{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Heo J"],"funding":["National Research Foundation of Korea (NRF)"],"pagination":["1760"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12698673"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["8(1)"],"pubmed_abstract":["The transcription machinery is assembled via interactions of DNA-bound transcriptional activators and coactivators. When the eukaryotic RNA polymerase II complex is formed, cAMP-regulated transcription factor (CREB) binding protein (CBP) acts as a general coactivator bridging the transcriptional apparatus. Forkhead box protein O4 (FOXO4), a transcription factor, has been reported to bind to the KIX domain of CBP (CBP-KIX). Although the CR3 of FOXO4 (FOXO4-CR3) binds as expected to the MLL and c-Myb sites of CBP-KIX, its substantially higher affinity for CBP, compared to its homolog FOXO3a, cannot be explained by a single conserved ΦXXΦΦ binding motif. Here, we found that a second ΦXXΦΦ motif in FOXO4-CR3 provides an additional point of contact for CBP-KIX. Isothermal titration calorimetry "],"journal":["Communications biology"],"pubmed_title":["Recognition of two hydrophobic pockets in the KIX domain of CBP by FOXO4 transactivation domain."],"pmcid":["PMC12698673"],"funding_grant_id":["RS-2024-00440614","RS-2024-00411137","RS-2025-16068849"],"pubmed_authors":["Ryu KS","Heo J","Park CJ"],"additional_accession":[]},"is_claimable":false,"name":"Recognition of two hydrophobic pockets in the KIX domain of CBP by FOXO4 transactivation domain.","description":"The transcription machinery is assembled via interactions of DNA-bound transcriptional activators and coactivators. When the eukaryotic RNA polymerase II complex is formed, cAMP-regulated transcription factor (CREB) binding protein (CBP) acts as a general coactivator bridging the transcriptional apparatus. Forkhead box protein O4 (FOXO4), a transcription factor, has been reported to bind to the KIX domain of CBP (CBP-KIX). Although the CR3 of FOXO4 (FOXO4-CR3) binds as expected to the MLL and c-Myb sites of CBP-KIX, its substantially higher affinity for CBP, compared to its homolog FOXO3a, cannot be explained by a single conserved ΦXXΦΦ binding motif. Here, we found that a second ΦXXΦΦ motif in FOXO4-CR3 provides an additional point of contact for CBP-KIX. Isothermal titration calorimetry ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Dec","modification":"2026-06-06T02:15:58.011Z","creation":"2026-05-24T03:12:15.018Z"},"accession":"S-EPMC12698673","cross_references":{"pubmed":["41381850"],"doi":["10.1038/s42003-025-09146-w"]}}