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Journal articles on the topic 'Receptor heteromerization'

Author: Grafiati

Published: 4 June 2021

Last updated: 2 February 2022

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1

Albee, Lauren J., Xianlong Gao, and Matthias Majetschak. "Plasticity of seven-transmembrane-helix receptor heteromers in human vascular smooth muscle cells." PLOS ONE 16, no. 6 (June 24, 2021): e0253821. http://dx.doi.org/10.1371/journal.pone.0253821.

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Recently, we reported that the chemokine (C-X-C motif) receptor 4 (CXCR4) and atypical chemokine receptor 3 (ACKR3) heteromerize with α1A/B/D-adrenoceptors (ARs) and arginine vasopressin receptor 1A (AVPR1A) in recombinant systems and in rodent and human vascular smooth muscle cells (hVSMCs). In these studies, we observed that heteromerization between two receptor partners may depend on the presence and the expression levels of other partnering receptors. To test this hypothesis and to gain initial insight into the formation of these receptor heteromers in native cells, we utilized proximity ligation assays in hVSMCs to visualize receptor-receptor proximity and systematically studied how manipulation of the expression levels of individual protomers affect heteromerization patterns among other interacting receptor partners. We confirmed subtype-specific heteromerization between endogenously expressed α1A/B/D-ARs and detected that AVPR1A also heteromerizes with α1A/B/D-ARs. siRNA knockdown of CXCR4 and of ACKR3 resulted in a significant re-arrangement of the heteromerization patterns among α1-AR subtypes. Similarly, siRNA knockdown of AVPR1A significantly increased heteromerization signals for seven of the ten receptor pairs between CXCR4, ACKR3, and α1A/B/D-ARs. Our findings suggest plasticity of seven transmembrane helix (7TM) receptor heteromerization in native cells and could be explained by a supramolecular organization of these receptors within dynamic clusters in the plasma membrane. Because we previously observed that recombinant CXCR4, ACKR3, α1a-AR and AVPR1A form hetero-oligomeric complexes composed of 2–4 different protomers, which show signaling properties distinct from individual protomers, re-arrangements of receptor heteromerization patterns in native cells may contribute to the phenomenon of context-dependent GPCR signaling. Furthermore, these findings advise caution in the interpretation of functional consequences after 7TM receptor knockdown in experimental models. Alterations of the heteromerization patterns among other receptor partners may alter physiological and pathological responses, in particular in more complex systems, such as studies on the function of isolated organs or in in vivo experiments.

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2

Johnstone, Elizabeth K. M., Heng B. See, Rekhati S. Abhayawardana, Angela Song, K. Johan Rosengren, Stephen J. Hill, and Kevin D. G. Pfleger. "Investigation of Receptor Heteromers Using NanoBRET Ligand Binding." International Journal of Molecular Sciences 22, no. 3 (January 22, 2021): 1082. http://dx.doi.org/10.3390/ijms22031082.

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Receptor heteromerization is the formation of a complex involving at least two different receptors with pharmacology that is distinct from that exhibited by its constituent receptor units. Detection of these complexes and monitoring their pharmacology is crucial for understanding how receptors function. The Receptor-Heteromer Investigation Technology (Receptor-HIT) utilizes ligand-dependent modulation of interactions between receptors and specific biomolecules for the detection and profiling of heteromer complexes. Previously, the interacting biomolecules used in Receptor-HIT assays have been intracellular proteins, however in this study we have for the first time used bioluminescence resonance energy transfer (BRET) with fluorescently-labeled ligands to investigate heteromerization of receptors on the cell surface. Using the Receptor-HIT ligand binding assay with NanoBRET, we have successfully investigated heteromers between the angiotensin II type 1 (AT1) receptor and the β2 adrenergic receptor (AT1-β2AR heteromer), as well as between the AT1 and angiotensin II type 2 receptor (AT1-AT2 heteromer).

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3

Rozenfeld, Raphael, and Lakshmi A. Devi. "Receptor heteromerization and drug discovery." Trends in Pharmacological Sciences 31, no. 3 (March 2010): 124–30. http://dx.doi.org/10.1016/j.tips.2009.11.008.

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4

Pelassa, Simone, Diego Guidolin, Arianna Venturini, Monica Averna, Giulia Frumento, Letizia Campanini, Rosa Bernardi, et al. "A2A-D2 Heteromers on Striatal Astrocytes: Biochemical and Biophysical Evidence." International Journal of Molecular Sciences 20, no. 10 (May 17, 2019): 2457. http://dx.doi.org/10.3390/ijms20102457.

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Our previous findings indicate that A2A and D2 receptors are co-expressed on adult rat striatal astrocytes and on the astrocyte processes, and that A2A-D2 receptor–receptor interaction can control the release of glutamate from the processes. Functional evidence suggests that the receptor–receptor interaction was based on heteromerization of native A2A and D2 receptors at the plasma membrane of striatal astrocyte processes. We here provide biochemical and biophysical evidence confirming that receptor–receptor interaction between A2A and D2 receptors at the astrocyte plasma membrane is based on A2A-D2 heteromerization. To our knowledge, this is the first direct demonstration of the ability of native A2A and D2 receptors to heteromerize on glial cells. As striatal astrocytes are recognized to be involved in Parkinson’s pathophysiology, the findings that adenosine A2A and dopamine D2 receptors can form A2A-D2 heteromers on the astrocytes in the striatum (and that these heteromers can play roles in the control of the striatal glutamatergic transmission) may shed light on the molecular mechanisms involved in the pathogenesis of the disease.

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5

Woods, Amina S., Francisco Ciruela, Kjell Fuxe, Luigi F. Agnati, Carmen Lluis, Rafael Franco, and Sergi Ferré. "Role of Electrostatic Interaction in Receptor–Receptor Heteromerization." Journal of Molecular Neuroscience 26, no. 2-3 (2005): 125–32. http://dx.doi.org/10.1385/jmn:26:2-3:125.

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6

Canals, Meritxell, Daniel Marcellino, Francesca Fanelli, Francisco Ciruela, Piero de Benedetti, Steven R. Goldberg, Kim Neve, et al. "Adenosine A2A-Dopamine D2Receptor-Receptor Heteromerization." Journal of Biological Chemistry 278, no. 47 (August 21, 2003): 46741–49. http://dx.doi.org/10.1074/jbc.m306451200.

