ArticleCommunications biology2026
Distinct membrane binding properties of the two non-visual arrestins.
Article in Communications biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Arrestins as programmable integrators of GPCR signaling: structural microstates, spatiotemporal logic, and therapeutic control.Cell discovery · 2026Review
- Precise Alternation Between Image-Forming Sample Planes Enables Quantitative Monitoring of Receptor-Arrestin Interaction Dynamics at the Plasma Membrane of Live Cells.bioRxiv : the preprint server for biology · 2026Article
- Cooperative Control of Arrestin Activation By Membrane Lipids And Phosphorylation Barcodes.bioRxiv : the preprint server for biology · 2026Article
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Authors and funding
12 authors.
Funding
Abstract
Membrane interactions play a crucial role in regulating arrestin activation and its binding to phosphorylated G protein-coupled receptors (GPCRs). Here, we combine in vitro biophysical approaches with cell-based fluorescence intensity fluctuation analysis to systematically compare the membrane-binding properties of the two highly conserved non-visual arrestin subtypes, arrestin-2 and arrestin-3. We find that in the absence of stimulation, arrestin-2 primarily engages PI(4,5)P
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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 OpenQuestion graph.