Stom, also known as stomatin, is a 31-kDa integral membrane protein. It has a single hydrophobic domain, is phosphorylated, and is widely distributed in animal tissues. Stom belongs to the stomatin-domain protein family, members of which are oligomeric, mostly localize to membrane domains, and often modulate ion channel activity [1,2].

In a mouse model of non-alcoholic fatty liver disease (NAFLD), damage-regulated autophagy modulator (DRAM) was found to interact with Stom. DRAM recruits Stom to lysosomes, induces lysosomal membrane permeabilization (LMP), and promotes exosome release from hepatocytes, suggesting Stom's role in exosome-related processes in NAFLD [3].

In a mouse lung epithelial cell line (MLE-12) treated with lipopolysaccharide (LPS), Stom expression was upregulated. Knockdown of Stom reversed the inhibitory effects of LPS on cell viability and the promoting effects on oxidative stress and inflammation, and these changes were alleviated by overexpression of CD36, indicating that Stom may interact with CD36 to affect oxidative stress and inflammation levels in sepsis-induced acute lung injury [4].

In conclusion, Stom is an integral membrane protein with functions related to membrane domains and ion channel modulation. Studies using mouse models have revealed its role in diseases such as NAFLD and sepsis-induced acute lung injury, providing insights into its biological functions in disease-related processes.