{
  "id": 8828615,
  "title": "A multivalent docking platform and Rcn1-mediated inhibition control the extent of calcineurin recruitment to the cell division site for the dephosphorylation of multiple cytokinetic proteins",
  "url": "https://urgent.news/2026/09/20/a-multivalent-docking-platform-and-rcn1-mediated-inhibition-control",
  "topic": "science",
  "section": "Science",
  "published": "2026-09-20T00:00:00.000Z",
  "source": {
    "name": "bioRxiv",
    "slug": "biorxiv",
    "url": "https://www.biorxiv.org/content/10.64898/2026.09.14.751435v1?rss=1"
  },
  "original_language": "en",
  "account": "Calcineurin (CN), a crucial phosphatase in various organisms, plays a vital role in cytokinesis, the process responsible for accurately separating daughter cells. However, the regulation of CN at the division site and the specific substrates it targets for dephosphorylation during cell division have not been well understood. To address this knowledge gap, researchers turned to Schizosaccharomyces pombe, a species of fission yeast that displays significant cell division defects in the absence of CN.\n\nThe study reveals that CN's recruitment to the cytokinetic ring (CR) - the structure responsible for cytokinesis - relies on specific binding surfaces of CN and multivalent interactions with CR components paxillin-like Pxl1 and the F-BAR protein Cdc15. Disruption of these interactions nearly eliminates CN from the CR, leading to severe cytokinetic defects akin to complete loss of CN function.\n\nThrough quantitative phosphoproteomics and proximity labeling-based proteomics, researchers identified candidate substrates of CN involved in cytokinesis, including the F-BAR protein Rga7, the actin regulator Aim21, and three protein kinases. These findings suggest that CN targets a wide array of structural and signaling components essential for cell division. Additionally, the research identifies conserved CN inhibitor Rcn1 as a substrate itself, indicating that Rcn1 restricts CN accumulation at the CR, thereby providing an extra layer of spatial regulation.\n\nIn summary, spatial control of CN is essential for the proper dephosphorylation of multiple cytokinetic proteins, ensuring successful cytokinesis in fission yeast and potentially other organisms.",
  "summary": "Cytokinesis requires coordinated signaling to ensure the accurate physical separation of daughter cells. Calcineurin (CN), a conserved Ca2+/calmodulin-dependent phosphatase, is required for cytokinesis in organisms ranging from yeast to humans, yet how CN is regulated at the division site and the substrates through which it promotes cell division remain poorly understood. Here we use the fission…",
  "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."
}