{
  "abstract": "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 enzymes recognize specific acyl-CoA donors, select lysophospholipid acceptors, and release products is unclear. Phosphatidylserine (PS), a critical anionic phospholipid, controls membrane surface charge, signaling-protein recruitment, and cell-death-associated membrane recognition, and PS acyl-chain remodeling is linked to ferroptosis resistance. Here, we showed that MBOAT1 preferentially generates monounsaturated fatty acid-containing PS from lyso-PS. High-resolution cryo-electron microscopy structures of human MBOAT1 captured distinct binding poses of the fatty acyl donor, lyso-PS acceptor, and PS product. With lipidomics, enzymology and molecular dynamics simulations, these structures reveal the mechanism and pathway of MBOAT1-dependent PS remodeling.",
  "abstract_shown": true,
  "affiliations": [
    "Memorial Sloan Kettering Cancer Center"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 9,
  "authors": [
    {
      "name": "L. Kim"
    },
    {
      "name": "S. Kim"
    },
    {
      "name": "R. Ly"
    },
    {
      "name": "L. Cohen-Abeles"
    },
    {
      "name": "P. Liu"
    },
    {
      "name": "X. Jiang"
    },
    {
      "name": "D. Kwon"
    },
    {
      "name": "R. V. Farese"
    },
    {
      "affs": [
        0
      ],
      "name": "T. C. Walther"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/exmm0q7r3x90s.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.09.01.748671",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.09.01.748671v1.full",
  "id": "exmm0q7r3x90s",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.09.01.748671v1",
  "language": null,
  "licence": "CC-BY",
  "licence_label": "CC BY",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "biorxiv",
      "biochemistry"
    ],
    [
      "openalex",
      "1303|Lipid metabolism and biosynthesis"
    ]
  ],
  "openalex": "W7207776008",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.09.01.748671v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-09-01",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/exmm0q7r3x90s.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:18:50Z",
      "native_id": "10.64898/2026.09.01.748671",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.09.01.748671v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "openalex:1303|Lipid metabolism and biosynthesis",
      "subfield": "enzymology-metabolism"
    }
  ],
  "title": "Cryo-EM structures reveal the mechanism of phosphatidylserine remodeling by membrane-bound glycerophospholipid O-acyltransferase 1",
  "title_text": "Cryo-EM structures reveal the mechanism of phosphatidylserine remodeling by membrane-bound glycerophospholipid O-acyltransferase 1",
  "type": "preprint",
  "updated_at": "2026-10-30T12:18:50Z",
  "url": "https://research.draconitic.com/paper/exmm0q7r3x90s",
  "venue": "bioRxiv",
  "versions": []
}