{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["15(3)"],"submitter":["Zhang H"],"pubmed_abstract":["The interaction between m<sup>6</sup>A-methylated RNA and chromatin modification remains largely unknown. We found that targeted inhibition of bromodomain-containing protein 4 (BRD4) by siRNA or its inhibitor (JQ1) significantly decreases mRNA m<sup>6</sup>A levels and suppresses the malignancy of breast cancer (BC) cells <i>via</i> increased expression of demethylase AlkB homolog 5 (ALKBH5). Mechanistically, inhibition of BRD4 increases the mRNA stability of ALKBH5 <i>via</i> enhanced binding between its 3' untranslated regions (3'UTRs) with RNA-binding protein RALY. Further, BRD4 serves as a scaffold for ubiquitin enzymes tripartite motif containing-21 (TRIM21) and ALKBH5, resulting in the ubiquitination and degradation of ALKBH5 protein. JQ1-increased ALKBH5 then demethylates mRNA of ex"],"journal":["Acta pharmaceutica Sinica. B"],"pagination":["1552-1570"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12069253"],"repository":["biostudies-literature"],"pubmed_title":["BRD4 regulates m&lt;sup&gt;6&lt;/sup&gt;A of ESPL1 mRNA &lt;i&gt;via&lt;/i&gt; interaction with ALKBH5 to modulate breast cancer progression."],"pmcid":["PMC12069253"],"pubmed_authors":["Peng Y","Li J","Lu Y","Zhang H","Jiang T","Wang H","Asadikaram G","Yang X","Lu L","Jiang Z","Xie G","Chen Z","Yi C","Zhou D","Zhong K","Zhou J"],"additional_accession":[]},"is_claimable":false,"name":"BRD4 regulates m&lt;sup&gt;6&lt;/sup&gt;A of ESPL1 mRNA &lt;i&gt;via&lt;/i&gt; interaction with ALKBH5 to modulate breast cancer progression.","description":"The interaction between m<sup>6</sup>A-methylated RNA and chromatin modification remains largely unknown. We found that targeted inhibition of bromodomain-containing protein 4 (BRD4) by siRNA or its inhibitor (JQ1) significantly decreases mRNA m<sup>6</sup>A levels and suppresses the malignancy of breast cancer (BC) cells <i>via</i> increased expression of demethylase AlkB homolog 5 (ALKBH5). Mechanistically, inhibition of BRD4 increases the mRNA stability of ALKBH5 <i>via</i> enhanced binding between its 3' untranslated regions (3'UTRs) with RNA-binding protein RALY. Further, BRD4 serves as a scaffold for ubiquitin enzymes tripartite motif containing-21 (TRIM21) and ALKBH5, resulting in the ubiquitination and degradation of ALKBH5 protein. JQ1-increased ALKBH5 then demethylates mRNA of ex","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Mar","modification":"2026-06-01T05:22:53.875Z","creation":"2026-04-08T09:35:18.394Z"},"accession":"S-EPMC12069253","cross_references":{"pubmed":["40370540"],"doi":["10.1016/j.apsb.2024.12.037"]}}