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7

Bono, Federica, Veronica Mutti, Chiara Fiorentini, and Cristina Missale. "Dopamine D3 Receptor Heteromerization: Implications for Neuroplasticity and Neuroprotection." Biomolecules 10, no. 7 (July 9, 2020): 1016. http://dx.doi.org/10.3390/biom10071016.

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The dopamine (DA) D3 receptor (D3R) plays a pivotal role in the control of several functions, including motor activity, rewarding and motivating behavior and several aspects of cognitive functions. Recently, it has been reported that the D3R is also involved in the regulation of neuronal development, in promoting structural plasticity and in triggering key intracellular events with neuroprotective potential. A new role for D3R-dependent neurotransmission has thus been proposed both in preserving DA neuron homeostasis in physiological conditions and in preventing pathological alterations that may lead to neurodegeneration. Interestingly, there is evidence that nicotinic acetylcholine receptors (nAChR) located on DA neurons also provide neurotrophic support to DA neurons, an effect requiring functional D3R and suggesting the existence of a positive cross-talk between these receptor systems. Increasing evidence suggests that, as with the majority of G protein-coupled receptors (GPCR), the D3R directly interacts with other receptors to form new receptor heteromers with unique functional and pharmacological properties. Among them, we recently identified a receptor heteromer containing the nAChR and the D3R as the molecular effector of nicotine-mediated neurotrophic effects. This review summarizes the functional and pharmacological characteristics of D3R, including the capability to form active heteromers as pharmacological targets for specific neurodegenerative disorders. In particular, the molecular and functional features of the D3R-nAChR heteromer will be especially discussed since it may represent a possible key etiologic effector for DA-related pathologies, such as Parkinson’s disease (PD), and a target for drug design.

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8

Rozenfeld, Raphael, and Lakshmi A. Devi. "Exploring a role for heteromerization in GPCR signalling specificity." Biochemical Journal 433, no. 1 (December 15, 2010): 11–18. http://dx.doi.org/10.1042/bj20100458.

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The critical involvement of GPCRs (G-protein-coupled receptors) in nearly all physiological processes, and the presence of these receptors at the interface between the extracellular and the intracellular milieu, has positioned these receptors as pivotal therapeutic targets. Although a large number of drugs targeting GPCRs are currently available, significant efforts have been directed towards understanding receptor properties, with the goal of identifying and designing improved receptor ligands. Recent advances in GPCR pharmacology have demonstrated that different ligands binding to the same receptor can activate discrete sets of downstream effectors, a phenomenon known as ‘ligand-directed signal specificity’, which is currently being explored for drug development due to its potential therapeutic advantage. Emerging studies suggest that GPCR responses can also be modulated by contextual factors, such as interactions with other GPCRs. Association between different GPCR types leads to the formation of complexes, or GPCR heteromers, with distinct and unique signalling properties. Some of these heteromers activate discrete sets of signalling effectors upon activation by the same ligand, a phenomenon termed ‘heteromer-directed signalling specificity’. This has been shown to be involved in the physiological role of receptors and, in some cases, in disease-specific dysregulation of a receptor effect. Hence targeting GPCR heteromers constitutes an emerging strategy to select receptor-specific responses and is likely to be useful in achieving specific beneficial therapeutic effects.

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Toneatti, Rudy, Jong M. Shin, Urjita H. Shah, Carl R. Mayer, Justin M. Saunders, Miguel Fribourg, Paul T. Arsenovic, et al. "Interclass GPCR heteromerization affects localization and trafficking." Science Signaling 13, no. 654 (October 20, 2020): eaaw3122. http://dx.doi.org/10.1126/scisignal.aaw3122.

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Membrane trafficking processes regulate G protein–coupled receptor (GPCR) activity. Although class A GPCRs are capable of activating G proteins in a monomeric form, they can also potentially assemble into functional GPCR heteromers. Here, we showed that the class A serotonin 5-HT2A receptors (5-HT2ARs) affected the localization and trafficking of class C metabotropic glutamate receptor 2 (mGluR2) through a mechanism that required their assembly as heteromers in mammalian cells. In the absence of agonists, 5-HT2AR was primarily localized within intracellular compartments, and coexpression of 5-HT2AR with mGluR2 increased the intracellular distribution of the otherwise plasma membrane–localized mGluR2. Agonists for either 5-HT2AR or mGluR2 differentially affected trafficking through Rab5-positive endosomes in cells expressing each component of the 5-HT2AR–mGluR2 heterocomplex alone, or together. In addition, overnight pharmacological 5-HT2AR blockade with clozapine, but not with M100907, decreased mGluR2 density through a mechanism that involved heteromerization between 5-HT2AR and mGluR2. Using TAT-tagged peptides and chimeric constructs that are unable to form the interclass 5-HT2AR–mGluR2 complex, we demonstrated that heteromerization was necessary for the 5-HT2AR–dependent effects on mGluR2 subcellular distribution. The expression of 5-HT2AR also augmented intracellular localization of mGluR2 in mouse frontal cortex pyramidal neurons. Together, our data suggest that GPCR heteromerization may itself represent a mechanism of receptor trafficking and sorting.

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10

Zrein, Adel, Amina M. Bagher, Alexander P. Young, Eileen M. Denovan-Wright, and Melanie E. M. Kelly. "Endothelin receptor heteromerization inhibits β-arrestin function in HEK293 cells." Canadian Journal of Physiology and Pharmacology 98, no. 8 (August 2020): 531–40. http://dx.doi.org/10.1139/cjpp-2019-0620.

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The endothelin receptor A (ETA) and endothelin receptor B (ETB) are G protein-coupled receptors that are co-expressed in vascular smooth muscle cells. Endothelin-1 (ET-1) activates endothelin receptors to cause microvascular vasoconstriction. Previous studies have shown that heteromerization between ETA and ETB prolongs Ca2+ transients, leading to prolongation of Gαq-dependent signaling and sustained vasoconstriction. We hypothesized that these effects are in part mediated by the resistance of ETA/ETB heteromers to β-arrestin recruitment and subsequent desensitization. Using bioluminescence resonance energy transfer 2 (BRET2), we found that ETB has a relatively equal affinity to form either homomers or heteromers with ETA when co-expressed in the human embryonic kidney 293 (HEK293) cells. When co-expressed, activation of ETA and ETB by ET-1 caused a heteromer-specific reduction and delay in β-arrestin-2 recruitment with a corresponding reduction and delay in ET-1-induced ETA/ETB co-internalization. Furthermore, the co-expression of ETA and ETB inhibited ET-1-induced β-arrestin-1-dependent extracellular signal-regulated kinase (ERK) phosphorylation while prolonging ET-1-induced Gαq-dependent ERK phosphorylation. ETA/ETB heteromerization mediates the long-lasting vasoconstrictor response to ET-1 by the prolongation of Gαq-dependent signaling and inhibition of β-arrestin function.

