{
  "abstract": "Coordination of biological function requires the partition of cellular components including into biomolecular condensates, but an overall landscape of how protein compartmentalize into higher-order assemblies under stress is still emerging. We apply proteome-wide solubility profiling to compare the compositions of NP-40-insoluble proteins and their phosphorylation status, using a new mass spectrometry-based hybrid bottom-up and chemical middle-down proteomics approach to analyze the solubility behavior of 8,740 proteins and 31,647 phosphopeptides under normal and ER stress conditions. Cell stress induces a pervasive differential partition of proteins in and out of detergent-insoluble cellular compartments. This differential partition is partially orthogonal to stress-induced abundance changes and comprises both phosphorylation-dependent and phosphorylation-independent mechanisms. Whereas phosphorylation-independent partition changes involve largely secretory pathway proteins and implicate higher-order assemblies of chaperones and clients, phosphorylation-based partitions suggest a dynamic rearrangement of biomolecular condensate compositions across cytoplasmic and nuclear ribonucleoprotein assemblies. The accumulation of serine/arginine rich (SR) proteins and other annotated nuclear speckle members in the condensate-rich proteome fractions emerges as a central feature of stress-induced remodeling. Our results establish global solubility dynamics as an integral component of proteome stress response and implicates broad involvements of splice factor spatial reorganization as a prominent facet of ER stress response.",
  "abstract_shown": true,
  "affiliations": [
    "University of Colorado School of Medicine"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 7,
  "authors": [
    {
      "name": "B. Pandi"
    },
    {
      "name": "D. C. M. Ng"
    },
    {
      "name": "P. Schaal"
    },
    {
      "name": "L. Alamillo"
    },
    {
      "name": "S. Binti"
    },
    {
      "name": "E. Lau"
    },
    {
      "affs": [
        0
      ],
      "name": "M. P. Y. Lam"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/5tqda5yn71rmk.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.09.22.753649",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.09.22.753649v1.full",
  "id": "5tqda5yn71rmk",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.09.22.753649v1",
  "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",
      "biochemistry"
    ],
    [
      "openalex",
      "1607|Advanced Proteomics Techniques and Applications"
    ]
  ],
  "openalex": "W7214103682",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.09.22.753649v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-09-22",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/5tqda5yn71rmk.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:24:07Z",
      "native_id": "10.64898/2026.09.22.753649",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.09.22.753649v1"
    }
  ],
  "subjects": [
    {
      "field": "chemistry",
      "origin": "openalex:1607|Advanced Proteomics Techniques and Applications",
      "subfield": "physical"
    }
  ],
  "title": "Tracking cellular biomolecular condensate dynamics under proteostatic stress with middle-down phosphoproteomics",
  "title_text": "Tracking cellular biomolecular condensate dynamics under proteostatic stress with middle-down phosphoproteomics",
  "type": "preprint",
  "updated_at": "2026-10-30T12:24:07Z",
  "url": "https://research.draconitic.com/paper/5tqda5yn71rmk",
  "venue": "bioRxiv",
  "versions": []
}