Uap1, also known as UDP-N-acetylglucosamine pyrophosphorylase 1, is an enzyme that catalyzes the last step in the eukaryotic biosynthesis of uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc), converting UTP and GlcNAc-1P to the sugar nucleotide [5]. It is involved in multiple biological processes, including innate immune response, N-linked glycosylation, and is associated with pathways such as amino sugar and nucleotide sugar metabolism [1,2,3].

Uap1 deficiency significantly impairs the activation of both DNA-and RNA-viruse-induced type I IFN pathways, and Uap1-deficient mice are highly susceptible to lethal viral infection, demonstrating its crucial role in the regulation of antiviral responses [1]. In prostate cancer, Uap1 is highly overexpressed and protects cancer cells from endoplasmic reticulum (ER) stress, conferring a growth advantage [2]. In lung adenocarcinoma, Uap1 is upregulated, correlating with poor clinical outcome, larger tumour sizes, and later TNM stages [3]. In bladder cancer, silencing of Uap1 leads to reduction in proliferation, invasion, colony formation and migration capability of bladder cancer cell lines [4].

In conclusion, Uap1 plays essential biological functions in various processes. Gene-knockout models, especially in mice, have revealed its significance in antiviral innate immune responses and in the development and progression of several cancers, including prostate, lung, and bladder cancers. Understanding Uap1's functions provides insights into the crosstalk between metabolism and innate immunity and may offer potential therapeutic targets for related diseases.