MST1/2 kinases contain C‐terminal SARAH domains that mediate their homodimerization and facilitate autophosphorylation and activation.[35] Moreover, MST1 and MST2 also heterodimerize in cells, leading to MST1/2 inactivation, depending on the order of RASSF5 binding and activation‐loop phosphorylation.[36, 37] The observation that MISP disrupts both MST1/2 homodimerization and heterodimerization here provides one possible explanation for MST1/2 inactivation in cancers with aberrant MISP, at least in NSCLC. The gene discussed is MST1; the disease is non-small cell lung carcinoma.