{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Han D"],"funding":["HHS | NIH | National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["e2305092120"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10523488"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["120(39)"],"pubmed_abstract":["Histone modifications are critical for regulating chromatin structure and gene expression. Dysregulation of histone modifications likely contributes to disease states and cancer. Depletion of the chromatin-binding protein BRWD3 (Bromodomain and WD repeat-containing protein 3), a known substrate-specificity factor of the Cul4-DDB1 E3 ubiquitin ligase complex, results in increased H3K4me1 (H3 lysine 4 monomethylation) levels. The underlying mechanism linking BRWD3 and H3K4 methylation, however, has yet to be defined. Here, we show that depleting BRWD3 not only causes an increase in H3K4me1 levels but also causes a decrease in H3K4me3 (H3 lysine 4 trimethylation) levels, indicating that BRWD3 influences H3K4 methylation more broadly. Using immunoprecipitation coupled to quantitative mass spec"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["BRWD3 promotes KDM5 degradation to maintain H3K4 methylation levels."],"pmcid":["PMC10523488"],"funding_grant_id":["R35 GM133552","R35 GM128650","R35GM128650","R35GM133552"],"pubmed_authors":["Davies JP","Nordman JT","Plate L","Schaffner SH","Han D","Benton ML"],"additional_accession":[]},"is_claimable":false,"name":"BRWD3 promotes KDM5 degradation to maintain H3K4 methylation levels.","description":"Histone modifications are critical for regulating chromatin structure and gene expression. Dysregulation of histone modifications likely contributes to disease states and cancer. Depletion of the chromatin-binding protein BRWD3 (Bromodomain and WD repeat-containing protein 3), a known substrate-specificity factor of the Cul4-DDB1 E3 ubiquitin ligase complex, results in increased H3K4me1 (H3 lysine 4 monomethylation) levels. The underlying mechanism linking BRWD3 and H3K4 methylation, however, has yet to be defined. Here, we show that depleting BRWD3 not only causes an increase in H3K4me1 levels but also causes a decrease in H3K4me3 (H3 lysine 4 trimethylation) levels, indicating that BRWD3 influences H3K4 methylation more broadly. Using immunoprecipitation coupled to quantitative mass spec","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Sep","modification":"2026-07-14T22:33:24.004Z","creation":"2025-02-19T04:07:15.259Z"},"accession":"S-EPMC10523488","cross_references":{"pubmed":["37722046"],"doi":["10.1073/pnas.2305092120"]}}