Researchers at the University of California, San Francisco, report a new approach to cancer therapy built on slowing the rise of the MyC protein, a driver that shows up in roughly seventy percent of solid tumors across a range of cancer types. The findings come from a comprehensive set of experiments that map how MyC levels are controlled in cells and how those controls can be turned down without mutating the DNA itself. The work stands out for shifting the focus from directly disabling MyC to stepping away from the protein’s production line, a strategy that could sidestep some of the obstacles that have hampered previous attempts to target MyC with drugs.
MYC has been a central player in cell growth since the 1980s. It acts as a master regulator, instructing cells to divide and, in many cases, fueling tumor expansion. For decades scientists searched for a direct way to disarm MyC, only to hit roadblocks because the protein is essential to many normal cellular functions as well. The team tackled the problem from another angle by examining how the cell makes MyC, hoping to intercept the process before MyC accumulates to dangerous levels. Their approach investigates production mechanisms rather than the protein itself.
Using a refined CRISPRI method, the researchers identified RBM42 as a crucial regulator that oversees the translation stage—the moment when instructions stored in genetic material are converted into functional machines that make proteins, including MyC. CRISPRI borrows ideas from CRISPR technology but avoids altering the DNA sequence; instead, it modulates the activity of specific molecules that control gene expression. In this study, RBM42 appeared to orchestrate when and how efficiently ribosomes—the cellular factories for protein synthesis—are produced, effectively tuning the output of MyC.
When RBM42 activity was inhibited in pancreatic cancer cell models, MyC production diminished and cells showed reduced proliferation. In those same experiments, tumor-like growth slowed, and in some conditions ceased altogether. The changes were robust across several cell lines, suggesting a broader applicability beyond a single cancer type. The team highlights that the effect seems tightly linked to the regulation of ribosome biogenesis, which in turn governs how aggressively a tumor can grow.
While the detailed mechanism is still being explored, experts emphasize that the work provides a clear map of how MyC levels are controlled in cancer cells. By modulating RBM42 and the ribosome production step, researchers may develop therapies that bring MyC-dependent tumors under control without risking widespread disruption of normal cell function. The findings add to a growing body of evidence that targeting the machinery of protein synthesis can be a viable route to slow down or halt tumor progression.
In animal studies, disabling RBM42 led to a noticeable slowdown in tumor growth, reinforcing the potential translational value of this strategy. The implications are exciting for aggressive cancers where MyC-driven growth is a hallmark and treatment options are limited. Researchers are now exploring compounds or biologics that can block RBM42 or its interaction with the ribosome assembly pathway, aiming to translate these findings into safe and effective therapies. If successful, such drugs could complement existing treatments and broaden the range of tumors that become controllable targets.
Overall, the study illuminates a new choke point in cancer biology and offers a promising avenue for therapies that limit tumor growth by downshifting MyC production through ribosome biogenesis control.