New Drug Blocks Key Enzyme to Slow Cancer Growth - Johns Hopkins University School of Medicine (2025)

By Editorial Team
A 2025 study from Johns Hopkins suggests that blocking a key enzyme could help stop cancer cells from growing. The enzyme, called Pol 1, helps cells make ribosomal RNA, which is needed to build proteins. When researchers blocked Pol 1 using a drug, it triggered a stress response in cancer cells that slowed their growth.

The study found this treatment worked especially well in cancers with certain genetic problems, like mismatch repair deficiency (MMRd), which is common in colorectal, stomach, and uterine cancers. In lab tests, a new drug called BOB-42 reduced tumor growth by up to 77% in some cases.

Scientists also discovered that this approach could help the immune system spot cancer cells more easily. They believe combining Pol 1 blockers with immunotherapy may improve treatment results, giving hope to patients with cancers that don’t respond well to current options.

"Ribosome biogenesis has long been known as a hallmark of cancer," says study leader Marikki Laiho, M.D., Ph.D., the Willard and Lillian Hackerman Professor of Radiation Oncology and Vice Chair for Research of the Department of Radiation Oncology and Molecular Radiation Sciences. "Our study reveals that the ribosomal protein RPL22, typically a structural component of the ribosome, plays an unexpected dual role as a critical regulator of RNA splicing."


Summary

Ribosome biosynthesis is a cancer vulnerability targeted by inhibiting RNA polymerase I (Pol I) transcription. We developed specific Pol I inhibitors that activate a ribotoxic stress pathway to uncover drivers of sensitivity. Integrating multi-omics and drug response data from a large cancer cell panel, we found that RPL22 frameshift mutations confer Pol I inhibitor sensitivity. Mechanistically, RPL22 interacts directly with 28S rRNA and mRNA splice junctions, acting as a splicing regulator. RPL22 deficiency, intensified by 28S rRNA sequestration, promotes splicing of its paralog RPL22L1 and the p53 negative regulator MDM4. Both chemical and genetic inhibition of rRNA synthesis broadly remodel mRNA splicing controlling hundreds of targets. Notably, RPL22-dependent alternative splicing is reversed by Pol I inhibition, revealing a non-canonical ribotoxic stress-initiated tumor suppressive pathway. This study uncovers a robust mechanism linking rRNA synthesis activity to splicing, coordinated by the ribosomal protein RPL22.

Keywords



More information: Ribosomal RNA transcription regulates splicing through ribosomal protein RPL22, Cell Chemical Biology (2025). DOI: 10.1016/j.chembiol.2025.05.012. www.cell.com/cell-chemical-bio … 2451-9456(25)00173-4












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