement.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/k2-research/29176978.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "14dfae68318cd2654ee423539418eb489da66e26117e35473e99986b29b8efd7", "start_char": 0, "end_char": 1704, "text_sha256": "14dfae68318cd2654ee423539418eb489da66e26117e35473e99986b29b8efd7"}
- experimental_model
- TAM reporter cells and GAS6 domain/point mutagenesis
- exposure
- Warfarin, Gla/EGF mutations and PS-positive cells or vesicles
- limitations
- Receptor binding and receptor activation are different endpoints; no clinical K2 immune benefit was tested.
- nutrient_topic
- Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin K2 / menaquinone family
- organism
- Recombinant human GAS6 and TAM reporter systems
- plain_language
- A modified signaling protein needs the right membrane surface to activate its receptor.
- primary_references
- [k2-p29176978] Requirement of Gamma-Carboxyglutamic Acid Modification and Phosphatidylserine Binding for the Activation of Tyro3, Axl, and Mertk Receptors by Growth Arrest-Specific 6. (2017). https://pubmed.ncbi.nlm.nih.gov/29176978/ DOI: 10.3389/fimmu.2017.01521
- tissue_or_cell_type
- Phosphatidylserine-bearing surfaces and receptors
Vitamin K2: menaquinone forms, carboxylation, recycling and nutrient interactions (2026-09-17) · lines 591–602
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · TAM reporter cells and GAS6 domain/point mutagenesis · source_derived_draft · unverified_draft
### k2-gas6-axl Functional AXL activation by GAS6 in the reporter system depended on vitamin K-mediated carboxylation and phosphatidylserine engagement. Condition category: normal nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: A modified signaling protein needs the right membrane surface to activate its receptor. organism: Recombinant human GAS6 and TAM reporter systems tissue_or_cell_type: Phosphatidylserine-bearing surfaces and receptors experimental_model: TAM reporter cells and GAS6 domain/point mutagenesis limitations: Receptor binding and receptor activation are different endpoints; no clinical K2 immune benefit was tested. exposure: Warfarin, Gla/EGF mutations and PS-positive cells or vesicles evidence_span: {"source_cache": "artifacts/k2-research/29176978.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "14dfae68318cd2654ee423539418eb489da66e26117e35473e99986b29b8efd7", "start_char": 0, "end_char": 1704, "text_sha256": "14dfae68318cd2654ee423539418eb489da66e26117e35473e99986b29b8efd7"} [k2-p29176978] Requirement of Gamma-Carboxyglutamic Acid Modification and Phosphatidylserine Binding for the Activation of Tyro3, Axl, and Mertk Receptors by Growth Arrest-Specific 6. (2017). https://pubmed.ncbi.nlm.nih.gov/29176978/ DOI: 10.3389/fimmu.2017.01521
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.