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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
24
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pubmed:dateCreated |
1994-1-21
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pubmed:abstractText |
The 14-residue peptide (peptide 14) corresponding to Arg2410-Lys2423 of the insulin-like growth factor II receptor (IGF-IIR) can activate the adenylate cyclase-inhibitor guanine nucleotide-binding protein Gi, and the 15-residue beta III-2 peptide Arg259-Lys273 of the beta 2-adrenergic receptor (beta 2AR) can activate the stimulatory protein Gs. In phospholipid vesicles, IGF-IIR and beta 2AR activate Gi and Gs in response to IGF-II and isoproterenol, respectively. We constructed a chimeric IGF-II receptor (beta III-2/IGF-IIR) by converting its native peptide 14 sequence to the beta III-2 sequence. In cells expressing beta III-2/IGF-IIR, membrane adenylate cyclase activity markedly increased without IGF-II and was further promoted by IGF-II. This was verified by measuring chloramphenicol acetyltransferase (CAT) activity in beta III-2/IGF-IIR cells with cotransfection of a cAMP response element-CAT construct. This study shows not only the conversion of G-protein specificity of a receptor from Gi to Gs but also the simulation of G protein-coupled receptor signals by using a short receptor region and intact cells. These findings indicate that the G protein-activation signals are interchangeable, self-determined structural motifs that function in the setting of either a single-spanning or multiple-spanning receptor.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8265625-1312225,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8265625-1314825,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8265625-1323236,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8265625-1327875,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8265625-1346134,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8265625-1645720,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8265625-1654554,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8265625-1657404,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8265625-1833393,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8265625-1985936,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8265625-2122258,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8265625-2124972,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8265625-2167177,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8265625-2170379,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8265625-2538455,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8265625-2547780,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8265625-2556294,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8265625-2780545,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8265625-2846532,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8265625-2957598,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8265625-6960240,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8265625-8383880,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8265625-8446172
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Adenylate Cyclase,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin-Like Growth Factor II,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, IGF Type 2,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Adrenergic, beta-2,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
90
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11772-6
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8265625-Adenylate Cyclase,
pubmed-meshheading:8265625-Amino Acid Sequence,
pubmed-meshheading:8265625-Animals,
pubmed-meshheading:8265625-Base Sequence,
pubmed-meshheading:8265625-Cell Line,
pubmed-meshheading:8265625-Cell Membrane,
pubmed-meshheading:8265625-Cercopithecus aethiops,
pubmed-meshheading:8265625-Cloning, Molecular,
pubmed-meshheading:8265625-DNA, Complementary,
pubmed-meshheading:8265625-GTP-Binding Proteins,
pubmed-meshheading:8265625-Humans,
pubmed-meshheading:8265625-Insulin-Like Growth Factor II,
pubmed-meshheading:8265625-Kinetics,
pubmed-meshheading:8265625-Models, Biological,
pubmed-meshheading:8265625-Molecular Sequence Data,
pubmed-meshheading:8265625-Oligodeoxyribonucleotides,
pubmed-meshheading:8265625-Protein Structure, Secondary,
pubmed-meshheading:8265625-Receptor, IGF Type 2,
pubmed-meshheading:8265625-Receptors, Adrenergic, beta-2,
pubmed-meshheading:8265625-Recombinant Fusion Proteins,
pubmed-meshheading:8265625-Transfection
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pubmed:year |
1993
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pubmed:articleTitle |
Conversion of G-protein specificity of insulin-like growth factor II/mannose 6-phosphate receptor by exchanging of a short region with beta-adrenergic receptor.
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pubmed:affiliation |
Department of Medicine, Harvard Medical School, Massachusetts General Hospital-East, Charlestown 02129.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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