{
  "abstract": "Receptor signaling is often framed as protein recruitment after stimulation, but whether receptor-proximal environments are organized in composition and phosphorylation state beforehand remains unclear. We used CD18-APEX2 proximity labeling and a spatial membrane reference to quantify proteins and phosphosites near leukocyte {beta}2 integrins. At rest, receptors, adaptors and Rap GTPases were preferentially represented relative to several catalytic classes. Parent-protein correction revealed spatial phosphoform organization, with 32% of 4,564 phosphosites deviating significantly from the distribution center and 56% of proteins with multiple quantified sites showing divergence beyond measurement error. Sustained activation altered 31% of phosphosites while 95.9% of proteins remained equivalent within {+/-}0.5 log2 and spatial phosphoform organization largely persisted. Most phosphorylation responses were shared across both labeling environments, whereas receptor-preferential changes were dominated by phosphosites. These findings suggest that receptor signaling can regulate pre-existing molecular states without extensive protein redistribution.",
  "abstract_shown": true,
  "affiliations": [
    "The University of Texas Health Science Center at Houston"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 4,
  "authors": [
    {
      "affs": [
        0
      ],
      "name": "T. I. Moore"
    },
    {
      "name": "N. A. Hummell"
    },
    {
      "name": "H. Jonnagaddala"
    },
    {
      "name": "M. Kalocsay"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/1v2c9nxdtd8yv.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.11.04.762546",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.11.04.762546v1.full",
  "id": "1v2c9nxdtd8yv",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.11.04.762546v1",
  "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": null,
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.11.04.762546v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-11-04",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/1v2c9nxdtd8yv.ris",
  "sources": [
    {
      "first_seen": "2026-11-06T12:20:54Z",
      "native_id": "10.64898/2026.11.04.762546",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.11.04.762546v1"
    }
  ],
  "subjects": [
    {
      "field": "biology",
      "origin": "biorxiv:cell biology",
      "subfield": "cell-biology"
    }
  ],
  "title": "Receptor-proximal phosphoform organization precedes β2 integrin activation",
  "title_text": "Receptor-proximal phosphoform organization precedes β2 integrin activation",
  "type": "preprint",
  "updated_at": "2026-11-07T00:21:02Z",
  "url": "https://research.draconitic.com/paper/1v2c9nxdtd8yv",
  "venue": "bioRxiv",
  "versions": []
}