|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
2
|
|
pubmed:dateCreated |
2000-4-24
|
|
pubmed:abstractText |
To delineate the role of the cytoplasmic tail in the distinct binding and coupling properties of human dopamine D1-like receptors, chimeric receptors were generated in which the entire tail region of wild-type human D1A (or D1) and D1B (or D5) receptors was exchanged. The hD1A-D1BT, but not hD1B-D1AT, receptor expression was dramatically reduced compared with wild-type receptor expression. Swapping the cytoplasmic tail resulted in a full switch of dopamine binding affinity and constitutive activity, while dopamine potency decreased and agonist-mediated maximal activation of adenylyl cyclase increased for both chimeras. Hence, the cytoplasmic tail plays a crucial role in D1-like receptor expression, agonist binding affinity and constitutive activation but regulates in a distinct fashion the formation of D1A and D1B receptor active states upon dopamine binding.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenylate Cyclase,
http://linkedlifedata.com/resource/pubmed/chemical/Antipsychotic Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/DRD5 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Dopamine Antagonists,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Dopamine D1,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Dopamine D5,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/dopamine D1A receptor
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Mar
|
|
pubmed:issn |
0014-5793
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
24
|
|
pubmed:volume |
470
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
183-8
|
|
pubmed:dateRevised |
2006-11-15
|
|
pubmed:meshHeading |
pubmed-meshheading:10734231-Adenylate Cyclase,
pubmed-meshheading:10734231-Antipsychotic Agents,
pubmed-meshheading:10734231-Binding Sites,
pubmed-meshheading:10734231-Cell Line,
pubmed-meshheading:10734231-Cell Membrane,
pubmed-meshheading:10734231-Cyclic AMP,
pubmed-meshheading:10734231-Dopamine,
pubmed-meshheading:10734231-Dopamine Antagonists,
pubmed-meshheading:10734231-Dose-Response Relationship, Drug,
pubmed-meshheading:10734231-Enzyme Activation,
pubmed-meshheading:10734231-Gene Expression,
pubmed-meshheading:10734231-Humans,
pubmed-meshheading:10734231-Ligands,
pubmed-meshheading:10734231-Receptors, Dopamine D1,
pubmed-meshheading:10734231-Receptors, Dopamine D5,
pubmed-meshheading:10734231-Recombinant Fusion Proteins,
pubmed-meshheading:10734231-Structure-Activity Relationship,
pubmed-meshheading:10734231-Thermodynamics,
pubmed-meshheading:10734231-Transfection
|
|
pubmed:year |
2000
|
|
pubmed:articleTitle |
Distinct function of the cytoplasmic tail in human D1-like receptor ligand binding and coupling.
|
|
pubmed:affiliation |
Neurosciences, Loeb Health Research Institute, Ottawa Hospital (Civic Campus) and Department of Cellular and Molecular Medicine, University of Ottawa, Ontario, Canada.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
