Zinc finger matrin-type protein 2 (ZMAT2)

Zinc finger matrin-type protein 2 (ZMAT2) is a highly conserved nuclear zinc finger protein that is a core component of the spliceosome complex, specifically associated with the U2-type spliceosome and implicated in pre-mRNA splicing[3][5]. Structurally, ZMAT2 contains a matrin-type zinc finger motif and binds both zinc ions and nucleic acids. ZMAT2 participates directly in the regulation of alternative splicing by forming condensates with target pre-mRNAs, including TRIM28, influencing not only mRNA maturation but also cellular processes such as reactive oxygen species (ROS) handling and proliferation, notably in hepatocellular carcinoma where elevated ZMAT2 expression is associated with tumor progression and proliferation via modulation of TRIM28 and ROS metabolism[2]. In addition, ZMAT2 exerts a negative regulatory role on epidermal cell differentiation—its loss promotes epithelial stratification. Despite its central involvement in RNA processing and links to cancer biology, ZMAT2 is not a typical direct therapeutic target (e.g., a receptor or enzyme addressed by drugs), and there are no known drug interactions or mechanisms of action described for direct pharmacologic targeting[2][3][5].

Other names

FLJ31121hSNU23Snu23Ptg-12zinc finger matrin-type protein 2