JMJD6, also known as Jumonji domain-containing 6, is a Fe (II)-and 2-oxoglutarate (2OG)-dependent oxygenase. It catalyzes arginine demethylation and lysine hydroxylation of histone and non-histone peptides, and is involved in multiple biological processes such as embryonic development, cellular proliferation, migration, and angiogenesis [3,4]. It has been implicated in various pathways, including those related to immune response and lipid metabolism [1,2].

In tumor-associated macrophages, JMJD6 deficiency attenuated the growth of Lewis lung carcinoma and B16F10 melanomas by reversing M2-like activation of macrophages, suggesting its role in tumor progression through the STAT3/IL-10 axis [1]. In clear cell renal cell carcinoma, downregulation of JMJD6 abolished colony formation in vitro and inhibited orthotopic tumor growth in vivo, uncovering an oncogenic JMJD6-DGAT1 axis that tunes lipid droplet formation [2]. In placental development, understanding its interaction with other factors may identify therapeutic targets for abnormal placental angiogenesis [3].

In conclusion, JMJD6 plays essential roles in multiple biological processes, especially in tumor-related and placental development processes. Studies using gene-knockout or conditional-knockout models have revealed its significance in these areas, providing insights into potential therapeutic strategies for cancer and pregnancy-related diseases.