Membrane-bound O-acyltransferase domain-containing protein 7 (MBOAT7)

Membrane-bound O-acyltransferase domain-containing protein 7 (MBOAT7) is an integral membrane enzyme of the MBOAT family that catalyzes the transfer of an acyl group, preferentially from arachidonoyl-CoA, to lysophosphatidylinositol (lyso-PI), thereby generating phosphatidylinositol. This enzyme plays a central role in the phospholipid remodeling cycle (Land’s cycle), which is vital for maintaining the correct composition of glycerophospholipids in cell membranes. MBOAT7 activity is especially important in neuronal tissues for normal brain development and function. Genetic variants in MBOAT7 are linked to intellectual disability, early onset seizure disorders, and autism-like syndromes, and its dysregulation has been associated with liver disease and carcinogenesis. Recent structural studies reveal MBOAT7 comprises 11 transmembrane helices and operates at the interface of the cytosol and endoplasmic reticulum lumen, coordinating the selective acylation of lyso-phospholipids. Small-molecule inhibitors targeting MBOAT7 are under research for their potential to modulate disease-related lipid remodeling pathways.

Other names

LPIATLPIAT1LPLAT7LPLAT11Lyso-PI acyltransferaseLysophosphatidylinositol acyltransferaseO-acyltransferase domain-containing protein 7Bladder and breast carcinoma-overexpressed gene 1BB1LENG4OACT7hMBOA-7LRC4MRT57MBOA7membrane bound O-acyltransferase domain containing 7LPLAT

Inhibition of MBOAT7 reduces phospholipid remodeling by preventing transfer of arachidonoyl (or other acyl) groups to lysophosphatidylinositol (lyso-PI), affecting membrane lipid content and downstream signaling pathways