{
  "abstract": "KDM6A and KDM6B, lysine demethylases, play a central role in regulation of transcription through their demethylation activity towards H3K27me3 and have also been shown to be dynamically regulated upon epithelial-mesenchymal transition (EMT). In particular, KDM6A has been implicated in a variety of malignancies and is frequently mutated in cancers including those in kidney, bladder, colorectal, and breast. KDM6A and KDM6B function as part of the COMPASS-like protein complex (CLC) which includes methyltransferases KMT2C/KMT2D and the regulatory WRAD-subcomplex. KDM6A total protein is known to be suppressed by TGF-{beta} in MCF10A breast cells; however, our examination of protein localization by immunofluorescence and LC-MS/MS reveals that KDM6A expression is lost in the nucleus but retained in the Golgi apparatus, independent of other CLC complex members. Importantly, KDM6A isolated from a biochemically-separated subcellular membranous fraction possesses the catalytic JmjC domain and is enzymatically active, indicating that KDM6A may have non-nuclear substrates. Further, knockdown of KDM6A and treatment with TGF-{beta} similarly alter Golgi apparatus morphology, in a cell type specific manner, suggesting context-dependent regulatory functions. These findings support a model in which KDM6A is necessary to maintain Golgi apparatus morphology and is enzymatically active outside of the nucleus.",
  "abstract_shown": true,
  "affiliations": [
    "Baylor University"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 13,
  "authors": [
    {
      "name": "C. S. Worth"
    },
    {
      "name": "J. M. Conforti"
    },
    {
      "name": "A. M. Nambiar"
    },
    {
      "name": "J. Malone"
    },
    {
      "name": "R. Budhathoki"
    },
    {
      "name": "A. M. Ziegler"
    },
    {
      "name": "K. Polavarapu"
    },
    {
      "name": "H. Lilley"
    },
    {
      "name": "L. Climer"
    },
    {
      "name": "D. D. Simmons"
    },
    {
      "name": "J. Kelber"
    },
    {
      "name": "E. S. Gallagher"
    },
    {
      "affs": [
        0
      ],
      "name": "J. Taube"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/dpqkq2mj58xfn.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.11.02.763691",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.11.02.763691v1.full",
  "id": "dpqkq2mj58xfn",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.11.02.763691v1",
  "language": null,
  "licence": "CC-BY-NC-ND",
  "licence_label": "CC BY-NC-ND",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by-nc-nd/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "biorxiv",
      "cell biology"
    ]
  ],
  "openalex": null,
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.11.02.763691v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-11-02",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/dpqkq2mj58xfn.ris",
  "sources": [
    {
      "first_seen": "2026-11-04T12:21:08Z",
      "native_id": "10.64898/2026.11.02.763691",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.11.02.763691v1"
    }
  ],
  "subjects": [
    {
      "field": "biology",
      "origin": "biorxiv:cell biology",
      "subfield": "cell-biology"
    }
  ],
  "title": "KDM6A is enzymatically active at the Golgi apparatus where it is necessary for maintenance of Golgi apparatus morphology",
  "title_text": "KDM6A is enzymatically active at the Golgi apparatus where it is necessary for maintenance of Golgi apparatus morphology",
  "type": "preprint",
  "updated_at": "2026-11-06T00:21:10Z",
  "url": "https://research.draconitic.com/paper/dpqkq2mj58xfn",
  "venue": "bioRxiv",
  "versions": []
}