Srsf7, also known as serine/arginine-rich splicing factor 7, is an essential RNA-binding protein involved in multiple aspects of RNA processing, such as splicing, mRNA nuclear export, stability, and translation [5]. It is associated with various biological pathways, including those related to cell growth, death, and immune response [4,6]. Genetic models, especially KO/CKO mouse models, are valuable for studying its functions.

In senescent cells, down-regulation of Srsf7 is observed, and its knockdown in human diploid fibroblast (HDF) can induce cellular senescence through generation of MDM2 variants, suggesting its role in p53-mediated senescence [2]. In glioblastoma, Srsf7 is a novel m6A regulator, promoting cell proliferation and migration by facilitating m6A methylation near its binding sites on relevant mRNAs [1]. In colon and lung cancer cells, Srsf7 knockdown inhibits proliferation and enhances apoptosis, and it regulates the splicing of the apoptosis regulator Fas [5]. In murine diabetic kidney disease, diabetes down-regulates Srsf7 in the proximal tubule, and its in vitro knockdown induces a pro-inflammatory phenotype [3].

In conclusion, Srsf7 plays crucial roles in multiple biological processes, including cell senescence, cancer progression, and diabetic kidney disease. Studies using KO/CKO mouse models and other loss-of-function experiments have revealed its functions in these specific disease areas, providing insights into the underlying molecular mechanisms and potential therapeutic targets.