Recent research has revealed that certain leukemia-driving oncoproteins, such as NUP98 fusion proteins, undergo liquid-liquid phase separation to form biomolecular condensates in the nucleus. By combining high-resolution subcellular imaging with cutting-edge genomic and proteomic approaches, we explore how these higher-order structures hijack the cellular machinery to drive oncogenic gene expression. Ultimately, understanding the dynamic properties and molecular vulnerabilities of these phase-separated oncoproteins will allow us to design novel, highly specific targeted treatments and therapeutic intervention strategies. 

Investigating translational dynamics in pediatric cancer has revealed that ribosomes are not static factories for protein production but dynamic regulators of gene expression. By altering their RNA or protein composition, "specialized ribosomes" selectively translate specific mRNAs that drive cancer cell survival and therapy resistance. Furthermore, aberrations in translation regulation and ribosome-associated quality control (RQC) pathways allow cells to evade stress-induced apoptosis, fueling disease progression. Understanding how these translation monitoring systems fail or are hijacked in pediatric malignancies will identify new cancer-specific vulnerabilities, ultimately opening up novel, highly targeted avenues for therapeutic intervention.

Our research develops and applies diverse genetic and pharmacological screening approaches to uncover therapeutic vulnerabilities and disease drivers in leukemia. We integrate imaging-based readouts in reporter cell lines to quantify phenotypes, proximity-based screens to map targetable interactions, and next-generation genetic approaches, including domain-specific base editing, to dissect essential protein functions. We also pair genetic perturbations with small-molecule treatments to reveal synergistic dependencies, building a prioritized atlas of actionable targets and mechanistic insights that guide precision therapies.