Component
Mouse autophagy initiating kinase / Ulk1
Context-specific entity; species, compartment and exposure are stated on each claim.
2 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
Under glucose starvation AMPK directly activated Ulk1 through Ser317 and Ser777 phosphorylation.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Mammalian cell experiments with study Ulk1 constructs; mouse residue numbering.
- limitations
- Do not transfer residue numbers to human ULK1 or infer a fasting-hour threshold.
- nutrient_topic
- Fasting physiological-state collection; human protocols, cellular deprivation and refeeding are distinguished. · Fasting / abstention from energy intake
- plain_language
- Energy stress can act on the autophagy-starting machinery.
- primary_references
- AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21258367/ · DOI 10.1038/ncb2152
Fasting: fuel switching, nutrient sensing, ketone signaling, nutrient dependencies and refeeding (2026-09-18) · lines 296–302
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Mammalian cell experiments with study Ulk1 constructs; mouse residue numbering. · source_derived_draft · unverified_draft
## fast-ampk-ulk Energy stress can act on the autophagy-starting machinery. Under glucose starvation AMPK directly activated Ulk1 through Ser317 and Ser777 phosphorylation. Model: Mammalian cell experiments with study Ulk1 constructs; mouse residue numbering. Limitations: Do not transfer residue numbers to human ULK1 or infer a fasting-hour threshold. Evidence access: Primary abstract AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21258367/ · DOI 10.1038/ncb2152
Complete structured claim and evidence
Where it participates (unsigned role)
High mTOR activity phosphorylated Ulk1 Ser757 and disrupted its interaction with AMPK.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Cellular kinase and autophagy assays; mouse Ulk1 numbering.
- limitations
- Specific signaling mechanism, not a whole-body autophagic-flux measurement.
- nutrient_topic
- Fasting physiological-state collection; human protocols, cellular deprivation and refeeding are distinguished. · Fasting / abstention from energy intake
- plain_language
- Nutrient sufficiency can restrain this initiation route.
- primary_references
- AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21258367/ · DOI 10.1038/ncb2152
Fasting: fuel switching, nutrient sensing, ketone signaling, nutrient dependencies and refeeding (2026-09-18) · lines 304–310
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Cellular kinase and autophagy assays; mouse Ulk1 numbering. · source_derived_draft · unverified_draft
## fast-mtor-ulk Nutrient sufficiency can restrain this initiation route. High mTOR activity phosphorylated Ulk1 Ser757 and disrupted its interaction with AMPK. Model: Cellular kinase and autophagy assays; mouse Ulk1 numbering. Limitations: Specific signaling mechanism, not a whole-body autophagic-flux measurement. Evidence access: Primary abstract AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21258367/ · DOI 10.1038/ncb2152
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.