Scin, also known as scinderin, is a calcium-dependent actin severing and capping protein. It is involved in regulating the F-actin cytoskeleton network, which is crucial for maintaining cell structure and polarity. The dysregulation of Scin is associated with various cellular processes and diseases, highlighting its biological importance. Genetic models, especially gene knockout models, are valuable tools for studying its functions [2,4].

In Sertoli cells, specific deletion of Pik3c3 (encoding a class III phosphatidylinositol 3-kinase catalytic subunit) led to an increase in Scin levels. The accumulation of Scin caused disorder and disassembly of the F-actin cytoskeleton, disrupting Sertoli cell polarity and impairing spermiogenesis. This was due to the failure of Scin degradation through the autophagy-lysosome pathway [1]. In addition, in lung carcinoma, lentivirus-mediated silencing of Scin significantly inhibited cell proliferation and colony formation, and led to cell cycle arrest in the G0/G1 phase [2]. Similar effects were seen in prostate cancer cells, where knockdown of Scin inhibited proliferation and induced G0/G1 phase arrest [4]. In acute myeloid leukemia, decreased Scin expression, associated with promoter methylation, was related to a poor prognosis, and Scin expression was restored in patients who achieved complete remission after induction therapy [3].

In conclusion, Scin plays a vital role in maintaining the integrity of the F-actin cytoskeleton and is involved in processes such as cell proliferation and cell cycle regulation. Studies using KO or CKO mouse models, as well as other loss-of-function experiments, have revealed its significance in spermatogenesis-related disorders, and various cancers like lung, prostate, and acute myeloid leukemia, providing insights into potential therapeutic targets for these diseases.