ArticlePharmacology research & perspectives2019
Using the novel HiBiT tag to label cell surface relaxin receptors for BRET proximity analysis.
Article in Pharmacology research & perspectives, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- Membrane-Traversing Peptides: Mechanistic Landscapes, Assays, and Applications.Chemical reviews · 2026Review
- Sweet and Bright: Illuminating Glycoprotein-Mediated Endocytosis via Metabolic Labeling and NanoLuciferase.ACS chemical biology · 2026Article
- Lack of evidence for cargo release of CD63-EVs into recipient cells.Scientific reports · 2026Article
- Amylin receptor subunit interactions are modulated by agonists and determine signaling.Science signaling · 2025Article
- A flexible, high-throughput system for studying live mRNA translation with HiBiT technology.Nucleic acids research · 2025Article
- Oligomerization of the heteromeric γ-aminobutyric acid receptor GABAScientific reports · 2022Article
- Orthogonal Peptide-Templated Labeling Elucidates Lateral ETChembiochem : a European journal of chemical biology · 2022Article
- NanoBRET and NanoBiT/BRET-Based Ligand Binding Assays Permit Quantitative Assessment of Small Molecule Ligand Binding to Smoothened.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Strategies for Site-Specific Labeling of Receptor Proteins on the Surfaces of Living Cells by Using Genetically Encoded Peptide Tags.Chembiochem : a European journal of chemical biology · 2021Review
- Coelenterazine-Dependent Luciferases as a Powerful Analytical Tool for Research and Biomedical Applications.International journal of molecular sciences · 2020Review
- The luminescent HiBiT peptide enables selective quantitation of G protein-coupled receptor ligand engagement and internalization in living cells.The Journal of biological chemistry · 2020Article
- Using the novel HiBiT tag to label cell surface relaxin receptors for BRET proximity analysis.Pharmacology research & perspectives · 2019Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Relaxin family peptide 1 (RXFP1) is the receptor for relaxin a peptide hormone with important therapeutic potential. Like many G protein-coupled receptors (GPCRs), RXFP1 has been reported to form homodimers. Given the complex activation mechanism of RXFP1 by relaxin, we wondered whether homodimerization may be explicitly required for receptor activation, and therefore sought to determine if there is any relaxin-dependent change in RXFP1 proximity at the cell surface. Bioluminescence resonance energy transfer (BRET) between recombinantly tagged receptors is often used in GPCR proximity studies. RXFP1 targets poorly to the cell surface when overexpressed in cell lines, with the majority of the receptor proteins sequestered within the cell. Thus, any relaxin-induced changes in RXFP1 proximity at the cell surface may be obscured by BRET signal originating from intracellular compartments. We therefore, utilized the newly developed split luciferase system called HiBiT to specifically label the extracellular terminus of cell surface RXFP1 receptors in combination with mCitrine-tagged receptors, using the GABA
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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.