{
  "id": 192673,
  "title": "Structural studies reveal how lipid-transport proteins may influence neurodegenerative disease",
  "url": "https://urgent.news/2026/08/05/structural-studies-reveal-how-lipid-transport-proteins-may-influence",
  "topic": "health",
  "section": "Health & Medicine",
  "published": "2026-08-05T20:40:01.000Z",
  "source": {
    "name": "Medical Xpress",
    "slug": "medical-xpress",
    "url": "https://medicalxpress.com/news/2026-08-reveal-lipid-proteins-neurodegenerative-disease.html"
  },
  "original_language": "en",
  "account": "Researchers at Yale School of Medicine have undertaken the most comprehensive structural analysis of a class of proteins linked to neurodegenerative diseases. The studies, published in Cell and Molecular Cell, examine two similar proteins whose mutations cause chorea-acanthocytosis (a Huntington-like condition) and Parkinson's disease. The findings provide a foundation for understanding how these proteins function and are regulated, as well as how their mutations result in disease. Lipids, which make up cell membranes and organelles, are primarily produced in the endoplasmic reticulum (ER). While scientists previously believed lipids were transported from the ER to other organelles via vesicles or small movements, recent structural studies revealed a third method: rod-like protein structures called VPS13 proteins act as bridges, facilitating bulk lipid movement directly from the ER to organelle membranes. The two new studies are the first complete molecular characterizations of two VPS13 proteins, offering insight into their regulation. The VPS13A study, led by Karin Reinisch, found that mutations in this protein are associated with chorea-acanthocytosis (now renamed VPS13A disease), a disorder causing involuntary movements and abnormal blood cells. Cryo-electron microscopy revealed how VPS13A delivers lipids to one layer of the membrane, while a protein called XK helps evenly distribute those lipids between both layers. This dual-layer regulation is crucial, as uneven layers could lead to membrane dysfunction. The VPS13C study, conducted by Dazhi Li, found that when VPS13C isn't attached to a lysosome (a cell's \"trash can\"), a crown-like structure blocks the lipid transport tube, rendering the protein inactive. Only when VPS13C undergoes a conformational change can it deliver lipids effectively. This same crown-like structure exists on VPS13A, allowing the team to capture the protein in its active state. Understanding the regulation of VPS13 proteins could help scientists uncover the mechanisms behind neurodegenerative diseases and develop therapies. For instance, enhancing VPS13C's function could potentially treat Parkinson's disease, where lysosome membrane dysfunction is implicated.",
  "summary": "Researchers at Yale School of Medicine have conducted the first comprehensive structural analyses of a class of proteins whose dysfunction is associated with neurodegenerative diseases.",
  "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."
}