Lpcat4, also known as LPLAT10 and LPEAT2, is a lysophosphatidylcholine acyltransferase enzyme. It plays a crucial role in phospholipid remodeling, which is essential for membrane structural integrity, protein complex assembly, and various cellular functions. Phospholipid remodeling via Lpcat4 is involved in multiple biological pathways, such as the Lands' cycle, and is important for processes like cell differentiation, metabolism, and maintaining tissue homeostasis [1,2,3,5]. Genetic models, especially knockout (KO) mouse models, are valuable for studying Lpcat4's function.

In urothelial cells, Lpcat4 knockdown led to impaired proliferation rate, altered trans-epithelial electrical resistances, and reduced capacity to restitute barrier function after wounding, suggesting its importance in urothelial barrier integrity [2]. In ATDC5 cells, Lpcat4 knockdown decreased chondrogenic markers, Alcian blue staining intensity, and alkaline phosphatase activity, indicating its role in chondrogenic differentiation [5]. In hepatocellular carcinoma, Lpcat4 enhanced cell growth and cholesterol biosynthesis by up-regulating ACSL3 through the WNT/β-catenin/c-JUN signaling pathway [4].

In conclusion, Lpcat4 is essential for phospholipid remodeling, which impacts diverse biological processes like urothelial barrier function, chondrogenic differentiation, and cancer cell growth. The study of Lpcat4 using KO or conditional knockout (CKO) mouse models has provided insights into its role in diseases such as urothelial-related disorders and hepatocellular carcinoma, contributing to our understanding of disease mechanisms and potential therapeutic targets.