{
  "id": 4683604,
  "title": "S-Palmitoylation stabilizes OGT and the OGT-PPP1CC complex",
  "url": "https://urgent.news/2026/08/31/s-palmitoylation-stabilizes-ogt-and-the-ogt-ppp1cc-complex",
  "topic": "science",
  "section": "Science",
  "published": "2026-08-31T00:00:00.000Z",
  "source": {
    "name": "bioRxiv",
    "slug": "biorxiv",
    "url": "https://www.biorxiv.org/content/10.64898/2026.08.29.747956v1?rss=1"
  },
  "original_language": "en",
  "account": "O-linked beta-N-acetylglucosamine (O-GlcNAc) transferase, known as OGT, is responsible for adding O-GlcNAc to thousands of proteins within cells. However, researchers have found that OGT itself undergoes a modification called S-palmitoylation at two specific sites, Cys-472 and Cys-477. This modification is facilitated by a protein called zDHHC14 and undone by another enzyme called acyl protein thioesterase 2 (APT2).\n\nThe study reveals that S-palmitoylation helps stabilize OGT, keeping it away from a lysosomal pathway called CMA. This stabilization is achieved by reducing the interaction between OGT and a chaperone protein called HSC70. Additionally, S-palmitoylation increases the binding affinity between OGT and a protein called PPP1CC, although it does not affect another PPP1CC variant, PPP1CB.\n\nThe researchers further discovered that S-palmitoylation enhances the interaction between OGT and Yes-associated protein-1 (YAP), a protein that works with PPP1CC. As a result, this modification boosts O-GlcNAcylation, a process that modifies YAP. The findings highlight the importance of S-palmitoylation and the CMA-mediated breakdown of lysosomal OGT in fine-tuning the activity of key OGT complexes, such as OGT-PPP1CC. This mechanism also contributes to the selective targeting of OGT substrates.",
  "summary": "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…",
  "key_points": [],
  "editors_take": null,
  "illustration": null,
  "coverage": {
    "outlets": 1,
    "also_reported_by": []
  },
  "ai_generated": true,
  "disclaimer": "Summaries, key points and the editor’s take are written by software from other outlets’ reporting and may contain errors — always check the linked original."
}