{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Zhang T"],"pubmed_abstract":["Besides its mitochondria-based anti-apoptotic role, Bcl-xL also travels to the nucleus to promote cancer metastasis by upregulating global histone H3 trimethyl Lys4 (H3K4me3) and TGFβ transcription. How Bcl-xL is translocated into the nucleus and how nuclear Bcl-xL regulates H3K4me3 modification are not understood. Here, we report that C-terminal Binding Protein 2 (CtBP2) binds Bcl-xL via its N-terminus and translocates Bcl-xL into the nucleus. Knockdown of CtBP2 by shRNA decreases the nuclear portion of Bcl-xL and reverses Bcl-xL-induced cell migration and metastasis in mouse models. Furthermore, knockout of CtBP2 suppresses Bcl-xL transcription. The binding between Bcl-xL and CtBP2 is required for their interaction with MLL1, a histone H3K4 methyltransferase. Pharmacologic inhibition of "],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2023.04.26.538373"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10168309"],"repository":["biostudies-literature"],"pubmed_title":["Bcl-xL is translocated to the nucleus via CtBP2 to epigenetically promote metastasis."],"pmcid":["PMC10168309"],"pubmed_authors":["Grossman SR","Tan YA","Wang D","Choi S","Li Y","Zhang T","Li S","Chen Z","Mishra B","Chen YT","Jiang X","Du YN","Damle P","Chen X","Na JH","Xiang JZ"],"additional_accession":[]},"is_claimable":false,"name":"Bcl-xL is translocated to the nucleus via CtBP2 to epigenetically promote metastasis.","description":"Besides its mitochondria-based anti-apoptotic role, Bcl-xL also travels to the nucleus to promote cancer metastasis by upregulating global histone H3 trimethyl Lys4 (H3K4me3) and TGFβ transcription. How Bcl-xL is translocated into the nucleus and how nuclear Bcl-xL regulates H3K4me3 modification are not understood. Here, we report that C-terminal Binding Protein 2 (CtBP2) binds Bcl-xL via its N-terminus and translocates Bcl-xL into the nucleus. Knockdown of CtBP2 by shRNA decreases the nuclear portion of Bcl-xL and reverses Bcl-xL-induced cell migration and metastasis in mouse models. Furthermore, knockout of CtBP2 suppresses Bcl-xL transcription. The binding between Bcl-xL and CtBP2 is required for their interaction with MLL1, a histone H3K4 methyltransferase. Pharmacologic inhibition of ","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Apr","modification":"2025-04-04T13:07:19.418Z","creation":"2025-04-04T13:07:19.418Z"},"accession":"S-EPMC10168309","cross_references":{"pubmed":["37163116"],"doi":["10.1101/2023.04.26.538373"]}}