Component
Lys48-polyubiquitinated protein substrates
Protein-bound site or substrate state, not free dietary L-lysine. Sequence and assay context limit the relationship.
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
The 26S proteasome degrades suitable Lys48-polyubiquitinated substrates; chain trimming permits continued substrate loading.
Experimental context and source evidence
- experimental_model
- Biochemical proteasome/polyubiquitin assays.
- limitations
- Recognition and substrate accessibility matter; this is not a prediction that dietary lysine accelerates protein destruction.
- organism
- Experimental proteasome system
- plain_language
- A lysine-linked tag can help deliver a protein for breakdown.
- primary_references
- [proteasome-trimming-2011] Ubiquitin chain trimming recycles the substrate binding sites of the 26 S proteasome and promotes degradation of lysine 48-linked polyubiquitin conjugates (2011). https://pubmed.ncbi.nlm.nih.gov/21632534/
- tissue_or_cell_type
- Not specified as a whole tissue; see experimental model.
L-Lysine: mechanism-first literature curation (2026-09-17) · lines 608–616
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Biochemical proteasome/polyubiquitin assays. · source_derived_draft · unverified_draft
### k48-proteasome-degradation The 26S proteasome degrades suitable Lys48-polyubiquitinated substrates; chain trimming permits continued substrate loading. Plain language: A lysine-linked tag can help deliver a protein for breakdown. Condition category: normal organism: Experimental proteasome system tissue_or_cell_type: Not specified as a whole tissue; see experimental model. experimental_model: Biochemical proteasome/polyubiquitin assays. limitations: Recognition and substrate accessibility matter; this is not a prediction that dietary lysine accelerates protein destruction. [proteasome-trimming-2011] Ubiquitin chain trimming recycles the substrate binding sites of the 26 S proteasome and promotes degradation of lysine 48-linked polyubiquitin conjugates (2011). https://pubmed.ncbi.nlm.nih.gov/21632534/
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.