In an RRP Research Webinar held on November 9th, 2021, Dr. Stephen Nimer, Director of the Sylvester Comprehensive Cancer Center, shared these key takeaways from his lab’s research:

RUNX1 protein function is controlled by methylation sites that are marked by methyltransferases like PRMT1, PRMT4 and PRMT5.

RUNX1 is methylated by PRMT4, specifically methylation at R319 promotes activation of RUNX1.

PRMT4 is essential for myeloid leukemogenesis but not for normal hematopoiesis.

PRMT4 requires JAK2, inhibition of JAK2 via ruxolitinib reduces PRMT4 which in turn reduces RUNX1 methylation.

Conclusion: A tyrosine kinase inhibitor, like ruxolitinib may be an FDA-approved drug that could regulate RUNX1 function. Further studies are needed to fully understand how ruxolitinib changes RUNX1 function and if it could directly impact the process of leukemogenesis in RUNX1-FPD.