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11

Borroto-Escuela, Dasiel O., Kathleen Van Craenenbroeck, Wilber Romero-Fernandez, Diego Guidolin, Amina S. Woods, Alicia Rivera, Guy Haegeman, Luigi F. Agnati, Alexander O. Tarakanov, and Kjell Fuxe. "Dopamine D2 and D4 receptor heteromerization and its allosteric receptor–receptor interactions." Biochemical and Biophysical Research Communications 404, no. 4 (January 2011): 928–34. http://dx.doi.org/10.1016/j.bbrc.2010.12.083.

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12

Massotte, D. "In vivoopioid receptor heteromerization: where do we stand?" British Journal of Pharmacology 172, no. 2 (July 1, 2014): 420–34. http://dx.doi.org/10.1111/bph.12702.

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13

Damian, Marjorie, Véronique Pons, Pedro Renault, Céline M’Kadmi, Bartholomé Delort, Lucie Hartmann, Ali I. Kaya, et al. "GHSR-D2R heteromerization modulates dopamine signaling through an effect on G protein conformation." Proceedings of the National Academy of Sciences 115, no. 17 (April 9, 2018): 4501–6. http://dx.doi.org/10.1073/pnas.1712725115.

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The growth hormone secretagogue receptor (GHSR) and dopamine receptor (D2R) have been shown to oligomerize in hypothalamic neurons with a significant effect on dopamine signaling, but the molecular processes underlying this effect are still obscure. We used here the purified GHSR and D2R to establish that these two receptors assemble in a lipid environment as a tetrameric complex composed of two each of the receptors. This complex further recruits G proteins to give rise to an assembly with only two G protein trimers bound to a receptor tetramer. We further demonstrate that receptor heteromerization directly impacts on dopamine-mediated Gi protein activation by modulating the conformation of its α-subunit. Indeed, association to the purified GHSR:D2R heteromer triggers a different active conformation of Gαi that is linked to a higher rate of GTP binding and a faster dissociation from the heteromeric receptor. This is an additional mechanism to expand the repertoire of GPCR signaling modulation that could have implications for the control of dopamine signaling in normal and physiopathological conditions.

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14

Franco, Nuria, and Rafael Franco. "Understanding the Added Value of G-Protein-Coupled Receptor Heteromers." Scientifica 2014 (2014): 1–7. http://dx.doi.org/10.1155/2014/362937.

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G-protein-coupled receptors (GPCRs) constitute the most populated family of proteins within the human genome. Since the early sixties work on GPCRs and on GPCR-mediated signaling has led to a number of awards, the most recent being the Nobel Prize in Chemistry for 2012. The future of GPCRs research is surely based on their capacity for heteromerization. Receptor heteromers offer a series of challenges that will help in providing success in academic/basic research and translation into more effective and safer drugs.

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Fuxe, Kjell, and Dasiel O. Borroto-Escuela. "Understanding receptor heteromerization and its allosteric integration of signals." Neuropharmacology 152 (July 2019): 1–3. http://dx.doi.org/10.1016/j.neuropharm.2019.05.001.

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16

Franco, R. "Evidence for Adenosine/Dopamine Receptor Interactions Indications for Heteromerization." Neuropsychopharmacology 23, no. 4 (October 2000): S50—S59. http://dx.doi.org/10.1016/s0893-133x(00)00144-5.

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17

Gaitonde, Supriya A., and Javier González-Maeso. "Contribution of heteromerization to G protein-coupled receptor function." Current Opinion in Pharmacology 32 (February 2017): 23–31. http://dx.doi.org/10.1016/j.coph.2016.10.006.

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18

Trang, Mira, Günther Schmalzing, Christa E. Müller, and Fritz Markwardt. "Dissection of P2X4 and P2X7 Receptor Current Components in BV-2 Microglia." International Journal of Molecular Sciences 21, no. 22 (November 11, 2020): 8489. http://dx.doi.org/10.3390/ijms21228489.

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Microglia cells represent the immune system of the central nervous system. They become activated by ATP released from damaged and inflamed tissue via purinergic receptors. Ionotropic purinergic P2X4 and P2X7 receptors have been shown to be involved in neurological inflammation and pain sensation. Whether the two receptors assemble exclusively as homotrimers or also as heterotrimers is still a matter of debate. We investigated the expression of P2X receptors in BV-2 microglia cells applying the whole-cell voltage-clamp technique. We dissected P2X4 and P2X7 receptor-mediated current components by using specific P2X4 and P2X7 receptor blockers and by their characteristic current kinetics. We found that P2X4 and P2X7 receptors are activated independently from each other, indicating that P2X4/P2X7 heteromers are not of functional significance in these cells. The pro-inflammatory mediators lipopolysaccharide and interferon γ, if applied in combination, upregulated P2X4, but not P2X7 receptor-dependent current components also arguing against phenotypically relevant heteromerization of P2X4 and P2X7 receptor subunits.

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19

Ang, Zhiwei, Ding Xiong, Min Wu, and Jeak Ling Ding. "FFAR2‐FFAR3 receptor heteromerization modulates short‐chain fatty acid sensing." FASEB Journal 32, no. 1 (September 7, 2017): 289–303. http://dx.doi.org/10.1096/fj.201700252rr.

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Bacart, Johan, Audrey Leloire, Angélique Levoye, Philippe Froguel, Ralf Jockers, and Cyril Couturier. "Evidence for leptin receptor isoforms heteromerization at the cell surface." FEBS Letters 584, no. 11 (March 27, 2010): 2213–17. http://dx.doi.org/10.1016/j.febslet.2010.03.033.

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21

Gao, Xianlong, You-Hong Cheng, Garrett A. Enten, Anthony J. DeSantis, Vadim Gaponenko, and Matthias Majetschak. "Regulation of the thrombin/protease-activated receptor 1 axis by chemokine (CXC motif) receptor 4." Journal of Biological Chemistry 295, no. 44 (August 24, 2020): 14893–905. http://dx.doi.org/10.1074/jbc.ra120.015355.

