{"id":"7ab06eb8-95c1-52b3-9bfc-d0b3753e3fec","stable_key":"63ce713e-6aea-59f6-9896-ca30e010b2ce:l-tyrosine-yrs-proteolysis","predicate":"enhances","statement":"MMP cleavage of YARS1 increased TLR2 signaling, TNF secretion and chemotaxis relative to unprocessed YARS1.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"cb834744-d15d-5abc-bc87-1704a5d4ac03","mechanism_event_label":"Protease activity changes the strength of an extracellular signal.","subject":{"id":"ecfa9184-22c1-5465-8df6-ddf33cee0bbf","slug":"mmp8","display_name":"Human matrix metalloproteinase 8 / MMP8","entity_type_key":"protein"},"object":{"id":"f55276d4-1d1f-5329-9881-1c9592483d8c","slug":"human-yars-proteolytic-inflammatory-signaling","display_name":"Human YARS1 proteolysis-dependent inflammatory signaling","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"cb834744-d15d-5abc-bc87-1704a5d4ac03","stable_key":"63ce713e-6aea-59f6-9896-ca30e010b2ce:l-tyrosine-yrs-proteolysis-event","event_type":"observed_relationship","label":"Protease activity changes the strength of an extracellular signal.","description":"MMP cleavage of YARS1 increased TLR2 signaling, TNF secretion and chemotaxis relative to unprocessed YARS1.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"ecfa9184-22c1-5465-8df6-ddf33cee0bbf","slug":"mmp8","display_name":"Human matrix metalloproteinase 8 / MMP8","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"f55276d4-1d1f-5329-9881-1c9592483d8c","slug":"human-yars-proteolytic-inflammatory-signaling","display_name":"Human YARS1 proteolysis-dependent inflammatory signaling","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"bcfef85f-831d-5439-ba51-1aef4b090441","slug":"l-tyrosine","display_name":"L-Tyrosine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"1e70f8cb-144f-5c63-b862-0c8670840077","slug":"yars1","display_name":"Human cytosolic tyrosyl-tRNA synthetase / YARS1","entity_type_key":"protein"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"754f79df-5314-5c4a-ae4f-77193d72489d","slug":"mmp7","display_name":"Human matrix metalloproteinase 7 / MMP7","entity_type_key":"protein"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""},{"entity":{"id":"7d88fac7-eee3-541d-a202-e73c3f04186e","slug":"tlr2","display_name":"Human Toll-like receptor 2 / TLR2","entity_type_key":"protein"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":5,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary full text and abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Protein cleavage and macrophage assays; MMP7 and MMP8 among tested enzymes.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"A proposed feed-forward inflammatory loop still requires in vivo testing.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"L-Tyrosine collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"l-tyrosine","display_name":"L-Tyrosine","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"Protease activity changes the strength of an extracellular signal.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Moonlighting matrix metalloproteinase substrates: Enhancement of proinflammatory functions of extracellular tyrosyl-tRNA synthetase upon cleavage. · 2020 · https://pubmed.ncbi.nlm.nih.gov/31771979/ · DOI 10.1074/jbc.RA119.010486","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"7d7a7334-3f43-5f1d-b139-683a0883fcc6","evidence_kind":"source_excerpt","locator":"Lines 116-122","start_line":116,"end_line":122,"excerpt":"## l-tyrosine-yrs-proteolysis\nProtease activity changes the strength of an extracellular signal.\nMMP cleavage of YARS1 increased TLR2 signaling, TNF secretion and chemotaxis relative to unprocessed YARS1.\nModel: Protein cleavage and macrophage assays; MMP7 and MMP8 among tested enzymes.\nLimitations: A proposed feed-forward inflammatory loop still requires in vivo testing.\nEvidence access: Primary full text and abstract\nMoonlighting matrix metalloproteinase substrates: Enhancement of proinflammatory functions of extracellular tyrosyl-tRNA synthetase upon cleavage. · 2020 · https://pubmed.ncbi.nlm.nih.gov/31771979/ · DOI 10.1074/jbc.RA119.010486","model_system":"Protein cleavage and macrophage assays; MMP7 and MMP8 among tested enzymes.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Original curation paraphrase; evidence access and experimental limitations specified.","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"12917df2-c6e0-5b61-850f-dbff6d4b4d30","stable_key":"import-63ce713e-6aea-59f6-9896-ca30e010b2ce","title":"L-Tyrosine: catecholamines, thyroid chemistry, pigment, metabolism and cross-nutrient mechanisms (2026-09-19)","document_type":"imported_text","citation_label":"AI-assisted research curation; primary references, access levels and experimental limitations individually identified. 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