Slc7a2, a cationic amino acid transporter, plays crucial roles in multiple biological processes. It is involved in lysine and arginine transport, which are linked to various metabolic pathways, such as lysine catabolism, and is important for normal physiological functions like cell proliferation and immune response regulation [1-7].

In cancer, its role varies by type. In glioblastoma stem cells, up-regulation of Slc7a2 reprograms lysine catabolism, leading to histone crotonylation changes that impact tumor growth and immunity [1]. In triple-negative breast cancer, down-regulation of Slc7a2 is associated with advanced stages, and its restoration activates CD8+ T cells, promoting antitumor immunity [2]. In hepatocellular carcinoma, SLC7A2 deficiency promotes cancer progression by enhancing the recruitment of myeloid-derived suppressor cells [3]. In ovarian and non-small-cell lung cancer, lower Slc7a2 expression is related to worse prognosis, drug resistance, and less immune infiltration [4,5]. In pancreatic islets, Slc7a2 is essential for α cell function and proliferation in response to interrupted glucagon signaling [6]. In Huntington's disease, elevated Slc7a2 expression is associated with abnormal neuroinflammatory response and nitrosative stress [7].

In conclusion, Slc7a2 is vital for normal cellular functions and is significantly involved in cancer, pancreatic islet function, and neurodegenerative disease. Research using gene-knockout models, especially in cancer, has revealed its potential as a biomarker and therapeutic target, highlighting its importance in understanding disease mechanisms and developing treatments [1-7].