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The chemokine receptor CXCR4, a G protein–coupled receptor (GPCR) capable of heteromerizing with other GPCRs, is involved in many processes, including immune responses, hematopoiesis, and organogenesis. Evidence suggests that CXCR4 activation reduces thrombin/protease-activated receptor 1 (PAR1)-induced impairment of endothelial barrier function. However, the mechanisms underlying cross-talk between CXCR4 and PAR1 are not well-understood. Using intermolecular bioluminescence resonance energy transfer and proximity ligation assays, we found that CXCR4 heteromerizes with PAR1 in the HEK293T expression system and in human primary pulmonary endothelial cells (hPPECs). A peptide analog of transmembrane domain 2 (TM2) of CXCR4 interfered with PAR1:CXCR4 heteromerization. In HTLA cells, the presence of CXCR4 reduced the efficacy of thrombin to induce β-arrestin-2 recruitment to recombinant PAR1 and enhanced thrombin-induced Ca2+ mobilization. Whereas thrombin-induced extracellular signal-regulated protein kinase 1/2 (ERK1/2) phosphorylation occurred more transiently in the presence of CXCR4, peak ERK1/2 phosphorylation was increased when compared with HTLA cells expressing PAR1 alone. CXCR4-associated effects on thrombin-induced β-arrestin-2 recruitment to and signaling of PAR1 could be reversed by TM2. In hPPECs, TM2 inhibited thrombin-induced ERK1/2 phosphorylation and activation of Ras homolog gene family member A. CXCR4 siRNA knockdown inhibited thrombin-induced ERK1/2 phosphorylation. Whereas thrombin stimulation reduced surface expression of PAR1, CXCR4, and PAR1:CXCR4 heteromers, chemokine (CXC motif) ligand 12 stimulation reduced surface expression of CXCR4 and PAR1:CXCR4 heteromers, but not of PAR1. Finally, TM2 dose-dependently inhibited thrombin-induced impairment of hPPEC monolayer permeability. Our findings suggest that CXCR4:PAR1 heteromerization enhances thrombin-induced G protein signaling of PAR1 and PAR1-mediated endothelial barrier disruption.

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22

Derouiche, Lyes, Florian Pierre, Stéphane Doridot, Stéphane Ory, and Dominique Massotte. "Heteromerization of Endogenous Mu and Delta Opioid Receptors Induces Ligand-Selective Co-Targeting to Lysosomes." Molecules 25, no. 19 (September 30, 2020): 4493. http://dx.doi.org/10.3390/molecules25194493.

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Increasing evidence indicates that native mu and delta opioid receptors can associate to form heteromers in discrete brain neuronal circuits. However, little is known about their signaling and trafficking. Using double-fluorescent knock-in mice, we investigated the impact of neuronal co-expression on the internalization profile of mu and delta opioid receptors in primary hippocampal cultures. We established ligand selective mu–delta co-internalization upon activation by 1-[[4-(acetylamino)phenyl]methyl]-4-(2-phenylethyl)-4-piperidinecarboxylic acid, ethyl ester (CYM51010), [d-Ala2, NMe-Phe4, Gly-ol5]enkephalin (DAMGO), and deltorphin II, but not (+)-4-[(αR)-α-((2S,5R)-4-Allyl-2,5-dimethyl-1-piperazinyl)-3-methoxybenzyl]-N,N-diethylbenzamide (SNC80), morphine, or methadone. Co-internalization was driven by the delta opioid receptor, required an active conformation of both receptors, and led to sorting to the lysosomal compartment. Altogether, our data indicate that mu–delta co-expression, likely through heteromerization, alters the intracellular fate of the mu opioid receptor, which provides a way to fine-tune mu opioid receptor signaling. It also represents an interesting emerging concept for the development of novel therapeutic drugs and strategies.

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Fuxe, K., L. F. Agnati, K. Jacobsen, J. Hillion, M. Canals, M. Torvinen, B. Tinner-Staines, et al. "Receptor heteromerization in adenosine A2A receptor signaling: Relevance for striatal function and Parkinson's disease." Neurology 61, Issue 11, Supplement 6 (December 8, 2003): S19—S23. http://dx.doi.org/10.1212/01.wnl.0000095206.44418.5c.

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24

Cerrato, Bruno D., Oscar A. Carretero, Brana Janic, Hernán E. Grecco, and Mariela M. Gironacci. "Heteromerization Between the Bradykinin B 2 Receptor and the Angiotensin-(1–7) Mas Receptor." Hypertension 68, no. 4 (October 2016): 1039–48. http://dx.doi.org/10.1161/hypertensionaha.116.07874.

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Vekshina, N. L., P. K. Anokhin, A. G. Veretinskaya, and I. Yu Shamakina. "Heterodimeric D1-D2 dopamine receptors: a review." Biomeditsinskaya Khimiya 63, no. 1 (January 2017): 5–12. http://dx.doi.org/10.18097/pbmc20176301005.

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This review summarizes modern data on the structure and functions ofheteromersformed by D1 and D2 dopamine receptors focusing on their role in the mechanisms of drug dependence. This article discusses potential functional significance of heterodimeric D1-D2 dopamine receptorsdue to their localization in the brain as well as unique pharmacological propertiesversus constituent monomers. It is shown that heteromerization results in dramatic changes in activated signaling pathways compare to the corresponding monomers. These studies update our current knowledge of ligand-receptor interactions and provide better understanding of dopamine receptors pharmacology. Furthermore elucidation of significance of heterodimeric D1-D2 dopamine receptors as drug targets is important for the development of new effective drug addiction treatment.

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Rozenfeld, Raphael, Ittai Bushlin, Ivone Gomes, Nikos Tzavaras, Achla Gupta, Susana Neves, Lorenzo Battini, et al. "Receptor Heteromerization Expands the Repertoire of Cannabinoid Signaling in Rodent Neurons." PLoS ONE 7, no. 1 (January 3, 2012): e29239. http://dx.doi.org/10.1371/journal.pone.0029239.

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27

Younkin, Jason, Lia Baki, Amr Ellaithy, and Diomedes E. Logothetis. "Allosteric Effects of G-Protein Coupled Receptor Heteromerization: Relevance to Psychosis." Biophysical Journal 108, no. 2 (January 2015): 95a. http://dx.doi.org/10.1016/j.bpj.2014.11.548.

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Younkin, Jason, Lia Baki, and Diomedes E. Logothetis. "Allosteric Effects of G-Protein Coupled Receptor Heteromerization: Relevance to Psychosis." Biophysical Journal 110, no. 3 (February 2016): 426a. http://dx.doi.org/10.1016/j.bpj.2015.11.2303.

