CELF1, also known as CUGBP Elav-like family member 1, is an RNA-binding protein that binds to GU-rich elements in mRNA. It plays crucial roles in controlling mRNA splicing, translation, and decay, thus being involved in various physiological and pathological processes [7].

CELF1 has been associated with multiple diseases. In heart-related diseases, overexpression of CELF1 in cardiomyocytes leads to reduced capillary density, down-regulation of Vegfa mRNA, and degradation of connexin 43, contributing to vascular rarefaction and dilated cardiomyopathy [4,8]. In cataract development, CELF1 promotes matrix metalloproteinases gene expression at the transcriptional level and regulates alternative splicing of DNA repair genes in lens epithelial cells [1,2]. In Daphnia magna, CELF1 suppresses Doublesex1 expression, potentially avoiding sexual ambiguity [3]. In the context of total parenteral nutrition, the CELF1/p53 axis leads to intestinal villus atrophy by suppressing the proliferation of intestinal epithelial cells [6]. Also, targeting CELF1 RNA-binding activity with small molecules can control hepatic stellate cell activation and liver fibrosis [5].

In conclusion, CELF1 is a key RNA-binding protein involved in multiple biological processes and disease conditions. Studies on CELF1, especially through in vivo models, have enhanced our understanding of its functions in diseases such as heart failure, cataract, and liver fibrosis, providing potential therapeutic targets for these disorders.