ArticleJournal of proteome research2008
How calmodulin interacts with the adenosine A(2A) and the dopamine D(2) receptors.
Article in Journal of proteome research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
22 citing papers in PubMed, 40 citations in OpenAlex.
- FDA Drug Repurposing Uncovers Modulators of Dopamine DJournal of medicinal chemistry · 2025Article
- Tumor-Associated Glycan Exploits Adenosine Receptor 2A Signaling to Facilitate Immune Evasion.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Cathepsin D interacts with adenosine AThe Journal of biological chemistry · 2022Article
- Calmodulin Binding Proteins and Alzheimer's Disease: Biomarkers, Regulatory Enzymes and Receptors That Are Regulated by Calmodulin.International journal of molecular sciences · 2020Review
- Review
- Calcium Sensors in Neuronal Function and Dysfunction.Cold Spring Harbor perspectives in biology · 2019Review
- Histidine, the less interactive cousin of arginine.European journal of mass spectrometry (Chichester, England) · 2019Article
- Neuronal Calcium and cAMP Cross-Talk Mediated by Cannabinoid CBFrontiers in cell and developmental biology · 2018Article
- Human adenosine A2A receptor binds calmodulin with high affinity in a calcium-dependent manner.Biophysical journal · 2015Article
- Functional characterization of G-protein-coupled receptors: a bioinformatics approach.Neuroscience · 2014Article
- Moonlighting proteins and protein-protein interactions as neurotherapeutic targets in the G protein-coupled receptor field.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2014Review
- Imaging of noncovalent complexes by MALDI-MS.Journal of the American Society for Mass Spectrometry · 2013Article
- MALDI/post ionization-ion mobility mass spectrometry of noncovalent complexes of dopamine receptors' epitopes.Journal of proteome research · 2013Article
- On the g-protein-coupled receptor heteromers and their allosteric receptor-receptor interactions in the central nervous system: focus on their role in pain modulation.Evidence-based complementary and alternative medicine : eCAM · 2013Article
- NCS-1 associates with adenosine A(2A) receptors and modulates receptor function.Frontiers in molecular neuroscience · 2012Article
- The triplet puzzle of homologies in receptor heteromers exists also in other types of protein-protein interactions.Journal of molecular neuroscience : MN · 2011Article
- Functional selectivity of adenosine receptor ligands.Purinergic signalling · 2011Article
- Allosteric effects of the antipsychotic drug trifluoperazine on the energetics of calcium binding by calmodulin.Proteins · 2010Article
- The diversity of calcium sensor proteins in the regulation of neuronal function.Cold Spring Harbor perspectives in biology · 2010Review
- Triplet puzzle: homologies of receptor heteromers.Journal of molecular neuroscience : MN · 2010Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
Receptor heteromerization is a mechanism used by G protein-coupled receptors to diversify their properties and function. We previously demonstrated that these interactions occur through salt bridge formation between epitopes of the involved receptors. Recent studies claim that calmodulin (CaM) binds to an Arg-rich epitope located in the amino-terminus of the dopamine D(2) receptor third intracellular loop. This is the same epitope involved in adenosine A(2A)-D(2) receptor heteromerization, through Coulombic interaction between the Arg residues and a phosphorylated serine (pS) located in the medial segment of the C-terminus of the A(2A) receptor. Mass spectrometric analysis indicates that an electrostatic interaction involving the D(2) receptor Arg-rich epitope and several CaM acidic epitopes are mainly responsible for the D(2) receptor-CaM binding. CaM could also form multiple noncovalent complexes by means of electrostatic interactions with an epitope localized in the proximal segment of the C-terminus of the A(2A) receptor. Ca(2+) disrupted the binding of CaM to the D(2) but not to the A(2A) receptor epitope, and CaM disrupted the electrostatic interactions between the D(2) receptor epitope and the more distal A(2A) receptor epitope. A model is introduced with the possible functional implications of A(2A)-D(2)-CaM interactions. These in vitro findings imply a possible regulatory role for CaM in receptor heteromers formation.
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Registered trials
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.