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Yang, Yuchen, Candice N. Hatcher-Solis, Maria P. Papakonstantinou, Albert A. Steiner, Takeharu Kawano, Leigh D. Plant, and Diomedes E. Logothetis. "Pharmacological Implications of Adenosine 2A and Dopamine Type 2 Receptor Heteromerization." Biophysical Journal 118, no. 3 (February 2020): 95a. http://dx.doi.org/10.1016/j.bpj.2019.11.681.

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Santiago, Julia, Christine Henzler, and Michael Hothorn. "Molecular Mechanism for Plant Steroid Receptor Activation by Somatic Embryogenesis Co-Receptor Kinases." Science 341, no. 6148 (August 8, 2013): 889–92. http://dx.doi.org/10.1126/science.1242468.

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Brassinosteroids, which control plant growth and development, are sensed by the leucine-rich repeat (LRR) domain of the membrane receptor kinase BRASSINOSTEROID INSENSITIVE 1 (BRI1), but it is unknown how steroid binding at the cell surface activates the cytoplasmic kinase domain of the receptor. A family of somatic embryogenesis receptor kinases (SERKs) has been genetically implicated in mediating early brassinosteroid signaling events. We found a direct and steroid-dependent interaction between the BRI1 and SERK1 LRR domains by analysis of their complex crystal structure at 3.3 angstrom resolution. We show that the SERK1 LRR domain is involved in steroid sensing and, through receptor–co-receptor heteromerization, in the activation of the BRI1 signaling pathway. Our work reveals how known missense mutations in BRI1 and in SERKs modulate brassinosteroid signaling and the targeting mechanism of BRI1 receptor antagonists.

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Ayoub, Mohammed Akli, Heng B. See, Ruth M. Seeber, Stephen P. Armstrong, and Kevin D. G. Pfleger. "Profiling Epidermal Growth Factor Receptor and Heregulin Receptor 3 Heteromerization Using Receptor Tyrosine Kinase Heteromer Investigation Technology." PLoS ONE 8, no. 5 (May 20, 2013): e64672. http://dx.doi.org/10.1371/journal.pone.0064672.

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Whitaker, Gina M., Francis C. Lynn, Christopher H. S. McIntosh, and Eric A. Accili. "Regulation of GIP and GLP1 Receptor Cell Surface Expression by N-Glycosylation and Receptor Heteromerization." PLoS ONE 7, no. 3 (March 7, 2012): e32675. http://dx.doi.org/10.1371/journal.pone.0032675.

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Tripathi, Abhishek, P. Geoff Vana, Tanmay S. Chavan, Lioubov I. Brueggemann, Kenneth L. Byron, Nadya I. Tarasova, Brian F. Volkman, Vadim Gaponenko, and Matthias Majetschak. "Heteromerization of chemokine (C-X-C motif) receptor 4 with α1A/B-adrenergic receptors controls α1-adrenergic receptor function." Proceedings of the National Academy of Sciences 112, no. 13 (March 16, 2015): E1659—E1668. http://dx.doi.org/10.1073/pnas.1417564112.

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Recent evidence suggests that chemokine (C-X-C motif) receptor 4 (CXCR4) contributes to the regulation of blood pressure through interactions with α1-adrenergic receptors (ARs) in vascular smooth muscle. The underlying molecular mechanisms, however, are unknown. Using proximity ligation assays to visualize single-molecule interactions, we detected that α1A/B-ARs associate with CXCR4 on the cell surface of rat and human vascular smooth muscle cells (VSMC). Furthermore, α1A/B-AR could be coimmunoprecipitated with CXCR4 in a HeLa expression system and in human VSMC. A peptide derived from the second transmembrane helix of CXCR4 induced chemical shift changes in the NMR spectrum of CXCR4 in membranes, disturbed the association between α1A/B-AR and CXCR4, and inhibited Ca2+ mobilization, myosin light chain (MLC) 2 phosphorylation, and contraction of VSMC upon α1-AR activation. CXCR4 silencing reduced α1A/B-AR:CXCR4 heteromeric complexes in VSMC and abolished phenylephrine-induced Ca2+ fluxes and MLC2 phosphorylation. Treatment of rats with CXCR4 agonists (CXCL12, ubiquitin) reduced the EC50 of the phenylephrine-induced blood pressure response three- to fourfold. These observations suggest that disruption of the quaternary structure of α1A/B-AR:CXCR4 heteromeric complexes by targeting transmembrane helix 2 of CXCR4 and depletion of the heteromeric receptor complexes by CXCR4 knockdown inhibit α1-AR–mediated function in VSMC and that activation of CXCR4 enhances the potency of α1-AR agonists. Our findings extend the current understanding of the molecular mechanisms regulating α1-AR and provide an example of the importance of G protein-coupled receptor (GPCR) heteromerization for GPCR function. Compounds targeting the α1A/B-AR:CXCR4 interaction could provide an alternative pharmacological approach to modulate blood pressure.

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Ferré, Sergi, Francisco Ciruela, César Quiroz, Rafael Luján, Patrizia Popoli, Rodrigo A. Cunha, Luigi F. Agnati, et al. "Adenosine Receptor Heteromers and their Integrative Role in Striatal Function." Scientific World JOURNAL 7 (2007): 74–85. http://dx.doi.org/10.1100/tsw.2007.211.

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By analyzing the functional role of adenosine receptor heteromers, we review a series of new concepts that should modify our classical views of neurotransmission in the central nervous system (CNS). Neurotransmitter receptors cannot be considered as single functional units anymore. Heteromerization of neurotransmitter receptors confers functional entities that possess different biochemical characteristics with respect to the individual components of the heteromer. Some of these characteristics can be used as a “biochemical fingerprint” to identify neurotransmitter receptor heteromers in the CNS. This is exemplified by changes in binding characteristics that are dependent on coactivation of the receptor units of different adenosine receptor heteromers. Neurotransmitter receptor heteromers can act as “processors” of computations that modulate cell signaling, sometimes critically involved in the control of pre- and postsynaptic neurotransmission. For instance, the adenosine A1-A2Areceptor heteromer acts as a concentration-dependent switch that controls striatal glutamatergic neurotransmission. Neurotransmitter receptor heteromers play a particularly important integrative role in the “local module” (the minimal portion of one or more neurons and/or one or more glial cells that operates as an independent integrative unit), where they act as processors mediating computations that convey information from diverse volume-transmitted signals. For instance, the adenosine A2A-dopamine D2receptor heteromers work as integrators of two different neurotransmitters in the striatal spine module.

