{
  "id": 2189928,
  "title": "C. elegans Dicer stacks with the RIG-I-like receptor DRH-1 to cleave dsRNA",
  "url": "https://urgent.news/2026/08/20/c-elegans-dicer-stacks-with-the-rig-i-like-receptor-drh-1-to-cleave",
  "topic": "science",
  "section": "Science",
  "published": "2026-08-20T00:00:00.000Z",
  "source": {
    "name": "bioRxiv",
    "slug": "biorxiv",
    "url": "https://www.biorxiv.org/content/10.64898/2026.08.16.745104v1?rss=1"
  },
  "original_language": "en",
  "account": null,
  "summary": "In prior studies we showed that the nematode ancestor of Dicer's helicase domain had minimal ATP hydrolysis, translocation and dsRNA binding activity, and in extant C. elegans the RIG-I like receptor (RLR) DRH-1, and the dsRNA binding protein RDE-4, were co-opted to provide these activities. Here we report cleavage-competent cryo-EM structures of the antiviral complex (AVC; DCR-1{middle…",
  "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."
}