Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
1999-8-26
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.
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
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
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
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
96
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7922-7
pubmed:dateRevised
2009-11-18
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
pubmed:year
1999
pubmed:articleTitle
Five-transmembrane domains appear sufficient for a G protein-coupled receptor: functional five-transmembrane domain chemokine receptors.
pubmed:affiliation
Shanghai Institute of Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, People's Republic of China.
More...