{
  "abstract": "The endoplasmic reticulum (ER) is the primary site of eukaryotic membrane protein synthesis and quality control, which largely relies on ER-associated degradation (ERAD) to eliminate aberrant nascent proteins. In yeast, two ubiquitin ligases target proteins for ERAD based on aberrancies in substrate transmembrane (ERAD-M), lumenal (ERAD-L), or cytosolic (ERAD-C) domains. How an expanded repertoire of mammalian ERAD factors selects substrates across these classifications is unclear. Here, we show that the human ER-resident RNF185 ubiquitin ligase complex destabilizes a small but specific set of membrane proteins that span all three ERAD branches. Comparisons of three single-pass membrane proteins destabilized by RNF185 identify ERAD-M features in misoriented CHST10, ERAD-C features in unassembled SRPRB, and N-linked glycosylation-dependent ERAD-L features in ATP1B2. Our findings identify RNF185-destabilized membrane proteins with distinct aberrancies that collectively encompass all canonical ERAD substrate classifications and unexpectedly diverse quality control defects.",
  "abstract_shown": true,
  "affiliations": [
    "Harvard Medical School"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 5,
  "authors": [
    {
      "name": "H. Chino"
    },
    {
      "name": "I. M. Ruiz"
    },
    {
      "name": "J. H. Corbo"
    },
    {
      "name": "J. A. Paulo"
    },
    {
      "affs": [
        0
      ],
      "name": "S. Shao"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/a7ejcnargvh6f.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.09.23.753758",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.09.23.753758v1.full",
  "id": "a7ejcnargvh6f",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.09.23.753758v1",
  "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",
      "1307|Endoplasmic Reticulum Stress and Disease"
    ]
  ],
  "openalex": "W7214231259",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.09.23.753758v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-09-23",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/a7ejcnargvh6f.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:24:15Z",
      "native_id": "10.64898/2026.09.23.753758",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.09.23.753758v1"
    }
  ],
  "subjects": [
    {
      "field": "biology",
      "origin": "biorxiv:cell biology",
      "subfield": "cell-biology"
    }
  ],
  "title": "RNF185 destabilizes specific membrane proteins that span all ERAD branches",
  "title_text": "RNF185 destabilizes specific membrane proteins that span all ERAD branches",
  "type": "preprint",
  "updated_at": "2026-10-30T12:24:15Z",
  "url": "https://research.draconitic.com/paper/a7ejcnargvh6f",
  "venue": "bioRxiv",
  "versions": []
}