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Hesin, A.

Publications and source records attributed to Hesin, A..

2 recordsLinked to original sources

Systematic Generation of Mutations at Topoisomerase II Cleavage Sites Enables Cancer Adaptation to Doxorubicin Therapy

Acquired resistance to chemotherapy remains a major cause of treatment failure. Here, we investigate the early events underlying the development of resistance to doxorubicin (Dox), one of the most widely used anticancer agents, during repeated drug exposure. Dox intercalates into DNA at sites influenced by chromatin structure and inhibits the DNA religation step of topoisomerase II (Top2), thereby inducing double-strand DNA breaks (DSBs). Here, we show that, in the subpopulation of cancer cells that survive initial Dox treatment, repair of Dox-induced DSBs leads to the accumulation of recurrent mutations at Top2 cleavage sites. These mutations prevent the formation of Dox-induced DSBs at the same loci upon subsequent exposures, effectively protecting the genome from Top2-mediated DNA damage and promoting the development of drug resistance. Importantly, the loss of Top2-dependent DNA cleavage and relaxation caused by these mutations increases the reliance of adapted cells on topoisomerase I (Top1), thereby sensitizing them to Top1 inhibitors. Together, our findings reveal a previously unrecognized mechanism of resistance based on the active generation of highly adaptive mutations, providing new insight into cancer evolution under therapeutic pressure.

cancer biology↗

eIF2α integrates proteotoxic signals both from ER and cytoplasm: Hsp70-Bag3 module regulates HRI-dependent phosphorylation of eIF2α

The major heat shock protein Hsp70 has been implicated in many stages of cancer development. These effects are mediated by a scaffold protein Bag3 that binds to Hsp70 and links it to components of multiple cancer-related signaling pathways. Accordingly, the Hsp70-Bag3 complex has been targeted by small molecules, which showed strong anti-cancer effects. Here, our initial question was how JG-98, an allosteric inhibitor of Hsp70 that blocks its interaction with Bag3, causes cell death. Breast epithelial cells MCF10A transformed with a single oncogene Her2 showed higher sensitivity to JG-98 then parental MCF10A cells. RNA expression analysis showed that this enhanced sensitivity correlated with higher induction of the UPR genes. Indeed, depletion of the pro-apoptotic UPR responsive transcription factor CHOP significantly protected cells from JG-98. Surprisingly, only the eIF2-associated branch of the UPR was activated by JG-98, suggesting that the response was not related to the ER proteotoxicity. Indeed, it was dependent on activation of a distinct cytoplasmic eIF2 kinase HRI. HRI-dependent phosphorylation of eIF2 was also activated by the cytoplasmic proteotoxicity via Hsp70-Bag3 complex, which directly associates with HRI. Dissociation of Hsp70-Bag3 complex led to Bag3-dependent degradation of HRI via autophagy. Therefore, eIF2 integrates proteotoxicity signals from both ER and cytoplasm, and the cytoplasmic response mediates cytotoxicity of the Hsp70-Bag3 inhibitors.

cell biology↗