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Dopamine-induced arrestin recruitment and desensitization of the dopamine D4 receptor is regulated by G protein-coupled receptor kinase-2
Umeå universitet, Medicinska fakulteten, Institutionen för integrativ medicinsk biologi (IMB). Umeå universitet, Medicinska fakulteten, Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM).
Department of Neuroscience, Karolinska Institutet, Solna, Sweden.
Umeå universitet, Medicinska fakulteten, Institutionen för integrativ medicinsk biologi (IMB). Umeå universitet, Medicinska fakulteten, Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM).
Pharmacology Unit, Department of Pathology and Experimental Therapeutics, Faculty of Medicine and Health Sciences, Institute of Neurosciences, University of Barcelona, Barcelona, Spain; Neuropharmacology and Pain Group, Neuroscience Program, Institut d'Investigació Biomèdica de Bellvitge, IDIBELL, Barcelona, Spain.
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2023 (Engelska)Ingår i: Frontiers in Pharmacology, E-ISSN 1663-9812, Vol. 14, artikel-id 1087171Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

The dopamine D4 receptor (D4R) is expressed in the retina, prefrontal cortex, and autonomic nervous system and has been implicated in attention deficit hyperactivity disorder (ADHD), substance use disorders, and erectile dysfunction. D4R has also been investigated as a target for antipsychotics due to its high affinity for clozapine. As opposed to the closely related dopamine D2 receptor (D2R), dopamine-induced arrestin recruitment and desensitization at the D4R have not been studied in detail. Indeed, some earlier investigations could not detect arrestin recruitment and desensitization of this receptor upon its activation by agonist. Here, we used a novel nanoluciferase complementation assay to study dopamine-induced recruitment of β-arrestin2 (βarr2; also known as arrestin3) and G protein-coupled receptor kinase-2 (GRK2) to the D4R in HEK293T cells. We also studied desensitization of D4R-evoked G protein-coupled inward rectifier potassium (GIRK; also known as Kir3) current responses in Xenopus oocytes. Furthermore, the effect of coexpression of GRK2 on βarr2 recruitment and GIRK response desensitization was examined. The results suggest that coexpression of GRK2 enhanced the potency of dopamine to induce βarr2 recruitment to the D4R and accelerated the rate of desensitization of D4R-evoked GIRK responses. The present study reveals new details about the regulation of arrestin recruitment to the D4R and thus increases our understanding of the signaling and desensitization of this receptor.

Ort, förlag, år, upplaga, sidor
Frontiers Media S.A., 2023. Vol. 14, artikel-id 1087171
Nyckelord [en]
electrophysiology, G protein-coupled inwardly rectifying potassium channels, HEK 293 cells, luciferase, luminescence measurements, Xenopus laevis
Nationell ämneskategori
Farmakologi och toxikologi
Identifikatorer
URN: urn:nbn:se:umu:diva-205006DOI: 10.3389/fphar.2023.1087171ISI: 000989268800001Scopus ID: 2-s2.0-85147770245OAI: oai:DiVA.org:umu-205006DiVA, id: diva2:1740409
Forskningsfinansiär
Stiftelsen Lars Hiertas MinneÅhlén-stiftelsenMagnus Bergvalls StiftelseHjärnfonden, PS2022-0040Tillgänglig från: 2023-03-01 Skapad: 2023-03-01 Senast uppdaterad: 2025-05-19Bibliografiskt granskad
Ingår i avhandling
1. Signaling and regulation of dopamine D3 and D4 receptors
Öppna denna publikation i ny flik eller fönster >>Signaling and regulation of dopamine D3 and D4 receptors
2025 (Engelska)Doktorsavhandling, sammanläggning (Övrigt vetenskapligt)
Alternativ titel[sv]
Signalering och reglering av dopamin D3 och D4 receptorer
Abstract [en]

Dopamine based signaling makes up a small percentage of overall neuronal communication, but its regulation makes up a significant portion of CNS pharmacology. Dopamine is known to activate G protein-coupled receptors, which have been a drug target since at least the first modern antipsychotic (Chlorpromazine), although this was not clear at the time. Dopamine primarily binds a family of G protein-coupled receptors called the dopamine receptors. Dopamine receptors are either D1 or D2 -like, the significant difference being whether they bind and activate cyclic AMP production activating (D1-like) or inhibiting (D2-like) alpha subunits of G protein-coupled receptors. The D2-like receptors are the main targets of most antipsychotic and many anti-parkinsonian medicines currently in clinical use. 

