{
  "abstract": "Centromeres link chromosomes to spindle microtubules to direct their segregation during mitosis. The vertebrate centromere is built on two critical DNA-binding proteins, the histone H3-variant CENP-A and histone fold protein CENP-T. CENP-T is a potent scaffold for kinetochore assembly, such that concentrating it at ectopic sites is sufficient to build kinetochore-like structures. How cells prevent excess CENP-T from acting at non-centromere sites remains unclear. Here, using optical pooled screening to systematically define the requirements for CENP-A and CENP-T localization, we recover the established CENP-A deposition machinery and reveal a specific role for the proteasome in controlling CENP-T levels. We find that non-centromere CENP-T is degraded in a ubiquitin- and proteasome-dependent manner. Whereas centromere-incorporated CENP-T is stable, CENP-T that is not bound to centromeres is rapidly turned over, with the CENP-T histone fold region sufficient to confer proteasome sensitivity. Quiescent cells, which disassemble their centromeres, continue to express CENP-T but eliminate it through continuous degradation. Thus, whereas CENP-A is controlled primarily through regulated deposition, cells additionally control CENP-T by selectively degrading the unincorporated protein.",
  "abstract_shown": true,
  "affiliations": [
    "Whitehead Institute for Biomedical Research"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 7,
  "authors": [
    {
      "name": "O. Marescal"
    },
    {
      "name": "K.-C. Su"
    },
    {
      "name": "M. Di Bernardo"
    },
    {
      "name": "K. Manzer"
    },
    {
      "name": "J. He"
    },
    {
      "name": "R. Kern"
    },
    {
      "affs": [
        0
      ],
      "name": "I. M. Cheeseman"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/8tfd0f7nsvhnj.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.10.14.759079",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.10.14.759079v1.full",
  "id": "8tfd0f7nsvhnj",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.10.14.759079v1",
  "language": null,
  "licence": "CC-BY-NC",
  "licence_label": "CC BY-NC",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by-nc/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "biorxiv",
      "cell biology"
    ],
    [
      "openalex",
      "1307|Microtubule and mitosis dynamics"
    ]
  ],
  "openalex": "W7222757364",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.10.14.759079v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-14",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/8tfd0f7nsvhnj.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:28:04Z",
      "native_id": "10.64898/2026.10.14.759079",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.10.14.759079v1"
    }
  ],
  "subjects": [
    {
      "field": "biology",
      "origin": "biorxiv:cell biology",
      "subfield": "cell-biology"
    }
  ],
  "title": "Functional genetics reveals a role for the proteasome in regulating centromere assembly",
  "title_text": "Functional genetics reveals a role for the proteasome in regulating centromere assembly",
  "type": "preprint",
  "updated_at": "2026-10-30T12:28:04Z",
  "url": "https://research.draconitic.com/paper/8tfd0f7nsvhnj",
  "venue": "bioRxiv",
  "versions": []
}