{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Coppola V"],"funding":["Associazione Italiana per la Ricerca sul Cancro","Ricerca corrente program of Ministero della Salute","Intesa Sanpaolo Innovation Center"],"pagination":["2733-2751"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10472876"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["19(10)"],"pubmed_abstract":["Apoptosis is a tightly controlled cell death program executed by proteases, the so-called caspases. It plays an important role in tissue homeostasis and is often dysregulated in cancer. Here, we identified FYCO1, a protein that promotes microtubule plus end-directed transport of autophagic and endosomal vesicles as a molecular interaction partner of activated CASP8 (caspase 8). The absence of FYCO1 sensitized cells to basal and TNFSF10/TRAIL-induced apoptosis by receptor accumulation and stabilization of the Death Inducing Signaling Complex (DISC). Loss of FYCO1 resulted in impaired transport of TNFRSF10B/TRAIL-R2/DR5 (TNF receptor superfamily member 10b) to the lysosomes in TNFSF10/TRAIL-stimulated cells. More in detail, we show that FYCO1 interacted via its C-terminal GOLD domain with th"],"journal":["Autophagy"],"pubmed_title":["The autophagic protein FYCO1 controls TNFRSF10/TRAIL receptor induced apoptosis and is inactivated by CASP8 (caspase 8)."],"pmcid":["PMC10472876"],"funding_grant_id":["RCR-2019-23669115","IG Grant 2019","ISP-HGF29_0001"],"pubmed_authors":["Pasquini L","Warnken U","Biffoni M","Coppola V","De Maria R","Falchi M","Marino I","Haas TL"],"additional_accession":[]},"is_claimable":false,"name":"The autophagic protein FYCO1 controls TNFRSF10/TRAIL receptor induced apoptosis and is inactivated by CASP8 (caspase 8).","description":"Apoptosis is a tightly controlled cell death program executed by proteases, the so-called caspases. It plays an important role in tissue homeostasis and is often dysregulated in cancer. Here, we identified FYCO1, a protein that promotes microtubule plus end-directed transport of autophagic and endosomal vesicles as a molecular interaction partner of activated CASP8 (caspase 8). The absence of FYCO1 sensitized cells to basal and TNFSF10/TRAIL-induced apoptosis by receptor accumulation and stabilization of the Death Inducing Signaling Complex (DISC). Loss of FYCO1 resulted in impaired transport of TNFRSF10B/TRAIL-R2/DR5 (TNF receptor superfamily member 10b) to the lysosomes in TNFSF10/TRAIL-stimulated cells. More in detail, we show that FYCO1 interacted via its C-terminal GOLD domain with th","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Oct","modification":"2026-05-17T03:12:12.589Z","creation":"2025-02-19T01:17:58.84Z"},"accession":"S-EPMC10472876","cross_references":{"pubmed":["37418591"],"doi":["10.1080/15548627.2023.2229656"]}}