{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Adhikary S"],"funding":["NCI NIH HHS"],"pagination":["1398"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6438984"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(1)"],"pubmed_abstract":["The roles of Plant Homeodomain (PHD) fingers in catalysis of histone modifications are unknown. We demonstrated that the PHD finger of Ubiquitin Protein Ligase E3 Component N-Recognin7 (UBR7) harbors E3 ubiquitin ligase activity toward monoubiquitination of histone H2B at lysine120 (H2BK120Ub). Purified PHD finger or full-length UBR7 monoubiquitinated H2BK120 in vitro, and loss of UBR7 drastically reduced H2BK120Ub genome-wide binding sites in MCF10A cells. Low UBR7 expression was correlated with occurrence of triple-negative breast cancer and metastatic tumors. Consistently, UBR7 knockdown enhanced the invasiveness, induced epithelial-to-mesenchymal transition and promoted metastasis. Conversely, ectopic expression of UBR7 restored these cellular phenotypes and reduced tumor growth. Mecha"],"journal":["Nature communications"],"pubmed_title":["Atypical plant homeodomain of UBR7 functions as an H2BK120Ub ligase and breast tumor suppressor."],"pmcid":["PMC6438984"],"funding_grant_id":["P30 CA016672","R00 CA160578","K99 CA160578"],"pubmed_authors":["Sengupta I","Srivastava DK","Raman AT","Yang F","Tarco E","Sahin AA","Tapia C","Rai K","Das C","Maitituoheti M","Terranova C","Adhikary S","Roy S","Dasgupta A","Ma J","Bassett R","Chakravarti D"],"additional_accession":[]},"is_claimable":false,"name":"Atypical plant homeodomain of UBR7 functions as an H2BK120Ub ligase and breast tumor suppressor.","description":"The roles of Plant Homeodomain (PHD) fingers in catalysis of histone modifications are unknown. We demonstrated that the PHD finger of Ubiquitin Protein Ligase E3 Component N-Recognin7 (UBR7) harbors E3 ubiquitin ligase activity toward monoubiquitination of histone H2B at lysine120 (H2BK120Ub). Purified PHD finger or full-length UBR7 monoubiquitinated H2BK120 in vitro, and loss of UBR7 drastically reduced H2BK120Ub genome-wide binding sites in MCF10A cells. Low UBR7 expression was correlated with occurrence of triple-negative breast cancer and metastatic tumors. Consistently, UBR7 knockdown enhanced the invasiveness, induced epithelial-to-mesenchymal transition and promoted metastasis. Conversely, ectopic expression of UBR7 restored these cellular phenotypes and reduced tumor growth. Mecha","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Mar","modification":"2026-05-03T16:42:14.847Z","creation":"2019-06-06T21:03:41Z"},"accession":"S-EPMC6438984","cross_references":{"pubmed":["30923315"],"doi":["10.1038/s41467-019-08986-5"]}}