rdf:type |
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lifeskim:mentions |
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pubmed:issue |
14
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pubmed:dateCreated |
1999-8-26
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pubmed:abstractText |
The putative seven-transmembrane (TM) domains have been the structural hallmark for the superfamily of heterotrimeric G protein-coupled receptors (GPCRs) that regulate a variety of cellular functions by mediating a large number of extracellular signals. Five-TM GPCR mutants of chemokine receptor CCR5 and CXCR4, the N-terminal segment of which connected directly to TM3 as a result of a deletion of TM1-2 and the first intracellular and extracellular loops, have been obtained in this study. Laser confocal microscopy and flow cytometry analysis revealed that these five-TM mutant GPCRs were expressed stably on the cell surface after transfection into human embryonic kidney 293 cells. The five-TM CCR5 and CXCR4 functioned as normal chemokine receptors in mediating chemokine-stimulated chemotaxis, Ca2+ influx, and activation of pertussis toxin-sensitive G proteins. Like the wild-type GPCRs, the five-TM mutant receptors also underwent agonist-dependent internalization and desensitization and were subjected to regulation by GPCR kinases and arrestins. Our study indicates that five-TM domains, at least in the case of CCR5 and CXCR4, appear to meet the minimum structural requirements for a functional GPCR and suggests possible existence of functional five-TM GPCRs in nature during evolution.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-2830256,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-7651349,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-8385611,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-8658171,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-8756719,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-8903513,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-9038367,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-9056720,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-9125212,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-9141501,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-9303305,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-9334377,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-9353342,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-9387415,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-9405640,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-9433423,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-9445013,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-9505194,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-9547359,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-9560152,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-9630212,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-9651309,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-9660746,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-9668034,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-9733719,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10393923-9851919
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/1-Methyl-3-isobutylxanthine,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Chemokine CCL5,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/Forskolin,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine 5'-O-(3-Thiotriphosphate),
http://linkedlifedata.com/resource/pubmed/chemical/Pertussis Toxin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, CCR5,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, CXCR4,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Virulence Factors, Bordetella
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0027-8424
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
96
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7922-7
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:10393923-1-Methyl-3-isobutylxanthine,
pubmed-meshheading:10393923-Amino Acid Sequence,
pubmed-meshheading:10393923-Calcium,
pubmed-meshheading:10393923-Cell Line,
pubmed-meshheading:10393923-Cell Membrane,
pubmed-meshheading:10393923-Chemokine CCL5,
pubmed-meshheading:10393923-Chemotaxis,
pubmed-meshheading:10393923-Cloning, Molecular,
pubmed-meshheading:10393923-Cyclic AMP,
pubmed-meshheading:10393923-Evolution, Molecular,
pubmed-meshheading:10393923-Forskolin,
pubmed-meshheading:10393923-GTP-Binding Proteins,
pubmed-meshheading:10393923-Guanosine 5'-O-(3-Thiotriphosphate),
pubmed-meshheading:10393923-Humans,
pubmed-meshheading:10393923-Kidney,
pubmed-meshheading:10393923-Models, Molecular,
pubmed-meshheading:10393923-Molecular Sequence Data,
pubmed-meshheading:10393923-Pertussis Toxin,
pubmed-meshheading:10393923-Protein Structure, Secondary,
pubmed-meshheading:10393923-Receptors, CCR5,
pubmed-meshheading:10393923-Receptors, CXCR4,
pubmed-meshheading:10393923-Recombinant Proteins,
pubmed-meshheading:10393923-Sequence Alignment,
pubmed-meshheading:10393923-Transfection,
pubmed-meshheading:10393923-Virulence Factors, Bordetella
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pubmed:year |
1999
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pubmed:articleTitle |
Five-transmembrane domains appear sufficient for a G protein-coupled receptor: functional five-transmembrane domain chemokine receptors.
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pubmed:affiliation |
Shanghai Institute of Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, People's Republic of China.
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