BIOMAT Database Logo BIOMAT Database Logo

Interactions between calmodulin, adenosine A2A, and dopamine D2 receptors. 2009

Gemma Navarro, and Marisol S Aymerich, and Daniel Marcellino, and Antoni Cortés, and Vicent Casadó, and Josefa Mallol, and Enric I Canela, and Luigi Agnati, and Amina S Woods, and Kjell Fuxe, and Carmen Lluís, and Jose Luis Lanciego, and Sergi Ferré, and Rafael Franco
Institut d'Investigacions Biomèdiques August Pi i Sunyer, Centro de Investigación Biomédica en Red Sobre Enfermedades Neurodegenerativas, and Department of Biochemistry and Molecular Biology, Faculty of Biology, University of Barcelona, 08028 Barcelona, Spain.

The Ca(2+)-binding protein calmodulin (CaM) has been shown to bind directly to cytoplasmic domains of some G protein-coupled receptors, including the dopamine D(2) receptor. CaM binds to the N-terminal portion of the long third intracellular loop of the D(2) receptor, within an Arg-rich epitope that is also involved in the binding to G(i/o) proteins and to the adenosine A(2A) receptor, with the formation of A(2A)-D(2) receptor heteromers. In the present work, by using proteomics and bioluminescence resonance energy transfer (BRET) techniques, we provide evidence for the binding of CaM to the A(2A) receptor. By using BRET and sequential resonance energy transfer techniques, evidence was obtained for CaM-A(2A)-D(2) receptor oligomerization. BRET competition experiments indicated that, in the A(2A)-D(2) receptor heteromer, CaM binds preferentially to a proximal C terminus epitope of the A(2A) receptor. Furthermore, Ca(2+) was found to induce conformational changes in the CaM-A(2A)-D(2) receptor oligomer and to selectively modulate A(2A) and D(2) receptor-mediated MAPK signaling in the A(2A)-D(2) receptor heteromer. These results may have implications for basal ganglia disorders, since A(2A)-D(2) receptor heteromers are being considered as a target for anti-parkinsonian agents.

UI MeSH Term Description Entries
D008297 Male Males
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D011993 Recombinant Fusion Proteins Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes. Fusion Proteins, Recombinant,Recombinant Chimeric Protein,Recombinant Fusion Protein,Recombinant Hybrid Protein,Chimeric Proteins, Recombinant,Hybrid Proteins, Recombinant,Recombinant Chimeric Proteins,Recombinant Hybrid Proteins,Chimeric Protein, Recombinant,Fusion Protein, Recombinant,Hybrid Protein, Recombinant,Protein, Recombinant Chimeric,Protein, Recombinant Fusion,Protein, Recombinant Hybrid,Proteins, Recombinant Chimeric,Proteins, Recombinant Fusion,Proteins, Recombinant Hybrid
D002147 Calmodulin A heat-stable, low-molecular-weight activator protein found mainly in the brain and heart. The binding of calcium ions to this protein allows this protein to bind to cyclic nucleotide phosphodiesterases and to adenyl cyclase with subsequent activation. Thereby this protein modulates cyclic AMP and cyclic GMP levels. Calcium-Dependent Activator Protein,Calcium-Dependent Regulator,Bovine Activator Protein,Cyclic AMP-Phosphodiesterase Activator,Phosphodiesterase Activating Factor,Phosphodiesterase Activator Protein,Phosphodiesterase Protein Activator,Regulator, Calcium-Dependent,AMP-Phosphodiesterase Activator, Cyclic,Activating Factor, Phosphodiesterase,Activator Protein, Bovine,Activator Protein, Calcium-Dependent,Activator Protein, Phosphodiesterase,Activator, Cyclic AMP-Phosphodiesterase,Activator, Phosphodiesterase Protein,Calcium Dependent Activator Protein,Calcium Dependent Regulator,Cyclic AMP Phosphodiesterase Activator,Factor, Phosphodiesterase Activating,Protein Activator, Phosphodiesterase,Protein, Bovine Activator,Protein, Calcium-Dependent Activator,Protein, Phosphodiesterase Activator,Regulator, Calcium Dependent
D002460 Cell Line Established cell cultures that have the potential to propagate indefinitely. Cell Lines,Line, Cell,Lines, Cell
D004298 Dopamine One of the catecholamine NEUROTRANSMITTERS in the brain. It is derived from TYROSINE and is the precursor to NOREPINEPHRINE and EPINEPHRINE. Dopamine is a major transmitter in the extrapyramidal system of the brain, and important in regulating movement. A family of receptors (RECEPTORS, DOPAMINE) mediate its action. Hydroxytyramine,3,4-Dihydroxyphenethylamine,4-(2-Aminoethyl)-1,2-benzenediol,Dopamine Hydrochloride,Intropin,3,4 Dihydroxyphenethylamine,Hydrochloride, Dopamine
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000241 Adenosine A nucleoside that is composed of ADENINE and D-RIBOSE. Adenosine or adenosine derivatives play many important biological roles in addition to being components of DNA and RNA. Adenosine itself is a neurotransmitter. Adenocard,Adenoscan
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

