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Ponzo, E.

Publications and source records attributed to Ponzo, E..

2 recordsLinked to original sources

SMARCA4 MUTATIONS PROMOTE CHEMOTHERAPY RESISTANCE IN T-ACUTE LYMPHOBLASTIC LEUKEMIA THROUGH ALTERED CHROMATIN REMODELING AT AP1-ASSOCIATED REGULATORY REGIONS

Chromatin remodelers play a critical role in orchestrating chemotherapy responses in cancer cells. Components of the SWI/SNF complex are frequently mutated across cancer types, with the ATPase subunit SMARCA4 among the most commonly altered. In T-cell acute lymphoblastic leukemia (T-ALL), however, SMARCA4 mutations are rare at diagnosis but enriched in relapse samples, suggesting a potential role in therapy resistance. Using isogenic T-ALL cell lines with or without SMARCA4 mutations, we show that mutant SMARCA4 confers resistance to a broad range of chemotherapeutic agents. By combining ATAC-seq and RNA-seq, we demonstrate that SMARCA4-mutant cells display an attenuated transcriptional response to chemotherapy accompanied by impaired remodeling of AP-1-associated regulatory regions linked to stress response. These cells downregulate stress-related genes while maintaining expression programs associated with cellular fitness. Pharmacological inhibition of AP-1 phenocopies this response, further supporting a functional link between SWI/SNF-mediated remodeling at AP-1-associated regulatory regions, AP-1 activity, and chemotherapy sensitivity. Together, our findings indicate that SWI/SNF-mediated remodeling of these regions contributes to an effective chemotherapy-induced stress response, and that its failure provides T-ALL cells with a survival

cancer biology↗

BAP1 activity regulates PcG occupancy and global chromatin condensation counteracting diffuse PCGF3/5-dependent H2AK119ub1 deposition

BAP1 is recurrently mutated or deleted in a large number of diverse cancer types, including mesothelioma, uveal melanoma and hepatocellular cholangiocarcinoma. BAP1 is the catalytic subunit of the Polycomb Repressive De-Ubiquitination complex (PR-DUB) which removes PRC1 mediated H2AK119ub1. We and others have shown that H2AK119ub1 is essential for maintaining transcriptional repression and contributes to PRC2 chromatin recruitment. However, the precise relationship between BAP1 and PRC1 remains mechanistically elusive. Using embryonic stem cells, we show that a major function of BAP1 is to restrict H2AK119ub1 deposition to target sites. This increases the stability of PcG complexes with their targets and prevents diffuse accumulation of H2AK119ub1 and H3K27me3 modifications. Loss of BAP1 results in a broad increase in H2AK119ub1 levels that are primarily dependent on PCGF3/5-PRC1 complexes with a mechanism that is reminiscent of X-chromosome inactivation. Increased genome-wide H2AK119ub1 levels titrates away PRC2 from its targets and stimulates diffuse H3K27me3 accumulation across the genome. This decreases the activity of PcG repressive machineries at physiological targets and induces a general compaction of the entire chromatin. Our findings provide evidences for a unifying model that resolves the apparent contradiction between BAP1 catalytic activity and its role in vivo, uncovering molecular vulnerabilities that could be useful for BAP1-related pathologies.

molecular biology↗