LRAT catalyzes the acylation of all-trans retinol using the sn-1 acyl group from phosphatidylcholine to produce all-trans retinyl esters, which serve as the storage form of vitamin A. These retinyl esters are subsequently processed in the retinal pigment epithelium into 11-cis-retinaldehyde, the chr4 essential for rhodopsin and cone photopigments, making LRAT critical for normal vision. The gene is required for cone photoreceptor survival and proper rod photoreceptor morphology. Pathogenic variants in LRAT cause Leber congenital amaurosis and other early-onset retinal dystrophies. In a large German cohort, LRAT variants accounted for a small fraction of genetically confirmed Leber congenital amaurosis cases, though affected patients exhibited the characteristic severe phenotype of markedly reduced visual acuity and extinguished electroretinograms 1. Recent evidence suggests that modulating the retinoid cycle through pharmacological approaches may offer therapeutic benefit in retinal degeneration 2. Beyond retinal function, LRAT serves as a marker of hepatic stellate cell identity and plays a role in liver fibrosis pathophysiology. During pathological activation of hepatic stellate cells in liver injury, LRAT-expressing cells undergo metabolic and transcriptional changes associated with fibrogenesis 34.