{
  "abstract": "Cells degrade the autophagy receptor p62/sequestosome 1 (SQSTM1) in lysosomes. By knocking the HiBiT peptide into the endogenous SQSTM1 locus, we show that export is a second, quantitatively comparable fate. Specifically, p62 leaves cells continuously inside membrane-enclosed carriers at a rate similar to that of LC3B. Blocking lysosomal degradation amplifies release through an ATG5- and FIP200-dependent route, whereas a basal route persists in autophagy-deficient cells. Thus, p62 exits by at least two parallel pathways. Export requires PB1-mediated self-oligomerization but not LC3 binding, Kelch-like ECH-associated protein 1 (KEAP1) binding, or an intact ubiquitin-associated domain. Hence, oligomerization is the sorting determinant. KEAP1 is also released, and dominant-negative RAB27A retains both proteins inside cells and lowers nuclear factor erythroid 2-related factor 2 transcriptional output. Secretion is therefore a second outlet for the p62-KEAP1 module, and its interruption co-varies with a dampened oxidative stress response.",
  "abstract_shown": true,
  "affiliations": [
    "Hirosaki University"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 4,
  "authors": [
    {
      "name": "K. Saito"
    },
    {
      "name": "T. Takahashi"
    },
    {
      "name": "M. Arakawa"
    },
    {
      "affs": [
        0
      ],
      "name": "E. Morita"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/eg0yn8rmt5asy.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.10.07.757498",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.10.07.757498v1.full",
  "id": "eg0yn8rmt5asy",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.10.07.757498v1",
  "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",
      "cell biology"
    ],
    [
      "openalex",
      "2713|Autophagy in Disease and Therapy"
    ]
  ],
  "openalex": "W7221119459",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.10.07.757498v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-07",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/eg0yn8rmt5asy.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:26:53Z",
      "native_id": "10.64898/2026.10.07.757498",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.10.07.757498v1"
    }
  ],
  "subjects": [
    {
      "field": "biology",
      "origin": "biorxiv:cell biology",
      "subfield": "cell-biology"
    }
  ],
  "title": "Secretion is a second fate for p62 and is coupled to KEAP1/NRF2 signaling",
  "title_text": "Secretion is a second fate for p62 and is coupled to KEAP1/NRF2 signaling",
  "type": "preprint",
  "updated_at": "2026-10-30T12:26:53Z",
  "url": "https://research.draconitic.com/paper/eg0yn8rmt5asy",
  "venue": "bioRxiv",
  "versions": []
}