Snrpd2, a core component of the spliceosome, plays a crucial role in RNA splicing, a dynamic process regulated by the spliceosome in response to environmental stimuli. RNA splicing is essential for the maturation of pre-mRNA into functional mRNA, thereby affecting gene expression and various biological processes [1,2,3,4,6,7].

In the context of diseases, in hepatocellular carcinoma (HCC), Snrpd2 is the most highly upregulated Sm protein and acts as an oncogene. It modulates DDX39A intron retention with HNRNPL, leading to the expression of the DDX39A short variant which in turn mediates MYC mRNA nuclear export, forming a positive feedback loop [2]. In colorectal cancer, upregulated Snrpd2 can interact with the glutamic-proline (EP) domain of PABPN1, disrupt its liquid-liquid phase separation, and promote alternative polyadenylation of CTNNBIP1, driving cell proliferation and migration [3]. In melanoma, Snrpd2 is identified as a hub gene associated with metastasis and prognosis, and is also associated with immunotherapy [5]. Moreover, in the study of myotonic dystrophy type 1 (DM1), modest knockdown of Snrpd2 in DM1 fibroblasts and myoblasts significantly reduces DMPK expression and partially rescues MBNL-regulated alternative splicing dysfunction, revealing an unappreciated role for MBNL:spliceosomal protein stoichiometry in modulating the spliceopathy [4].

In conclusion, Snrpd2 is essential for RNA splicing and has significant implications in multiple disease areas. Through various functional studies, its role in cancer metastasis, oncogenic signaling in HCC, alternative polyadenylation in colorectal cancer, and spliceopathy in DM1 has been revealed. These findings from different disease-related research models contribute to a better understanding of the biological functions of Snrpd2 and offer potential targets for disease treatment [2,3,4,5].