{
  "id": 13965446,
  "title": "Phosphorylation of β-arrestins impacts recruitment to Parathyroid Hormone Receptor 1 (PTH1R) at the cell surface and endosomes",
  "url": "https://urgent.news/2026/10/12/phosphorylation-of-arrestins-impacts-recruitment-to-parathyroid",
  "topic": "science",
  "section": "Science",
  "published": "2026-10-12T00:00:00.000Z",
  "source": {
    "name": "bioRxiv",
    "slug": "biorxiv",
    "url": "https://www.biorxiv.org/content/10.64898/2026.10.05.756893v1?rss=1"
  },
  "original_language": "en",
  "account": "Beta-arrestins 1 and 2 are intracellular proteins that regulate the location and signaling of GPCRs, including Parathyroid Hormone Receptor 1 (PTH1R). PTH1R triggers {beta}-arrestin-dependent signaling that may enhance bone formation. {beta}-arrestins can also be modified through phosphorylation, which influences their movement and signaling. Researchers examined if phosphorylation of {beta}-arrestins affects their movement to the cell surface and early endosomes following PTH1R activation. Using specialized sensors and microscopic analysis, they measured the movement of {beta}-arrestins. They found that phosphorylation slightly alters plasma membrane movement, while it significantly reduces early endosome movement. Both mutations reduced endosome movement, but the phosphomimetic mutation had a greater effect. Restoring specific phosphorylation sites in {beta}-arrestin 1 or 2 restored more endosome movement compared to other mutations. Dephosphorylation is necessary for PTH1R-stimulated {beta}-arrestin movement to early endosomes, with different sites impacted compared to other GPCRs. These results suggest that {beta}-arrestins may be regulated differently by various stimuli, which could have implications for therapeutic targeting of {beta}-arrestin-dependent pathways.",
  "summary": "{beta}-arrestins 1 and 2 are intracellular adaptor proteins that regulate the subcellular localisation and signalling of GPCRs including Parathyroid Hormone Receptor 1 (PTH1R), which produces {beta}-arrestin-dependent signalling that may selectively stimulate bone anabolism. {beta}-arrestins can themselves be regulated by post-translational modifications including phosphorylation, which dictates…",
  "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."
}