{
  "abstract": "O-linked {beta}-N-acetylglucosamine (O-GlcNAc) transferase (OGT) is the sole writer for intracellular O-GlcNAcylation. It catalyzes O-GlcNAcylation of thousands of protein substrates, but relatively less is known about the post-translational modifications that occur on OGT itself. Herein, we demonstrate that OGT is S-palmitoylated at Cys-472 and Cys-477, which is mediated by the S-acyltransferase Zinc Finger DHHC-Type Palmitoyl transferase 14 (zDHHC14) and removed by acyl protein thioesterase 2 (APT2). S-Palmitoylation stabilizes OGT by shunting it away from the lysosomal chaperone-mediated autophagy (CMA) pathway, as S-palmitoylation decreases the interaction between OGT and heat shock cognate 70 kDa protein (HSC70), the CMA chaperone. Via label-free quantitative mass spectrometry, we find that S- palmitoylation elevates the affinity between OGT and protein phosphatase 1 catalytic subunit gamma (PPP1CC), but not PPP1CB. We further demonstrate that S-palmitoylation of OGT augments binding with Yes-associated protein-1 (YAP), a protein that associates with PPP1CC, and subsequently enhances YAP O-GlcNAcylation. Our work unearths S-palmitoylation of OGT and CMA-mediated degradation of lysosomal OGT, the orchestration of which finetunes the activity of key OGT complexes, such as OGT-PPP1CC, and contributes to OGT substrate selectivity.",
  "abstract_shown": true,
  "affiliations": [
    "Capital Normal University"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 10,
  "authors": [
    {
      "name": "X. Lu"
    },
    {
      "name": "T. Xu"
    },
    {
      "affs": [
        0
      ],
      "name": "J. Li"
    },
    {
      "name": "Y. Liu"
    },
    {
      "name": "W. Zhou"
    },
    {
      "name": "K. Wang"
    },
    {
      "name": "C. Niu"
    },
    {
      "name": "N. Tang"
    },
    {
      "name": "L. Zhang"
    },
    {
      "affs": [
        0
      ],
      "name": "J. Li"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/df20cjkehc13e.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.08.29.747956",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.08.29.747956v1.full",
  "id": "df20cjkehc13e",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.08.29.747956v1",
  "language": null,
  "licence": "CC-BY",
  "licence_label": "CC BY",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "biorxiv",
      "biochemistry"
    ],
    [
      "openalex",
      "1312|Glycosylation and Glycoproteins Research"
    ]
  ],
  "openalex": "W7204856689",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.08.29.747956v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-08-29",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/df20cjkehc13e.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:30Z",
      "native_id": "10.64898/2026.08.29.747956",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.08.29.747956v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "openalex:1312|Glycosylation and Glycoproteins Research",
      "subfield": "molecular-biology"
    }
  ],
  "title": "S-Palmitoylation stabilizes OGT and the OGT-PPP1CC complex",
  "title_text": "S-Palmitoylation stabilizes OGT and the OGT-PPP1CC complex",
  "type": "preprint",
  "updated_at": "2026-10-30T12:17:30Z",
  "url": "https://research.draconitic.com/paper/df20cjkehc13e",
  "venue": "bioRxiv",
  "versions": [
    {
      "doi": "10.3724/abbs.2026173",
      "pid": null,
      "relation": "published-as",
      "title": null,
      "venue": null
    }
  ]
}