{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Yeh IJ"],"funding":["BLRD VA","NCI NIH HHS"],"pubmed_abstract":["Central kinases of the Hippo tumor suppressor pathway phosphorylate the transcriptional coactivators YAP and TAZ to sequester them in the cytoplasm. In cancer, Hippo pathway kinases have reduced activity, leading to translocation of YAP and TAZ into the nucleus where they engage TEADs and other transcription factors. Here, we explore whether heterobifunctional small molecules that bind to the TEAD allosteric lipid-binding pocket can degrade the TEAD•YAP/TAZ complex. We design and synthesize heterobifunctional molecules that consist of flufenamic acid analogs that bind to the allosteric TEAD lipid pocket, a long and flexible linker, and thalidomide to engage E3 ubiquitin ligase component cereblon. The bifunctional compounds promote ternary complex formation in biochemical assays and mammali"],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2026.01.09.698724"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12803072"],"repository":["biostudies-literature"],"pubmed_title":["Degradation of the TEAD•YAP/TAZ Transcription Factor Complex by Heterobifunctional Small Molecules that Bind to the TEAD Allosteric Lipid Pocket."],"pmcid":["PMC12803072"],"funding_grant_id":["I01 BX005188","R01 CA264471"],"pubmed_authors":["Ghozayel MK","Yeh IJ","Bum-Erdene K","Meroueh SO"],"additional_accession":[]},"is_claimable":false,"name":"Degradation of the TEAD•YAP/TAZ Transcription Factor Complex by Heterobifunctional Small Molecules that Bind to the TEAD Allosteric Lipid Pocket.","description":"Central kinases of the Hippo tumor suppressor pathway phosphorylate the transcriptional coactivators YAP and TAZ to sequester them in the cytoplasm. In cancer, Hippo pathway kinases have reduced activity, leading to translocation of YAP and TAZ into the nucleus where they engage TEADs and other transcription factors. Here, we explore whether heterobifunctional small molecules that bind to the TEAD allosteric lipid-binding pocket can degrade the TEAD•YAP/TAZ complex. We design and synthesize heterobifunctional molecules that consist of flufenamic acid analogs that bind to the allosteric TEAD lipid pocket, a long and flexible linker, and thalidomide to engage E3 ubiquitin ligase component cereblon. The bifunctional compounds promote ternary complex formation in biochemical assays and mammali","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Jan","modification":"2026-06-05T03:26:10.496Z","creation":"2026-06-05T03:12:14.112Z"},"accession":"S-EPMC12803072","cross_references":{"pubmed":["41542630"],"doi":["10.64898/2026.01.09.698724"]}}