{
 "meta": {
  "api_version": "1.0.0",
  "dataset_version": "2.0.1+unreleased",
  "live_matches_release": false,
  "archived_release": {
   "version": "2.0.1",
   "version_doi": "10.5281/zenodo.23090261",
   "date": "2026-10-01",
   "studies": 428
  },
  "data_fingerprint": "21bd609b55973b7b5b84e545fdde629d79115243854f1595680c534e6e1ef96f",
  "corpus_snapshot": "2026-11-02T19:05:06+0100",
  "source_commit": "1e9de0d56d4ea503818c4095460addc4a0c7f4a3",
  "license": "CC-BY-4.0",
  "cite": "Barton O. Oliver's mTOR Atlas (live data, not an archived version; give corpus_snapshot and source_commit). doi:10.5281/zenodo.22059963",
  "docs": "https://mtor-atlas.org/api/"
 },
 "data": {
  "id": "LYSO-MTORC1",
  "claim": "Lysosome required-for mTORC1",
  "source": {
   "name": "Lysosome",
   "entity": "lysosome"
  },
  "target": {
   "name": "mTORC1",
   "entity": "mtorc1"
  },
  "effect": "required-for",
  "type": "localisation",
  "directness": "direct",
  "timescale": "minutes",
  "compartment": "lyso",
  "map_band": "lyso",
  "species": [
   "human cells"
  ],
  "mechanism": "In the canonical nutrient-dependent route, mTORC1 has to reach the lysosomal surface to be switched on, because that is where Rheb is waiting. SAN2010 showed what happens when you take the first step away: anchoring mTORC1 to the lysosome permanently makes the pathway amino-acid insensitive and independent of Rag and Ragulator, but still dependent on Rheb. Recruitment and activation are two steps, and that experiment separates them. The requirement is stated for this route, not for every pool of mTOR in the cell.",
  "mechanism_beginner": "In the amino-acid route, mTORC1 has to travel to the lysosome before it can work, because its activator Rheb waits there. Getting it there and switching it on are two different steps: when researchers glued mTORC1 to the lysosome so it no longer had to be delivered, amino acids stopped making any difference, but the activator was still needed.",
  "context": null,
  "boundary": "Scoped to amino-acid-driven activation. Live BRET imaging in this corpus (BOU2020) resolves mTOR activity in the cytosol, at the lysosome, in the nucleus and near mitochondria, so mTOR signalling is measurably not one pool. This map draws the lysosomal route and keeps the other localisations declared as open rather than asserting there are none. FER2024 refines this further: lysosomal mTORC1 (fed by local lysosomal proteolysis) and cytoplasmic mTORC1 (fed by exogenous amino acids) phosphorylate distinct downstream substrates — the lysosome is required for one regulatory sub-pool of mTORC1, not for all of it.",
  "boundary_tags": [
   "nutrient-state-dependent"
  ],
  "conflict": null,
  "note": null,
  "consensus_contested": false,
  "curation_contested": false,
  "contested": false,
  "confidence": {
   "mechanistic": "high",
   "human_relevance": "plausible",
   "consensus": "established"
  },
  "evidence": {
   "kind": "Genetic epistasis",
   "strongest": {
    "code": "M",
    "label": "Molecular — cells, biochemistry, structure"
   },
   "supporting": [
    "SAN2010",
    "ZON2011",
    "FER2024",
    "KOR2011",
    "CUI2025"
   ],
   "conflicting": []
  },
  "external_refs": [],
  "reviewed": null,
  "updated": null,
  "checked": null,
  "review_status": "unreviewed",
  "reviewer": null,
  "curation_status": "Proposed",
  "url": "https://mtor-atlas.org/relation/LYSO-MTORC1/",
  "api_url": "https://mtor-atlas.org/api/v1/relations/LYSO-MTORC1.json"
 }
}