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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2010-2-4
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pubmed:abstractText |
The adenosine A(2A)-dopamine D(2) receptor heteromer is one of the most studied receptor heteromers. It has important implications for basal ganglia function and pathology. Recent studies using Bioluminescence and Sequential Resonance Energy Transfer techniques shed light on the role of Ca(2+) in the modulation of the quaternary structure of the A(2A)-D(2) receptor heteromer, which was found to depend on the binding of calmodulin (CaM) to the carboxy-terminus of the A(2A) receptor in the A(2A)-D(2) receptor heteromer. Importantly, the changes in quaternary structure correlate with changes in function. A Ca(2+)/CaM-dependent modulation of MAPK signaling upon agonist treatment could be observed in cells expressing A(2A)-D(2) receptor heteromers. These studies provide a first example of a Ca(2+)-mediated modulation of the quaternary structure and function of a receptor heteromer.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19896897-10419536,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19896897-10488094,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19896897-10737597,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19896897-10926927,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19896897-12542690,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19896897-15362892,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19896897-15456930,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19896897-16083292,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19896897-17408563,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19896897-17572452,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19896897-17646043,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19896897-17692396,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19896897-17950471,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19896897-18297054,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19896897-18537670,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19896897-18768750,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19896897-18800071,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19896897-19219011,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19896897-19344374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19896897-19648932,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19896897-9242710
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1471-4973
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2009 Elsevier Ltd. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:volume |
10
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
67-72
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pubmed:dateRevised |
2011-7-22
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pubmed:meshHeading |
pubmed-meshheading:19896897-Calcium,
pubmed-meshheading:19896897-Calmodulin,
pubmed-meshheading:19896897-Energy Transfer,
pubmed-meshheading:19896897-Humans,
pubmed-meshheading:19896897-Mitogen-Activated Protein Kinases,
pubmed-meshheading:19896897-Protein Binding,
pubmed-meshheading:19896897-Protein Multimerization,
pubmed-meshheading:19896897-Protein Structure, Quaternary,
pubmed-meshheading:19896897-Receptor, Adenosine A2A,
pubmed-meshheading:19896897-Receptors, Dopamine D2,
pubmed-meshheading:19896897-Signal Transduction
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pubmed:year |
2010
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pubmed:articleTitle |
Calcium-mediated modulation of the quaternary structure and function of adenosine A2A-dopamine D2 receptor heteromers.
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pubmed:affiliation |
National Institute on Drug Abuse, IRP, NIH, DHHS, Baltimore, MD 21224, USA. sferre@intra.nida.nih.gov
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Intramural
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