ArticleNature nanotechnology2017
A synthetic intrabody-based selective and generic inhibitor of GPCR endocytosis.
Article in Nature nanotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
25 citing papers in PubMed, 46 citations in OpenAlex.
- Conformation-specific synthetic intrabodies modulate mTOR signaling with subcellular spatial resolution.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Principles and Design of Molecular Tools for Sensing and Perturbing Cell Surface Receptor Activity.Chemical reviews · 2025Review
- Review
- Structural snapshots uncover a key phosphorylation motif in GPCRs driving β-arrestin activation.Molecular cell · 2023Article
- Article
- Overcoming the On-Target Toxicity in Antibody-Mediated Therapies via an Indirect Active Targeting Strategy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Allosteric modulation of GPCR-induced β-arrestin trafficking and signaling by a synthetic intrabody.Nature communications · 2022Article
- Intracellular VHHs to monitor and modulate GPCR signaling.Frontiers in endocrinology · 2022Review
- Biphasic activation of β-arrestin 1 upon interaction with a GPCR revealed by methyl-TROSY NMR.Nature communications · 2021Article
- Intrinsic bias at non-canonical, β-arrestin-coupled seven transmembrane receptors.Molecular cell · 2021Article
- Discovery of a dual Ras and ARF6 inhibitor from a GPCR endocytosis screen.Nature communications · 2021Article
- The Role of β-Arrestins in Regulating Stem Cell Phenotypes in Normal and Tumorigenic Cells.International journal of molecular sciences · 2020Review
- Key phosphorylation sites in GPCRs orchestrate the contribution of β-Arrestin 1 in ERK1/2 activation.EMBO reports · 2020Article
- Genetically encoded intrabody sensors report the interaction and trafficking of β-arrestin 1 upon activation of G-protein-coupled receptors.The Journal of biological chemistry · 2020Article
- Purification of native CCL7 and its functional interaction with selected chemokine receptors.Protein expression and purification · 2020Article
- βAnnual review of pharmacology and toxicology · 2020Review
- Structure and function of β-arrestins, their emerging role in breast cancer, and potential opportunities for therapeutic manipulation.Advances in cancer research · 2020Article
- Site-directed labeling of β-arrestin with monobromobimane for measuring their interaction with G protein-coupled receptors.Methods in enzymology · 2020Article
- Reversible biotinylation of purified proteins for measuring protein-protein interactions.Methods in enzymology · 2020Article
- Why recombinant antibodies - benefits and applications.Current opinion in biotechnology · 2019Review
Corrections and comments
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Authors and funding
13 authors at 5 institutions in 3 countries.
Funding
Abstract
Beta-arrestins (βarrs) critically mediate desensitization, endocytosis and signalling of G protein-coupled receptors (GPCRs), and they scaffold a large number of interaction partners. However, allosteric modulation of their scaffolding abilities and direct targeting of their interaction interfaces to modulate GPCR functions selectively have not been fully explored yet. Here we identified a series of synthetic antibody fragments (Fabs) against different conformations of βarrs from phage display libraries. Several of these Fabs allosterically and selectively modulated the interaction of βarrs with clathrin and ERK MAP kinase. Interestingly, one of these Fabs selectively disrupted βarr-clathrin interaction, and when expressed as an intrabody, it robustly inhibited agonist-induced endocytosis of a broad set of GPCRs without affecting ERK MAP kinase activation. Our data therefore demonstrate the feasibility of selectively targeting βarr interactions using intrabodies and provide a novel framework for fine-tuning GPCR functions with potential therapeutic implications.
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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.