{
  "abstract": "The unfolded protein response (UPR) preserves endoplasmic reticulum (ER) proteostasis through coordinated transcriptional and translational programs that promote adaptation and prevents apoptosis. A central component of this response is the IRE1-XBP1 signaling axis, in which IRE1-mediated unconventional splicing of XBP1 mRNA generates the active transcription factor XBP1s. While the mechanisms governing IRE1 activation and XBP1 splicing have been extensively characterized, the post-transcriptional processes that sustain XBP1s expression remain poorly understood. Here, we identify RNA-binding motif protein 25 (RBM25) as a key post-transcriptional regulator of the UPR that selectively stabilizes spliced XBP1 mRNA during ER stress. RBM25 binds the XBP1s 3' untranslated region and prolongs XBP1s mRNA half-life without affecting unspliced XBP1u transcripts or IRE1-dependent regulated decay (RIDD) targets. Consequently, RBM25 depletion diminishes XBP1 transcriptional output, compromises adaptive UPR signaling, and sensitizes cells to ER stress-induced death across multiple stress paradigms. Together, our findings uncover a previously unrecognized RNA-based regulatory checkpoint that amplifies and sustains XBP1 signaling, thereby tuning the magnitude of the adaptive UPR and cellular survival under proteotoxic stress.",
  "abstract_shown": true,
  "affiliations": [
    "Uniwersity of Wroclaw"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 9,
  "authors": [
    {
      "name": "A. Wiech-Walow"
    },
    {
      "name": "A. Barton"
    },
    {
      "name": "M. Tracz"
    },
    {
      "name": "S. Koziol"
    },
    {
      "name": "J. Grzyb"
    },
    {
      "name": "P. Czechowicz"
    },
    {
      "name": "J. F. Collawn"
    },
    {
      "name": "E. Chevet"
    },
    {
      "affs": [
        0
      ],
      "name": "R. Bartoszewski"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/amd9zgraqwyrm.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.11.04.764219",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.11.04.764219v1.full",
  "id": "amd9zgraqwyrm",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.11.04.764219v1",
  "language": null,
  "licence": "CC-BY-ND",
  "licence_label": "CC BY-ND",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by-nd/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "biorxiv",
      "molecular biology"
    ]
  ],
  "openalex": null,
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.11.04.764219v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-11-04",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/amd9zgraqwyrm.ris",
  "sources": [
    {
      "first_seen": "2026-11-05T00:21:58Z",
      "native_id": "10.64898/2026.11.04.764219",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.11.04.764219v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "biorxiv:molecular biology",
      "subfield": "molecular-biology"
    }
  ],
  "title": "RBM25 selectively stabilizes XBP1s mRNA independently of splicing factor activity",
  "title_text": "RBM25 selectively stabilizes XBP1s mRNA independently of splicing factor activity",
  "type": "preprint",
  "updated_at": "2026-11-05T12:20:35Z",
  "url": "https://research.draconitic.com/paper/amd9zgraqwyrm",
  "venue": "bioRxiv",
  "versions": []
}