DPY30, a core subunit of the histone lysine methyltransferase complex, is essential for the activity of SET1/MLL methyltransferase [2,3,4,5,6,7,8,9]. It is involved in regulating histone H3K4 modification and is associated with various biological events such as tumorigenesis, cell senescence, and glucose homeostasis [1,2,4,9].

In a Dpy30F/F; LysM-Cre+/+ mouse model, deletion of Dpy30 in myeloid cells led to increased bone mass due to impaired osteoclastogenesis and defective osteoclast activity, suggesting a role in osteoclast differentiation and function [6].

In cancer research, knockdown of DPY30 in various cancer cell lines has shown inhibitory effects. For example, in colorectal carcinoma cells, DPY30 knockdown decreased EMT progression, migratory and invasive abilities, and promoted apoptosis [1,7]. In osteosarcoma cells, DPY30 knockdown impaired proliferation, migration, and invasion while inducing apoptosis [5]. In cervical squamous cell carcinoma cells, DPY30 knockdown decreased cell proliferation, migration, and invasion [8].

In conclusion, DPY30 plays crucial roles in multiple biological processes, especially in cancer and bone-related diseases. Studies using gene knockout or knockdown models have revealed its oncogenic potential in various cancers and its importance in osteoclast-mediated bone remodeling. Understanding DPY30's functions can provide new therapeutic targets for treating related diseases.