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A dynamic and screening-compatible nanoluciferase-based complementation assay enables profiling of individual GPCR-G protein interactions.
Laschet, Céline; Dupuis, Nadine; Hanson, Julien.
Afiliación
  • Laschet C; From the Laboratory of Molecular Pharmacology, GIGA-Molecular Biology of Diseases, University of Liège, 4000 Liège and.
  • Dupuis N; From the Laboratory of Molecular Pharmacology, GIGA-Molecular Biology of Diseases, University of Liège, 4000 Liège and.
  • Hanson J; From the Laboratory of Molecular Pharmacology, GIGA-Molecular Biology of Diseases, University of Liège, 4000 Liège and j.hanson@uliege.be.
J Biol Chem ; 294(11): 4079-4090, 2019 03 15.
Article en En | MEDLINE | ID: mdl-30593506
G protein-coupled receptors (GPCRs) are currently the target of more than 30% of the marketed medicines. However, there is an important medical need for ligands with improved pharmacological activities on validated drug targets. Moreover, most of these ligands remain poorly characterized, notably because of a lack of pharmacological tools. Thus, there is an important demand for innovative assays that can detect and drive the design of compounds with novel or improved pharmacological properties. In particular, a functional and screening-compatible GPCR-G protein interaction assay is still unavailable. Here, we report on a nanoluciferase-based complementation technique to detect ligands that promote a GPCR-G protein interaction. We demonstrate that our system can be used to profile compounds with regard to the G proteins they activate through a given GPCR. Furthermore, we established a proof of applicability of screening for distinct G proteins on dopamine receptor D2 whose differential coupling to Gαi/o family members has been extensively studied. In a D2-Gαi1versus D2-Gαo screening, we retrieved five agonists that are currently being used in antiparkinsonian medications. We determined that in this assay, piribedil and pergolide are full agonists for the recruitment of Gαi1 but are partial agonists for Gαo, that the agonist activity of ropinirole is biased in favor of Gαi1 recruitment, and that the agonist activity of apomorphine is biased for Gαo We propose that this newly developed assay could be used to develop molecules that selectively modulate a particular G protein pathway.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Receptores Acoplados a Proteínas G / Nanopartículas / Luciferasas Tipo de estudio: Diagnostic_studies / Screening_studies Límite: Humans Idioma: En Revista: J Biol Chem Año: 2019 Tipo del documento: Article Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Receptores Acoplados a Proteínas G / Nanopartículas / Luciferasas Tipo de estudio: Diagnostic_studies / Screening_studies Límite: Humans Idioma: En Revista: J Biol Chem Año: 2019 Tipo del documento: Article Pais de publicación: Estados Unidos