Zfp36, also known as ZFP36 ring finger protein or tristetraprolin (TTP), is an RNA-binding protein. It contains two tandemly repeated CCCH-type zinc-finger motifs and binds to adenine uridine-rich elements in the 3'-untranslated regions of specific mRNAs, leading to target mRNA decay. This process is involved in regulating various biological processes such as metabolism, immune responses, and cell death pathways, and is of great biological importance [3].

In hepatic stellate cells, Zfp36 protects against ferroptosis by regulating the autophagy signaling pathway. The ubiquitin ligase FBXW7 decreases Zfp36 protein expression, and Zfp36 inhibits autophagy activation by destabilizing ATG16L1 mRNA, thus influencing ferroptosis [1]. In T cells, deletion of all three ZFP36 family members (Zfp36, Zfp36l1, and Zfp36l2) leads to early lethality, immune cell activation, and multiorgan pathology. Triply deficient T cells overproduce pro-inflammatory cytokines due to increased mRNA stability. However, deletion of Zfp36l1 and Zfp36l2 renders mice resistant to experimental autoimmune encephalomyelitits [2]. In vascular smooth muscle cells, Zfp36 expression is elevated in hypertensive patients and rodents. VSMC-specific Zfp36 deletion reduces vessel contractility and blood pressure by impairing the mRNA stability of RGS2 [4].

In conclusion, Zfp36 is a key regulator in multiple biological processes. Its functions are revealed through gene-knockout mouse models in various disease areas, including liver fibrosis, autoimmune diseases, and hypertension. These studies provide insights into the underlying mechanisms of these diseases and suggest Zfp36 as a potential therapeutic target.