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Xiang, Guoqing, Lia Baki, Takeharu Kawano, and Diomedes Logothetis. "Modulation of Mu-Opioid Receptor Signaling by Cannabinoid CB1 Receptor through Heteromerization, a Novel Analgesic Target." Biophysical Journal 116, no. 3 (February 2019): 234a. http://dx.doi.org/10.1016/j.bpj.2018.11.1287.

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Hohmann, Ulrich, Julia Santiago, Joël Nicolet, Vilde Olsson, Fabio M. Spiga, Ludwig A. Hothorn, Melinka A. Butenko, and Michael Hothorn. "Mechanistic basis for the activation of plant membrane receptor kinases by SERK-family coreceptors." Proceedings of the National Academy of Sciences 115, no. 13 (March 12, 2018): 3488–93. http://dx.doi.org/10.1073/pnas.1714972115.

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Plant-unique membrane receptor kinases with leucine-rich repeat ectodomains (LRR-RKs) can sense small molecule, peptide, and protein ligands. Many LRR-RKs require SERK-family coreceptor kinases for high-affinity ligand binding and receptor activation. How one coreceptor can contribute to the specific binding of distinct ligands and activation of different LRR-RKs is poorly understood. Here we quantitatively analyze the contribution of SERK3 to ligand binding and activation of the brassinosteroid receptor BRI1 and the peptide hormone receptor HAESA. We show that while the isolated receptors sense their respective ligands with drastically different binding affinities, the SERK3 ectodomain binds the ligand-associated receptors with very similar binding kinetics. We identify residues in the SERK3 N-terminal capping domain, which allow for selective steroid and peptide hormone recognition. In contrast, residues in the SERK3 LRR core form a second, constitutive receptor–coreceptor interface. Genetic analyses of protein chimera between BRI1 and SERK3 define that signaling-competent complexes are formed by receptor–coreceptor heteromerization in planta. A functional BRI1–HAESA chimera suggests that the receptor activation mechanism is conserved among different LRR-RKs, and that their signaling specificity is encoded in the kinase domain of the receptor. Our work pinpoints the relative contributions of receptor, ligand, and coreceptor to the formation and activation of SERK-dependent LRR-RK signaling complexes regulating plant growth and development.

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Lebrun, J. J., and W. W. Vale. "Activin and inhibin have antagonistic effects on ligand-dependent heteromerization of the type I and type II activin receptors and human erythroid differentiation." Molecular and Cellular Biology 17, no. 3 (March 1997): 1682–91. http://dx.doi.org/10.1128/mcb.17.3.1682.

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Activins and inhibins belong to the transforming growth factor beta (TGF-beta)-like superfamily and exert their effects on a broad range of cellular targets by modulating cell differentiation and proliferation. Members of this family interact with two structurally related classes of receptors (type I and type II), both containing a serine/threonine kinase domain. When expressed alone, the type II but not the type I activin receptor can bind activin. However, the presence of a type I receptor is required for signaling. For TGF-beta1, ligand binding to the type II receptor results in the recruitment and transphosphorylation of the type I receptor. Transient overexpression of the two types of activin receptor results in ligand-independent receptor heteromerization and activation. Nevertheless, activin addition to the transfected cells increased complex formation between the two receptors, suggesting a mechanism of action similar to that observed for the TGF-beta receptor. In the present study, we generated a stable cell line, overexpressing the two types of activin receptor upon induction, in the human erythroleukemia cell line K562. We demonstrate here that activin specifically induces heteromer formation between the type I and type II receptors in a time-dependent manner. Using this stable line, we analyzed the effects of activin and inhibin on human erythroid differentiation. Our results indicate that activin signal transduction mediated through its type I and type II receptors results in an increase in the hemoglobin content of the cells and limits their proliferation. Finally, using cell lines that can be induced to overexpress ActRII and ActRIB or ActRIB only, we show that the inhibin antagonistic effects on activin-induced biological responses are mediated through a competition for the type II activin receptor but also require the presence of an inhibin-specific binding component.

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Maggio, Roberto, Irene Fasciani, Mario Rossi, Jacopo Di Gregorio, Ilaria Pietrantoni, Valentina Puca, Vincenzo Flati, and Marco Scarselli. "Variants of G protein-coupled receptors: a reappraisal of their role in receptor regulation." Biochemical Society Transactions 44, no. 2 (April 11, 2016): 589–94. http://dx.doi.org/10.1042/bst20150239.

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Truncated or shorter forms of G protein-coupled receptors (GPCRs), originating by alternative splicing, have been considered physiologically irrelevant for a rather long time. Nevertheless, it is now recognized that alternative splicing variants of GPCRs greatly increase the total number of receptor isoforms and can regulate receptor trafficking and signalling. Furthermore, dimerization of these truncated variants with other receptors concurs to expand receptor diversity. Highly truncated variants of GPCRs, typically, are retained in the endoplasmic reticulum (ER) and by heteromerization prevent the wild-type receptor to reach the plasma membrane, exerting a dominant-negative effect on its function. This can be responsible for some pathological conditions but in some other cases, it can offer protection from a disease because the expression of the receptor, that is necessary for binding an infectious agent, is attenuated. Here, we propose a possible new mechanism of creation of truncated GPCR variants through an internal ribosome entry site (IRES), a nucleotide sequence that allows cap independent translation of proteins by recruiting the ribosome in proximity of an internal initiation codon. We suggest that an IRES, situated in the third cytoplasmic loop, could be responsible for the translation of the last two transmembrane (TM) regions of the muscarinic M2 receptor. IRES driven expression of this C-terminal part of the muscarinic M2 receptor could represent a novel and additional mechanism of receptor regulation.

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Franco, Rafael, Vicent Casadó, Antoni Cortés, Carla Ferrada, Josefa Mallol, Amina Woods, Carme Lluis, Enric I. Canela, and Sergi Ferré. "Basic Concepts in G-Protein-Coupled Receptor Homo- and Heterodimerization." Scientific World JOURNAL 7 (2007): 48–57. http://dx.doi.org/10.1100/tsw.2007.197.

