{
  "id": 5307058,
  "title": "Cryo-EM structures reveal the mechanism of phosphatidylserine remodeling by membrane-bound glycerophospholipid O-acyltransferase 1",
  "url": "https://urgent.news/2026/09/03/cryo-em-structures-reveal-the-mechanism-of-phosphatidylserine",
  "topic": "science",
  "section": "Science",
  "published": "2026-09-03T00:00:00.000Z",
  "source": {
    "name": "bioRxiv",
    "slug": "biorxiv",
    "url": "https://www.biorxiv.org/content/10.64898/2026.09.01.748671v1?rss=1"
  },
  "original_language": "en",
  "account": "Membrane-bound glycerophospholipid O-acyltransferase 1 (MBOAT1) is essential for cells to maintain proper membrane composition. MBOAT1 cleaves glycerophospholipids at the glycerol sn2-position, creating lysophospholipids that are then reacylated by enzymes to incorporate specific fatty-acyl chains, adjusting membrane properties. The process of MBOAT1 recognizing specific acyl-CoA donors, selecting lysophospholipid acceptors, and releasing products remains unclear. Phosphatidylserine (PS), an anionic phospholipid, influences membrane surface charge, protein recruitment, and cell death-associated membrane recognition. PS acyl-chain remodeling is also associated with ferroptosis resistance.\n\nResearchers revealed that MBOAT1 preferentially generates monounsaturated fatty acid-containing PS from lyso-PS. To understand the mechanism and pathway of MBOAT1-dependent PS remodeling, they employed high-resolution cryo-electron microscopy structures of human MBOAT1. These structures displayed distinct binding poses of the fatty acyl donor, lyso-PS acceptor, and PS product. Using lipidomics, enzymology, and molecular dynamics simulations, the team uncovered the mechanism and pathway of MBOAT1-dependent PS remodeling.",
  "summary": "Lands cycle remodeling of glycerophospholipid acyl chains is crucial for cells to maintain appropriate membrane composition. Glycerophospholipids are cleaved at the glycerol sn2-position by phospholipase A. The lysophospholipids are reacylated by enzymes of the membrane-bound O-acyltransferase (MBOAT) family to incorporate specific fatty-acyl chains to adjust membrane properties. How MBOAT…",
  "key_points": [],
  "editors_take": null,
  "illustration": null,
  "coverage": {
    "outlets": 1,
    "also_reported_by": []
  },
  "ai_generated": true,
  "disclaimer": "Summaries, key points and the editor’s take are written by software from other outlets’ reporting and may contain errors — always check the linked original."
}