| http://purl.uniprot.org/citations/28130124 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/28130124 | http://www.w3.org/2000/01/rdf-schema#comment | "Adenosine receptors are G protein-coupled receptors that sense extracellular adenosine to transmit intracellular signals. One of the four adenosine receptor subtypes, the adenosine A2A receptor (A2AR), has an exceptionally long intracellular C terminus (A2AR-ct) that mediates interactions with a large array of proteins, including calmodulin and α-actinin. Here, we aimed to ascertain the α-actinin 1/calmodulin interplay whilst binding to A2AR and the role of Ca2+ in this process. First, we studied the A2AR-α-actinin 1 interaction by means of native polyacrylamide gel electrophoresis, isothermal titration calorimetry, and surface plasmon resonance, using purified recombinant proteins. α-Actinin 1 binds the A2AR-ct through its distal calmodulin-like domain in a Ca2+-independent manner with a dissociation constant of 5-12μM, thus showing an ~100 times lower affinity compared to the A2AR-calmodulin/Ca2+ complex. Importantly, calmodulin displaced α-actinin 1 from the A2AR-ct in a Ca2+-dependent fashion, disrupting the A2AR-α-actinin 1 complex. Finally, we assessed the impact of Ca2+ on A2AR internalization in living cells, a function operated by the A2AR-α-actinin 1 complex. Interestingly, while Ca2+ influx did not affect constitutive A2AR endocytosis, it abolished agonist-dependent internalization. In addition, we demonstrated that the A2AR/α-actinin interaction plays a pivotal role in receptor internalization and function. Overall, our results suggest that the interplay of A2AR with calmodulin and α-actinin 1 is fine-tuned by Ca2+, a fact that might power agonist-mediated receptor internalization and function."xsd:string |
| http://purl.uniprot.org/citations/28130124 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbamcr.2017.01.013"xsd:string |
| http://purl.uniprot.org/citations/28130124 | http://purl.uniprot.org/core/author | "Ciruela F."xsd:string |
| http://purl.uniprot.org/citations/28130124 | http://purl.uniprot.org/core/author | "Kursula P."xsd:string |
| http://purl.uniprot.org/citations/28130124 | http://purl.uniprot.org/core/author | "Jaakola V.P."xsd:string |
| http://purl.uniprot.org/citations/28130124 | http://purl.uniprot.org/core/author | "Taura J."xsd:string |
| http://purl.uniprot.org/citations/28130124 | http://purl.uniprot.org/core/author | "Piirainen H."xsd:string |
| http://purl.uniprot.org/citations/28130124 | http://purl.uniprot.org/core/date | "2017"xsd:gYear |
| http://purl.uniprot.org/citations/28130124 | http://purl.uniprot.org/core/name | "Biochim Biophys Acta Mol Cell Res"xsd:string |
| http://purl.uniprot.org/citations/28130124 | http://purl.uniprot.org/core/pages | "674-686"xsd:string |
| http://purl.uniprot.org/citations/28130124 | http://purl.uniprot.org/core/title | "Calcium modulates calmodulin/alpha-actinin 1 interaction with and agonist-dependent internalization of the adenosine Apisub>2Api/sub> receptor."xsd:string |
| http://purl.uniprot.org/citations/28130124 | http://purl.uniprot.org/core/volume | "1864"xsd:string |
| http://purl.uniprot.org/citations/28130124 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/28130124 |
| http://purl.uniprot.org/citations/28130124 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/28130124 |
| http://purl.uniprot.org/uniprot/#_A0A024R694-mappedCitation-28130124 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/28130124 |
| http://purl.uniprot.org/uniprot/#_A1L0V1-mappedCitation-28130124 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/28130124 |
| http://purl.uniprot.org/uniprot/#_A8K1F6-mappedCitation-28130124 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/28130124 |
| http://purl.uniprot.org/uniprot/#_B4DFY0-mappedCitation-28130124 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/28130124 |
| http://purl.uniprot.org/uniprot/#_A7UAQ1-mappedCitation-28130124 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/28130124 |
| http://purl.uniprot.org/uniprot/#_B3KUX9-mappedCitation-28130124 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/28130124 |
| http://purl.uniprot.org/uniprot/#_B4DRP5-mappedCitation-28130124 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/28130124 |
| http://purl.uniprot.org/uniprot/#_B4DW87-mappedCitation-28130124 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/28130124 |
| http://purl.uniprot.org/uniprot/#_B3KVQ4-mappedCitation-28130124 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/28130124 |
| http://purl.uniprot.org/uniprot/#_B4DJ51-mappedCitation-28130124 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/28130124 |