{
  "abstract": "The proteasome activator PA200 binds to the catalytic core of both standard proteasome (s20S) and the immunoproteasome (i20S); however, whether PA200 uses the same mechanisms to activate i20S remains unknown. In this work, the cryo-EM structures of singly- and doubly-capped i20S–PA200 complexes, combined with complementary in vitro biochemical assays, show that binding of the first PA200 induces allosteric bending of the i20S and widens the opposite α-ring, promoting higher PA200 occupancy and stronger activation compared to the s20S. PA200 also selectively modulates i20S proteolytic activity by enhancing peptide production and shifting cleavage specificity toward caspase-like activity. In cells and tissues co-expressing PA200, s20S, and i20S, PA200 preferentially associates with the i20S. Moreover, PA200 and i20S catalytic subunits are differentially regulated, with PA200 playing a potential role in regulating the i20S subunits’ expression. Overall, these findings suggest that PA200 contributes to the regulation of i20S function and dynamics.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": null,
  "author_total": 21,
  "authors": [
    {
      "name": "Dušan Živković"
    },
    {
      "name": "Amélie Bosc-Rosati"
    },
    {
      "name": "Angelique Sanchez Dafun"
    },
    {
      "name": "Fatme Mourtada"
    },
    {
      "name": "Przemysław Grygier"
    },
    {
      "name": "Ayse Seda Yazgili"
    },
    {
      "name": "Marijke Jansma"
    },
    {
      "name": "Michał Rawski"
    },
    {
      "name": "Anna Czarna"
    },
    {
      "name": "Stefan Bohn"
    },
    {
      "name": "Krzysztof M Zak"
    },
    {
      "name": "André Santos Dias Mourão"
    },
    {
      "name": "Norbert Reiling"
    },
    {
      "name": "Linda Zemke"
    },
    {
      "name": "Kai Guo"
    },
    {
      "name": "Jürgen Behr"
    },
    {
      "name": "Odile Burlet-Schiltz"
    },
    {
      "name": "Grzegorz M Popowicz"
    },
    {
      "name": "Julien Marcoux"
    },
    {
      "name": "Silke Meiners"
    },
    {
      "name": "Marie-Pierre Bousquet"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/1knt597gvzgdg.bib",
  "cited_by": 0,
  "doi": "10.1038/s41467-026-75325-w",
  "fulltext_url": null,
  "id": "1knt597gvzgdg",
  "issns": [
    "2041-1723",
    "2041-1723"
  ],
  "landing_url": "https://hal.science/hal-05746427v1",
  "language": "en",
  "licence": "CC-BY-4.0",
  "licence_label": "CC BY 4.0",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "hal",
      "0.sdv"
    ],
    [
      "hal",
      "1.sdv.bbm"
    ],
    [
      "hal",
      "1.sdv.imm"
    ],
    [
      "hal",
      "2.sdv.imm.ia"
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    [
      "hal",
      "2.sdv.imm.ii"
    ],
    [
      "openalex",
      "1312|Ubiquitin and proteasome pathways"
    ]
  ],
  "openalex": "W7202184583",
  "pdf_url": "https://hal.science/hal-05746427/document",
  "pmcid": null,
  "pmid": null,
  "published": "2026-09-11",
  "publisher": "Nature Publishing Group",
  "ris": "https://research.draconitic.com/paper/1knt597gvzgdg.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:33Z",
      "native_id": "hal-05746427",
      "source": "hal",
      "url": "https://hal.science/hal-05746427v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "hal:1.sdv.bbm",
      "subfield": "general"
    },
    {
      "field": "biology",
      "origin": "hal:1.sdv.imm",
      "subfield": "immunology"
    }
  ],
  "title": "PA200 modulates immunoproteasome structure and activity",
  "title_text": "PA200 modulates immunoproteasome structure and activity",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:17:33Z",
  "url": "https://research.draconitic.com/paper/1knt597gvzgdg",
  "venue": "Nature Communications",
  "versions": []
}