{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["25(3)"],"submitter":["Yonezawa H"],"pubmed_abstract":["Ivermectin (IVM), an avermectin-derivative anthelmintic, specifically binds to glutamate-gated chloride ion channels (GluCls), causing paralysis in invertebrates. IVM also exhibits other biological activities such as Wnt/β-catenin pathway inhibition in vertebrates that do not possess GluCls. This study showed that affinity purification using immobilized IVM B1a isolated TELO2, a cofactor of phosphatidylinositol 3-kinase-related kinases (PIKKs), as a specific IVM B1a-binding protein. <i>TELO2</i> knockdown reduced cytoplasmic β-catenin and the transcriptional activation of β-catenin/TCF. IVM B1a bound to TELO2 through the C-terminal α-helix, in which mutations conferred IVM resistance. IVM reduced the TELO2 and PIKK protein levels and the AKT and S6 kinase phosphorylation levels. The inhibi"],"journal":["iScience"],"pagination":["103912"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9072907"],"repository":["biostudies-literature"],"pubmed_title":["Ivermectin represses Wnt/β-catenin signaling by binding to TELO2, a regulator of phosphatidylinositol 3-kinase-related kinases."],"pmcid":["PMC9072907"],"pubmed_authors":["Nakamura K","Sugawara Y","Endo H","Goto M","Iwatsuki M","Uehara Y","Yonezawa H","Takahashi R","Ujiie H","Nishiya N","Hirose T","Ikeda A","Ogawa S","Sunazuka T","Kanno M"],"additional_accession":[]},"is_claimable":false,"name":"Ivermectin represses Wnt/β-catenin signaling by binding to TELO2, a regulator of phosphatidylinositol 3-kinase-related kinases.","description":"Ivermectin (IVM), an avermectin-derivative anthelmintic, specifically binds to glutamate-gated chloride ion channels (GluCls), causing paralysis in invertebrates. IVM also exhibits other biological activities such as Wnt/β-catenin pathway inhibition in vertebrates that do not possess GluCls. This study showed that affinity purification using immobilized IVM B1a isolated TELO2, a cofactor of phosphatidylinositol 3-kinase-related kinases (PIKKs), as a specific IVM B1a-binding protein. <i>TELO2</i> knockdown reduced cytoplasmic β-catenin and the transcriptional activation of β-catenin/TCF. IVM B1a bound to TELO2 through the C-terminal α-helix, in which mutations conferred IVM resistance. IVM reduced the TELO2 and PIKK protein levels and the AKT and S6 kinase phosphorylation levels. The inhibi","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Mar","modification":"2025-04-04T09:10:03.156Z","creation":"2025-04-04T09:10:03.156Z"},"accession":"S-EPMC9072907","cross_references":{"pubmed":["35530256"],"doi":["10.1016/j.isci.2022.103912"]}}