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Until recently, heptahelical G-protein-coupled receptors (GPCRs) were considered to be expressed as monomers on the cell surface of neuronal and non-neuronal cells. It is now becoming evident that this view must be overtly changed since these receptors can form homodimers, heterodimers, and higher-order oligomers on the plasma membrane. Here we discuss some of the basics and some new concepts of receptor homo- and heteromerization. Dimers-oligomers modify pharmacology, trafficking, and signaling of receptors. First of all, GPCR dimers must be considered as the main molecules that are targeted by neurotransmitters or by drugs. Thus, binding data must be fitted to dimer-based models. In these models, it is considered that the conformational changes transmitted within the dimer molecule lead to cooperativity. Cooperativity must be taken into account in the binding of agonists-antagonists-drugs and also in the binding of the so-called allosteric modulators. Cooperativity results from the intramolecular cross-talk in the homodimer. As an intramolecular cross-talk in the heterodimer, the binding of one neurotransmitter to one receptor often affects the binding of the second neurotransmitter to the partner receptor. Coactivation of the two receptors in a heterodimer can change completely the signaling pathway triggered by the neurotransmitter as well as the trafficking of the receptors. Heterodimer-specific drugs or dual drugs able to activate the two receptors in the heterodimer simultaneously emerge as novel and promising drugs for a variety of central nervous system (CNS) therapeutic applications.

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Gomes, Ivone, Adriaan P. IJzerman, Kai Ye, Emeline L. Maillet, and Lakshmi A. Devi. "G Protein-Coupled Receptor Heteromerization: A Role in Allosteric Modulation of Ligand Binding." Molecular Pharmacology 79, no. 6 (March 17, 2011): 1044–52. http://dx.doi.org/10.1124/mol.110.070847.

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Milan-Lobo, Laura, and Jennifer L. Whistler. "Heteromerization of the μ- and δ-Opioid Receptors Produces Ligand-Biased Antagonism and Alters μ-Receptor Trafficking." Journal of Pharmacology and Experimental Therapeutics 337, no. 3 (March 21, 2011): 868–75. http://dx.doi.org/10.1124/jpet.111.179093.

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Franco, Rafael, David Aguinaga, Jasmina Jiménez, Jaume Lillo, Eva Martínez-Pinilla, and Gemma Navarro. "Biased receptor functionality versus biased agonism in G-protein-coupled receptors." Biomolecular Concepts 9, no. 1 (December 26, 2018): 143–54. http://dx.doi.org/10.1515/bmc-2018-0013.

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AbstractFunctional selectivity is a property of G-protein-coupled receptors (GPCRs) by which activation by different agonists leads to different signal transduction mechanisms. This phenomenon is also known as biased agonism and has attracted the interest of drug discovery programs in both academy and industry. This relatively recent concept has raised concerns as to the validity and real translational value of the results showing bias; firstly biased agonism may vary significantly depending on the cell type and the experimental constraints, secondly the conformational landscape that leads to biased agonism has not been defined. Remarkably, GPCRs may lead to differential signaling even when a single agonist is used. Here we present a concept that constitutes a biochemical property of GPCRs that may be underscored just using one agonist, preferably the endogenous agonist. “Biased receptor functionality” is proposed to describe this effect with examples based on receptor heteromerization and alternative splicing. Examples of regulation of final agonist-induced outputs based on interaction with β-arrestins or calcium sensors are also provided. Each of the functional GPCR units (which are finite in number) has a specific conformation. Binding of agonist to a specific conformation, i.e. GPCR activation, is sensitive to the kinetics of the agonist-receptor interactions. All these players are involved in the contrasting outputs obtained when different agonists are assayed.

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Tadagaki, Kenjiro, Daniela Tudor, Florence Gbahou, Pia Tschische, Maria Waldhoer, Morgane Bomsel, Ralf Jockers, and Maud Kamal. "Human cytomegalovirus-encoded UL33 and UL78 heteromerize with host CCR5 and CXCR4 impairing their HIV coreceptor activity." Blood 119, no. 21 (May 24, 2012): 4908–18. http://dx.doi.org/10.1182/blood-2011-08-372516.

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AbstractHuman cytomegalovirus (HCMV) encodes four 7-transmembrane-spanning (7TM) proteins, US28, US27, UL33, and UL78, which present important sequence homology with human chemokine receptors. Whereas US28 binds a large range of chemokines and disturbs host cell signaling at different levels, the others are orphans with largely unknown functions. Assembly of 2 different 7TM proteins into hetero-oligomeric complexes may profoundly change their respective functional properties. We show that HCMV-encoded UL33 and UL78 form heteromers with CCR5 and CXCR4 chemokine receptors in transfected human embryonic kidney 293T cells and monocytic THP-1 cells. Expression of UL33 and UL78 had pleiotropic, predominantly negative, effects on CCR5 and CXCR4 cell surface expression, ligand-induced internalization, signal transduction, and migration without modifying the chemokine binding properties of CCR5 and CXCR4. Importantly, the coreceptor activity of CCR5 and CXCR4 for HIV was largely impaired in the presence of UL33 and UL78 without affecting expression of the primary HIV entry receptor CD4 and its interaction with CCR5 and CXCR4. Collectively, we identified the first molecular function for the HCMV-encoded orphan UL33 and UL78 7TM proteins, namely the regulation of cellular chemokine receptors through receptor heteromerization.

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Bontempi, Leonardo, Paola Savoia, Federica Bono, Chiara Fiorentini, and Cristina Missale. "Dopamine D3 and acetylcholine nicotinic receptor heteromerization in midbrain dopamine neurons: Relevance for neuroplasticity." European Neuropsychopharmacology 27, no. 4 (April 2017): 313–24. http://dx.doi.org/10.1016/j.euroneuro.2017.01.015.

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Azdad, Karima, David Gall, Amina S. Woods, Catherine Ledent, Sergi Ferré, and Serge N. Schiffmann. "Dopamine D2 and Adenosine A2A Receptors Regulate NMDA-Mediated Excitation in Accumbens Neurons Through A2A–D2 Receptor Heteromerization." Neuropsychopharmacology 34, no. 4 (September 17, 2008): 972–86. http://dx.doi.org/10.1038/npp.2008.144.

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Uhl, B., L. Mittmann, J. Dominik, J. Schaubächer, C. Braun, R. Pick, M. Canis, et al. "P03.17 uPA-PAI-1 heteromers promote advanced stages of breast cancer by attracting pro-tumorigenic neutrophils." Journal for ImmunoTherapy of Cancer 8, Suppl 2 (October 2020): A29.2—A29. http://dx.doi.org/10.1136/jitc-2020-itoc7.56.

