{
  "id": 17950018,
  "title": "Molecular basis of Cyclin B1-CDK1 recruitment by MAD1",
  "url": "https://urgent.news/2026/11/03/molecular-basis-of-cyclin-b1-cdk1-recruitment-by-mad1",
  "topic": "science",
  "section": "Science",
  "published": "2026-11-03T00:00:00.000Z",
  "source": {
    "name": "bioRxiv",
    "slug": "biorxiv",
    "url": "https://www.biorxiv.org/content/10.64898/2026.11.01.762963v1?rss=1"
  },
  "original_language": "en",
  "account": null,
  "summary": "The interaction between Cyclin B1-CDK1 and MAD1 recruits kinase activity to the nuclear pore complex and kinetochore corona to sustain spindle assembly checkpoint (SAC) signaling. Here, we characterize a short linear motif (SLiM) within MAD1 that mediates its interaction with Cyclin B1. This SLiM peptide is specific for B-type cyclins and lacks the canonical \"RxL\" cyclin-binding consensus…",
  "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."
}