Signaling by dopamine regulates D2 receptors trafficking at the membrane

التفاصيل البيبلوغرافية
العنوان: Signaling by dopamine regulates D2 receptors trafficking at the membrane
المؤلفون: Robert Edwards, Mustafa Oulad-Abdelghani, Monica Lombardi, Tarek A. Samad, Roberto Picetti, Emanuele Tirotta, Emiliana Borrelli, Valerie Fontaine
المساهمون: University of California [Irvine] (UCI), University of California, Institut de génétique et biologie moléculaire et cellulaire (IGBMC), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Louis Pasteur - Strasbourg I, University of California [Irvine] (UC Irvine), University of California (UC), Université Louis Pasteur - Strasbourg I-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Peney, Maité
المصدر: Cell Cycle
Cell Cycle, Taylor & Francis, 2008, 7 (14), pp.2241-8
Scopus-Elsevier
Cell Cycle, 2008, 7 (14), pp.2241-8
سنة النشر: 2008
مصطلحات موضوعية: MESH: Signal Transduction, Dopamine, MESH: Neurons, MESH: Protein Structure, Secondary, MESH: Protein Isoforms, Protein Structure, Secondary, MESH: Cell Compartmentation, Mice, 0302 clinical medicine, MESH: Receptors, Dopamine D2, Chlorocebus aethiops, Protein Isoforms, MESH: Animals, Receptor, Neurons, 0303 health sciences, Cell biology, MESH: COS Cells, Protein Transport, D2-like receptor, COS Cells, Signal transduction, Intracellular, Protein Binding, Signal Transduction, MESH: Protein Transport, G protein, D1-like receptor, MESH: Dopamine, Biology, Transfection, 03 medical and health sciences, Dopamine receptor D2, MESH: Protein Binding, Animals, Molecular Biology, MESH: Mice, 030304 developmental biology, G protein-coupled receptor, Receptors, Dopamine D2, MESH: Transfection, Cell Membrane, Cell Biology, [SDV.ETH] Life Sciences [q-bio]/Ethics, MESH: Cercopithecus aethiops, MESH: GTP-Binding Protein alpha Subunit, Gi2, [SDV.ETH]Life Sciences [q-bio]/Ethics, Cell Compartmentation, Neostriatum, MESH: Neostriatum, GTP-Binding Protein alpha Subunit, Gi2, 030217 neurology & neurosurgery, Developmental Biology, MESH: Cell Membrane
الوصف: International audience; sGi2 is a spliced variant of the GTP-binding protein G(alpha i2). By difference with G(alpha i2), which is mainly present at the plasma membrane, sGi2 is localized in intracellular compartments. The splicing event generates a novel C-terminal region in sGi2, which is necessary for its intracellular localization. The role of sGi2 is presently unknown, although its intracellular localization might underlie a possible role in the regulation of trafficking of 7TM receptors. Here, we show that sGi2 complexes with dopamine D2 receptors (D2R) in striatal neurons. The sGi2-D2R complex is readily observed in immunoprecipitation studies using specific antibodies for both proteins on mouse striatal extracts, which identify D2-specific bands of >80 KDa suggesting sGi2 interactions with D2R dimers. Importantly, the sGi2-D2R complex in the absence of receptor stimulation is mostly found in intracellular perinuclear areas in primary neuronal cultures. Treatment of neurons with quinpirole, a D2-specific agonist, results into diffusion of D2R and sGi2 staining throughout the cell and into neurites and membranes. This suggests that dopamine could regulate availability of D2 receptors at the cell surface. The formation of sGi2-D2R complex is mediated through the interaction of sGi2 with the third intracellular loop of D2Rs. As functional consequence of the D2R-sGi2 interaction, we observed a reduction of D2 binding sites at the plasma membrane, when the two proteins are co-expressed in transfected cells. Altogether these studies identify sGi2 as a D2R interacting protein involved in the regulation of D2R at the membrane through a dopamine mediated mechanism.
تدمد: 1551-4005
1538-4101
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9781923f0876ba4d09435e00cf220bf4
https://pubmed.ncbi.nlm.nih.gov/18635969
حقوق: OPEN
رقم الأكسشن: edsair.doi.dedup.....9781923f0876ba4d09435e00cf220bf4
قاعدة البيانات: OpenAIRE