Hnrnpul1, known as heterogeneous nuclear ribonucleoprotein U-like 1, belongs to the family of RNA-binding proteins. It is involved in nucleic acid binding, transcription, and splicing, either by directly binding to DNA and RNA or through interacting with other proteins in the spliceosome. It plays a role in multiple biological processes and is potentially associated with various diseases [1,2,3,4,5].

In zebrafish, Hnrnpul1 mutants show reduced body and fin growth, missing bones, craniofacial tendon growth defects, and adult-onset caudal scoliosis. RNA-sequencing reveals its role in alternative splicing and transcriptional regulation, especially of genes related to translation, ubiquitination, and DNA damage [1]. In esophageal squamous cell carcinoma, reduced Hnrnpul1 expression enhances cisplatin sensitivity, and it inhibits cisplatin sensitivity by regulating the formation of circMAN1A2 [2]. In cervical cancer, NAT10-mediated RNA acetylation enhances Hnrnpul1 mRNA stability, promoting cancer progression [3]. In ovarian cancer, AKAP8 regulates the transcription of a specific Hnrnpul1 isoform, and AKAP8 inhibition can enhance PAPR inhibitor cytotoxicity [4]. In bladder cancer, LINC00461 promotes epithelial-mesenchymal transition (EMT) through the miR-518b/Hnrnpul1 axis [5].

In conclusion, Hnrnpul1 is crucial for normal development, as shown by zebrafish models, and is involved in the progression of multiple cancers. Studies on Hnrnpul1 in disease models help to understand its function in specific biological processes and offer potential therapeutic targets for related diseases such as esophageal, cervical, ovarian, and bladder cancers.