{
  "id": 9625969,
  "title": "Chaperone isoform and interactome mapping reveals functional diversification of DNAJA2-DNAJA4 complexes via stress-regulated isoforms",
  "url": "https://urgent.news/2026/09/24/chaperone-isoform-and-interactome-mapping-reveals-functional",
  "topic": "science",
  "section": "Science",
  "published": "2026-09-24T00:00:00.000Z",
  "source": {
    "name": "bioRxiv",
    "slug": "biorxiv",
    "url": "https://www.biorxiv.org/content/10.64898/2026.09.23.753896v1?rss=1"
  },
  "original_language": "en",
  "account": "The human HSP70 chaperone network maintains cellular proteostasis through a diverse repertoire of HSP70s and co-chaperones. Researchers have now mapped the isoform, tissue-expression, and interaction landscapes of this network, revealing a modular interactome containing both known and novel DNAJ-DNAJ interactions. They found that there are differences in the expression of isoforms between different tissues, as well as widespread co-expression of alternative isoforms, suggesting additional ways in which these proteins can diversify their functions. Focusing on an uncharacterized complex involving DNAJA2 and DNAJA4, researchers identified a stress-inducible isoform of DNAJA4 called DNAJA4-CTD-II. This isoform was found to interact with both DNAJA2 and DNAJA4, and this interaction was enhanced following exposure to sodium arsenite, a stress-inducing agent. Functionally, DNAJA4-CTD-II was found to localize with aggregates of the protein TDP-43, and it significantly suppressed the accumulation of these aggregates in a DNAJA2-dependent manner. Overall, this research reveals extensive and previously unknown complexity within the HSP70 network, including isoform-dependent hetero-complex remodeling as a new layer of regulation for chaperone networks.",
  "summary": "The human HSP70 chaperone network maintains cellular proteostasis through a diverse repertoire of HSP70s and co-chaperones. Here we examine alternative isoforms and co-chaperone hetero-complexes as additional sources of network complexity. To that end, we systematically mapped the isoform, tissue-expression, and interaction landscapes of the human HSP70 network, revealing a modular interactome…",
  "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."
}