Lclat1, also known as LYCAT, AGPAT8, LPLAT6, or ALCAT1, is an acyltransferase. It contributes to specific acyl profiles for phosphatidylinositol, phosphoinositides, and cardiolipin, which are involved in various cellular functions like signal transduction, membrane traffic, mitochondrial function, cytoskeletal dynamics, and cell metabolism [2].

In MDA-MB-231 and ARPE-19 cells, Lclat1 silencing abated the levels of phosphatidylinositol-3,4,5-trisphosphate [PtdIns(3,4,5)P3] in response to EGF signaling, and also impaired EGF-driven and insulin-driven Akt activation and downstream signaling, indicating its requirement for receptor tyrosine kinase signaling [1]. In podocytes of diabetic kidney disease, increased Lclat1 (ALCAT1) expression was accompanied by increased oxidized cardiolipin and mitochondrial damage, and its deficiency effectively prevented high-glucose-induced oxidized cardiolipin production and mitochondrial damage [3].

In conclusion, Lclat1 plays a crucial role in regulating the fatty acyl profile of key lipids, which impacts multiple cellular functions and signaling pathways. Model-based research, such as knockdown experiments in cell lines and studies in disease-relevant cellular models, has revealed its significance in receptor tyrosine kinase signaling and in the pathogenesis of diabetic kidney disease, providing insights into potential therapeutic targets for related diseases.