{
  "abstract": "Integral membrane enzymes operate within molecular environments, yet how these are organized remains poorly understood. Using M. smegmatis as a mycobacterial model, we define the membrane environment of the protein O-mannosyltransferase MtPMT through stratified interactomics combining affinity purification-mass spectrometry under four stringencies with a persistence score. This approach resolves a persistent membrane-associated core of 108 proteins from more transient layers, revealing a hierarchically organized landscape enriched in Sec protein translocation, protein biogenesis and envelope proteostasis machineries.\n\nReciprocal affinity purification and in vivo FRET identify YajC and FtsH as neighbors of MtPMT, while structural modelling supports integration within a Sec-associated assembly. Genetic disruption of factors reduces O-mannosylation activity, demonstrating dependence on platform integrity. The MtPMT-associated network is remodelled during growth, indicating an adaptive system. Loss of POM compromises envelope permeability and stress resilience, linking Omannosylation to fitness. Together, our results establish protein O-mannosylation as an integrated component of a dynamic membrane platform coordinating secretion, membrane protein biogenesis and proteostasis. Our findings support a model in which mycobacterial membranes contain specialized domains dynamically modulated by physiological state.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 6,
  "authors": [
    {
      "name": "Chloé Rivière"
    },
    {
      "name": "Gabriel Publicola"
    },
    {
      "name": "Alexandre Stella"
    },
    {
      "name": "Odile Burlet-Schiltz"
    },
    {
      "name": "Jérôme Nigou"
    },
    {
      "name": "Michel Rivière"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/36vm0s13gvwkq.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.09.29.755281",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.09.29.755281v1.full",
  "id": "36vm0s13gvwkq",
  "issns": [],
  "landing_url": "https://hal.science/hal-05845083v1",
  "language": "en",
  "licence": "CC-BY-NC-ND-4.0",
  "licence_label": "CC BY-NC-ND 4.0",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by-nc-nd/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "biorxiv",
      "cell biology"
    ],
    [
      "hal",
      "0.sdv"
    ],
    [
      "openalex",
      "1311|Bacterial Genetics and Biotechnology"
    ]
  ],
  "openalex": "W7220364802",
  "pdf_url": "https://hal.science/hal-05845083/document",
  "pmcid": null,
  "pmid": null,
  "published": "2026-09-29",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/36vm0s13gvwkq.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:18:03Z",
      "native_id": "hal-05845083",
      "source": "hal",
      "url": "https://hal.science/hal-05845083v1"
    },
    {
      "first_seen": "2026-10-30T12:26:03Z",
      "native_id": "10.64898/2026.09.29.755281",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.09.29.755281v1"
    }
  ],
  "subjects": [
    {
      "field": "biology",
      "origin": "biorxiv:cell biology",
      "subfield": "cell-biology"
    }
  ],
  "title": "Dynamic membrane organization coordinates protein-O-mannosylation and proteostasis in mycobacteria",
  "title_text": "Dynamic membrane organization coordinates protein-O-mannosylation and proteostasis in mycobacteria",
  "type": "preprint",
  "updated_at": "2026-11-01T12:20:45Z",
  "url": "https://research.draconitic.com/paper/36vm0s13gvwkq",
  "venue": "HAL",
  "versions": []
}