We have investigated the downstream signaling of D2-like dopamine receptors D3 and D4. Specifically, we have used a nanoluciferase assay to measure G protein-coupled receptor interactions with intracellular proteins, primarily beta-arrestin2 (βarr2), G protein-coupled receptor kinase 2 (GRK2) and alpha subunits of G protein-coupled receptors. Included papers report on several intricacies of signaling downstream the D3 and D4 receptors. D4 receptor recruitment of GRK2 is dopamine dependent, transient and potentiates βarr2 recruitment. In addition, βarr2 desensitizes the response of G protein-coupled inward rectifier potassium (GIRK, also known as Kir3) channels to dopamine at the D4, this desensitization is similarly potentiated by GRK2 coexpression. This contrasts with the D3 receptor, where no dopamine-dependent GRK2 interaction could be detected. In time-resolved experiments, we found that the D3-selective agonist FAUC73 disassociates significantly faster from the D3 receptor than dopamine. We also investigated the common S9/G9 isoforms of the D3 receptor, with no significant difference found in either G protein, βarr2, or GRK2 recruitment, nor in downstream cAMP accumulation.

Additionally, we attempted to find D3 receptor mutants which only interact with Gαo subunits while not interacting with βarr2, and vice versa. The ultimate goal was to create mice with the corresponding D3 mutations, to allow for in vivo investigation of the behavioral consequences of the respective signaling pathways downstream of the D3 receptor. In this we have been partially successful with the discovery of the A131W point mutation, which seemingly renders the D3 receptor unable to signal though inhibitory G proteins while retaining βarr2 activity.

In preliminary experiments, c57BL/6 mice carrying the A131W point mutation have been tested using open field and prepulse inhibition paradigms. The goal of testing has been to compare the effects with wildtype and D3 knockout animals to pinpoint the pathways though which therapeutic drugs known to act via the D3 receptor, such as cariprazine, function downstream of the D3 receptor and to validate the efficacy of our model.

In conclusion, we set out to increase our understanding of how signaling downstream D3 and D4 receptors function. Beyond the basic science interest, we believe this knowledge might contribute to the development of novel therapies, as well as improving existing treatments acting via dopamine D2-like receptors, such as antipsychotics and antiparkinsonian drugs. Current receptor-level knowledge has allowed us to narrow the search for therapeutic targets, but continued progress will require research into the downstream signaling cascades. To facilitate this investigation, new tools need to be developed. Here, have adapted a nanoluciferase assay for use with D3 and D4 receptors to investigate protein-protein interactions between the receptors and GKR2, βarr2, and G protein Gα subunits (Gαo in particular). Using this method, we have identified a D3 receptor point mutation which disables G protein Gαo signaling while retaining βarr2 activity in vitro. Finally, we have created mutant c57BL/6 mice carrying this mutation and begun behavioral testing for comparison with wildtype (WT) and D3 knockout mice.

Ort, förlag, år, upplaga, sidor
Umeå: Umeå University, 2025. s. 67
Serie
Umeå University medical dissertations, ISSN 0346-6612 ; 2364
Nyckelord
GPCR, neurofarmakologi, biased signaling, punktmutationer
Nationell ämneskategori
Farmakologi och toxikologi Molekylärbiologi
Forskningsämne
molekylärbiologi
Identifikatorer
urn:nbn:se:umu:diva-239002 (URN)978-91-8070-726-8 (ISBN)978-91-8070-727-5 (ISBN)
Disputation
2025-06-13, KBE303, Stora Hörsalen, KBC-huset, Umeå, 13:00 (Engelska)
Opponent
Handledare
Forskningsfinansiär
Knut och Alice Wallenbergs StiftelseKempestiftelserna
Tillgänglig från: 2025-05-23 Skapad: 2025-05-19 Senast uppdaterad: 2026-06-13Bibliografiskt granskad

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Burström, ViktorBetari, NibalGarro-Martínez, EmilioSahlholm, Kristoffer

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