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 immune responses, metabolism, and cell death pathways [3].

In hepatic stellate cells, loss of Zfp36 promoted ferroptosis, a form of programmed cell death, by activating autophagy through stabilizing ATG16L1 mRNA. In mice, HSC-specific overexpression of Zfp36 impaired erastin-or sorafenib-induced HSC ferroptosis, suggesting its role in liver fibrosis [1]. T cell-specific deletion of all three ZFP36 family members in mice resulted in early lethality, immune cell activation, and multiorgan pathology, highlighting its importance in regulating T cell quiescence [2]. Zfp36-deficient mice also showed enhanced intestinal I/R-induced lung injury, apoptosis, inflammation, and fibrosis, indicating its protective role in the lung via the CREBBP/p53/p21/Bax pathway [4].

In conclusion, Zfp36 plays crucial roles in multiple biological processes, including ferroptosis, T cell regulation, and protection against tissue injury. Gene knockout or conditional knockout mouse models have been instrumental in revealing these functions, especially in diseases such as liver fibrosis, immune-related disorders, and lung injury. Understanding Zfp36's functions provides potential targets for treating these diseases.