Component
LCK phosphorylated at Y505
Independent entity for contextual scientific-audit claims; no universal nutritional effect implied.
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.
Where it participates (unsigned role)
CD45 removal of inhibitory LCK Y505 phosphorylation can favor an open activation-competent state.
Experimental context and source evidence
- cell_type
- T-cell and biochemical assays
- experimental_model
- Biochemical LCK/CD45 phosphorylation assays; CD45-deficient cells and LCK binding/phosphorylation experiments
- limitations
- Net effect depends on concentration/localization and both sites; no selenium-dependent site effect established.
- organism
- Mammalian biochemical and T-cell systems
Selenium: literature corrections and mechanism additions · lines 1275–1286
Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · Biochemical LCK/CD45 phosphorylation assays; CD45-deficient cells and LCK binding/phosphorylation experiments · secondary_verified · secondary_verified
## cd45-y505 Removing the Y505 phosphate can release LCK inhibition. CD45 removal of inhibitory LCK Y505 phosphorylation can favor an open activation-competent state. Organism: Mammalian biochemical and T-cell systems Cell type: T-cell and biochemical assays Experimental model: Biochemical LCK/CD45 phosphorylation assays; CD45-deficient cells and LCK binding/phosphorylation experiments Limitations: Net effect depends on concentration/localization and both sites; no selenium-dependent site effect established. Primary reference: [The noncatalytic domains of Lck regulate its dephosphorylation by CD45](https://pubmed.ncbi.nlm.nih.gov/12922168/) Primary reference: [CD45 specifically modulates binding of Lck to a phosphopeptide encompassing the negative regulatory tyrosine of Lck.](https://pubmed.ncbi.nlm.nih.gov/8428589/)
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.