ArticleResearch square2026
Phosphorylation site topology governs the functional dynamics of arrestin recruitment to GPCRs.
Article in Research square, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Authors and funding
12 authors.
Funding
Abstract
Desensitization and alternative signaling pathways of G protein-coupled receptors (GPCRs) are largely mediated by β-arrestins (arr). While most GPCRs recruit arrestin through phosphorylated C-terminal tails, many lack a canonical tail and instead rely on phosphorylation sites within long third intracellular loops (ICL3). Structural information on such complexes is largely missing, and the molecular details of arrestin engagement remain unknown. Here, we dissect the interaction between the muscarinic acetylcholine receptor M2 (M
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.