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BackgroundHigh tumor levels of urokinase-type plasminogen activator (uPA)-plasminogen activator inhibitor-1 (PAI-1) heteromers independently predict poor survival in early breast cancer. The pathogenetic role of this protein complex, however, remains largely obscure.Materials and MethodsNeutrophil trafficking was analyzed in orthotopic (multi-channel flow cytometry) and heterotopic (ear; multi-channel in vivo microscopy) mouse models of 4T1 breast cancer, in a mouse peritonitis assay (multi-channel flow cytometry), as well as in the mouse cremaster muscle (multi-channel in vivo microscopy). Cytokine expression in tumors was determined by multiplex ELISA. Phenotypic and functional properties of primary mouse neutrophils, microvascular endothelial cells (cell line bEnd.3), macrophages (cell line RAW 264.7), and breast cancer cells (cell line 4T1) were characterized in different in vitro assays. uPA/PAI-1 expression and neutrophil infiltration in human breast cancer samples were assessed by RNA sequencing, immunhistochemistry, and ELISA.ResultsHere, we demonstrate that uPA-PAI-1 heteromerization multiplies the potential of the single proteins to attract pro-tumorigenic neutrophils. To this end, tumor-released uPA-PAI-1 utilizes very low density lipoprotein receptor and ERK mitogen-activated protein kinases to initiate a pro-inflammatory program in peritumoral macrophages. This promotes neutrophil trafficking to cancerous lesions and primes these immune cells towards a pro-tumorigenic phenotype, thus supporting tumor growth and metastasis. Blockade of uPA-PAI-1 heteromerization by a novel inhibitor effectively interfered with these events and prevented tumor progression.ConclusionsOur findings identify an already therapeutically targetable interplay between hemostasis and innate immunity that drives advanced stages of breast cancer. As a personalized immunotherapeutic strategy, blockade of uPA-PAI-1 heteromerization might be particularly beneficial for patients with highly aggressive uPA-PAI-1hightumors.This study was supported by Deutsche Forschungsgemeinschaft (DFG), Sonderforschungsbereich (SFB) 914.Disclosure InformationB. Uhl: None. L. Mittmann: None. J. Dominik: None. J. Schaubächer: None. C. Braun: None. R. Pick: None. M. Canis: None. S. Kanse: None. W. Weichert: None. M. Sperandio: None. K. Lauber: None. F. Krombach: None. C.A. Reichel: None.

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Dewannieux, Marie, and Mary K. Collins. "Spontaneous Heteromerization of Gammaretrovirus Envelope Proteins: a Possible Novel Mechanism of Retrovirus Restriction." Journal of Virology 82, no. 19 (July 30, 2008): 9789–94. http://dx.doi.org/10.1128/jvi.02696-07.

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ABSTRACT The env gene of gammaretroviruses encodes a glycoprotein conserved among diverse retroviruses, except for the domains involved in receptor binding. Here we show that pairs of gammaretrovirus envelope proteins (from Friend virus and GALV or xenotropic viruses) assemble into heteromers when coexpressed. This assembly results in a strong inhibition of infectivity. An unrelated envelope protein does not assemble in heteromers with the gammaretrovirus glycoproteins tested and does not affect their infectivity, demonstrating the specificity of the mechanism we describe. We propose that the numerous copies of endogenous retroviral env genes conserved within mammalian genomes act as restriction factors against infectious retroviruses.

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Ferraro, Luca, Sarah Beggiato, Maria Cristina Tomasini, Kjell Fuxe, Tiziana Antonelli, and Sergio Tanganelli. "A2A/D2 receptor heteromerization in a model of Parkinson's disease. Focus on striatal aminoacidergic signaling." Brain Research 1476 (October 2012): 96–107. http://dx.doi.org/10.1016/j.brainres.2012.01.032.

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Fischer, Jana, Gunnar Kleinau, Claudia Rutz, Denise Zwanziger, Noushafarin Khajavi, Anne Müller, Maren Rehders, et al. "Evidence of G-protein-coupled receptor and substrate transporter heteromerization at a single molecule level." Cellular and Molecular Life Sciences 75, no. 12 (December 30, 2017): 2227–39. http://dx.doi.org/10.1007/s00018-017-2728-1.

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Rukavina Mikusic, Natalia L., Mauro G. Silva, Luciana R. Mazzitelli, Robson A. S. Santos, Karina A. Gómez, Hernán E. Grecco, and Mariela M. Gironacci. "Interaction Between the Angiotensin-(1–7) Mas Receptor and the Dopamine D2 Receptor." Hypertension 77, no. 5 (May 2021): 1659–69. http://dx.doi.org/10.1161/hypertensionaha.120.16614.

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Ang (angiotensin) 1–7 MasR (Mas receptor) and D2R (dopamine D2 receptor) stimulation is coupled to anti-inflammatory responses. In the present work, we investigated the hypothesis that the anti-inflammatory action mediated by both receptors results from MasR-D2R heteromerization. Human monocyte (THP-1) cells differentiated to macrophages and exposed to lipopolysaccharide were employed. Ang (1–7) and the D2R agonist SUM (sumanirole) induced a decrease in proinflammatory IL (interleukin) 6 release in human macrophages exposed to a proinflammatory stimulus. The Ang (1–7)–induced decrease in IL-6 was blocked by the D2R antagonist. Conversely, the SUM induced decrease in IL-6 was prevented by the MasR antagonist and when MasR expression was downregulated, suggesting MasR-D2R interaction. Co-immunoprecipitation assay in THP-1 cells and in human monocyte differentiated macrophages from peripheral blood mononuclear cells confirmed MasR-D2R interaction. To avoid the influence from other receptors, MasR-D2R interaction was characterized in transfected human embryonic kidney 293T cells. Fluorescence resonance energy transfer analysis showed that MasR and D2R formed a constitutive heteromer, which was not modified by their agonists. Ang (1–7) and dopamine stimulated ERK (extracellular signal-regulated kinase) 1/2 and Akt (protein kinase B) phosphorylation only in cells expressing MasR-D2R heteromers, but not in cells expressing each receptor alone. Ang (1–7)–stimulated ERK1/2 and Akt phosphorylation was prevented by D2R blockade while the effect of dopamine was prevented by MasR blockade, reinforcing the fact that MasR-D2R heteromers are involved in ERK1/2 and Akt activation induced by their agonists. Our findings provide new evidence regarding the mechanisms underlying the cross-talk between the Ang (1–7)/MasR axis and the dopaminergic system in response to a proinflammatory process.

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