Related Publications

Gemma Navarro, and Marisol S Aymerich, and Daniel Marcellino, and Antoni Cortés, and Vicent Casadó, and Josefa Mallol, and Enric I Canela, and Luigi Agnati, and Amina S Woods, and Kjell Fuxe, and Carmen Lluís, and Jose Luis Lanciego, and Sergi Ferré, and Rafael Franco
Trafficking of adenosine A2A and dopamine D2 receptors.
January 2005, Journal of molecular neuroscience : MN,
Gemma Navarro, and Marisol S Aymerich, and Daniel Marcellino, and Antoni Cortés, and Vicent Casadó, and Josefa Mallol, and Enric I Canela, and Luigi Agnati, and Amina S Woods, and Kjell Fuxe, and Carmen Lluís, and Jose Luis Lanciego, and Sergi Ferré, and Rafael Franco
Mapping interactions between dopamine and adenosine A2a receptors using pharmacologic MRI.
February 2005, Synapse (New York, N.Y.),
Gemma Navarro, and Marisol S Aymerich, and Daniel Marcellino, and Antoni Cortés, and Vicent Casadó, and Josefa Mallol, and Enric I Canela, and Luigi Agnati, and Amina S Woods, and Kjell Fuxe, and Carmen Lluís, and Jose Luis Lanciego, and Sergi Ferré, and Rafael Franco
Coaggregation, cointernalization, and codesensitization of adenosine A2A receptors and dopamine D2 receptors.
May 2002, The Journal of biological chemistry,
Gemma Navarro, and Marisol S Aymerich, and Daniel Marcellino, and Antoni Cortés, and Vicent Casadó, and Josefa Mallol, and Enric I Canela, and Luigi Agnati, and Amina S Woods, and Kjell Fuxe, and Carmen Lluís, and Jose Luis Lanciego, and Sergi Ferré, and Rafael Franco
Reciprocal interactions between adenosine A2A and dopamine D2 receptors in Chinese hamster ovary cells co-transfected with the two receptors.
September 1999, Biochemical pharmacology,
Gemma Navarro, and Marisol S Aymerich, and Daniel Marcellino, and Antoni Cortés, and Vicent Casadó, and Josefa Mallol, and Enric I Canela, and Luigi Agnati, and Amina S Woods, and Kjell Fuxe, and Carmen Lluís, and Jose Luis Lanciego, and Sergi Ferré, and Rafael Franco
Oligomerization of adenosine A2A and dopamine D2 receptors in living cells.
June 2003, Biochemical and biophysical research communications,
Gemma Navarro, and Marisol S Aymerich, and Daniel Marcellino, and Antoni Cortés, and Vicent Casadó, and Josefa Mallol, and Enric I Canela, and Luigi Agnati, and Amina S Woods, and Kjell Fuxe, and Carmen Lluís, and Jose Luis Lanciego, and Sergi Ferré, and Rafael Franco
Dopamine D2 and adenosine A2A receptors regulate NMDA-mediated excitation in accumbens neurons through A2A-D2 receptor heteromerization.
March 2009, Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology,
Gemma Navarro, and Marisol S Aymerich, and Daniel Marcellino, and Antoni Cortés, and Vicent Casadó, and Josefa Mallol, and Enric I Canela, and Luigi Agnati, and Amina S Woods, and Kjell Fuxe, and Carmen Lluís, and Jose Luis Lanciego, and Sergi Ferré, and Rafael Franco
Nucleus accumbens and effort-related functions: behavioral and neural markers of the interactions between adenosine A2A and dopamine D2 receptors.
April 2010, Neuroscience,
Gemma Navarro, and Marisol S Aymerich, and Daniel Marcellino, and Antoni Cortés, and Vicent Casadó, and Josefa Mallol, and Enric I Canela, and Luigi Agnati, and Amina S Woods, and Kjell Fuxe, and Carmen Lluís, and Jose Luis Lanciego, and Sergi Ferré, and Rafael Franco
Allosteric interactions between agonists and antagonists within the adenosine A2A receptor-dopamine D2 receptor heterotetramer.
July 2015, Proceedings of the National Academy of Sciences of the United States of America,
Gemma Navarro, and Marisol S Aymerich, and Daniel Marcellino, and Antoni Cortés, and Vicent Casadó, and Josefa Mallol, and Enric I Canela, and Luigi Agnati, and Amina S Woods, and Kjell Fuxe, and Carmen Lluís, and Jose Luis Lanciego, and Sergi Ferré, and Rafael Franco
mGlu5, Dopamine D2 and Adenosine A2A Receptors in L-DOPA-induced Dyskinesias.
January 2016, Current neuropharmacology,
Gemma Navarro, and Marisol S Aymerich, and Daniel Marcellino, and Antoni Cortés, and Vicent Casadó, and Josefa Mallol, and Enric I Canela, and Luigi Agnati, and Amina S Woods, and Kjell Fuxe, and Carmen Lluís, and Jose Luis Lanciego, and Sergi Ferré, and Rafael Franco
Interaction of A2A adenosine and D2 dopamine receptors modulates corticostriatal glutamatergic transmission.
November 2007, Neuropharmacology,
Copied contents to your clipboard!