While KMT2A does not appear to directly physically interact with NPM1c, menin-mediated wildtype KMT2A occupancy is a necessary prerequisite for the recruitment of NPM1c to the chromatin of leukemogenic genes, which may explain why NPM1c AML cells are sensitive to menin inhibition despite their lack of KMT2A-fusion proteins.36-39 NPM1c does, however, form multivalent heterotypic interactions with Pol II and components of the SEC and acts as a scaffold to stabilize the transcriptional machinery at its target genes. The gene discussed is MEN1; the disease is acute myeloid leukemia.