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rdf:type |
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lifeskim:mentions |
umls-concept:C0018787,
umls-concept:C0020792,
umls-concept:C0086376,
umls-concept:C0205341,
umls-concept:C0376315,
umls-concept:C1425135,
umls-concept:C1514562,
umls-concept:C1704735,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
20
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pubmed:dateCreated |
2001-5-23
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pubmed:abstractText |
AGS3, a 650-amino acid protein encoded by an approximately 4-kilobase (kb) mRNA enriched in rat brain, is a Galpha(i)/Galpha(t)-binding protein that competes with Gbetagamma for interaction with Galpha(GDP) and acts as a guanine nucleotide dissociation inhibitor for heterotrimeric G-proteins. An approximately 2-kb AGS3 mRNA (AGS3-SHORT) is enriched in rat and human heart. We characterized the heart-enriched mRNA, identified the encoded protein, and determined its ability to interact with and regulate the guanine nucleotide-binding properties of G-proteins. Screening of a rat heart cDNA library, 5'-rapid amplification of cDNA ends, and RNase protection assays identified two populations of cDNAs (1979 and 2134 nucleotides plus the polyadenylation site) that diverged from the larger 4-kb mRNA (AGS3-LONG) in the middle of the protein coding region. Transfection of COS-7 cells with AGS3-SHORT cDNAs resulted in the expression of a major immunoreactive AGS3 polypeptide (M(r) approximately 23,000) with a translational start site at Met(495) of AGS3-LONG. Immunoblots indicated the expression of the M(r) approximately 23,000 polypeptide in rat heart. Glutathione S-transferase-AGS3-SHORT selectively interacted with the GDP-bound versus guanosine 5'-O-(3-thiotriphosphate) (GTPgammaS)-bound conformation of Galpha(i2) and inhibited GTPgammaS binding to Galpha(i2). Protein interaction assays with glutathione S-transferase-AGS3-SHORT and heart lysates indicated interaction of AGS3-SHORT with Galpha(i1/2) and Galpha(i3), but not Galpha(s) or Galpha(q). Immunofluorescent imaging and subcellular fractionation following transient expression of AGS3-SHORT and AGS3-LONG in COS-7 and Chinese hamster ovary cells indicated distinct subcellular distributions of the two forms of AGS3. Thus, AGS3 exists as a short and long form, both of which apparently stabilize the GDP-bound conformation of Galpha(i), but which differ in their tissue distribution and trafficking within the cell.
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pubmed:grant |
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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/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Protein alpha...,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Protein alpha...,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Gpsm1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine 5'-O-(3-Thiotriphosphate),
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Heterotrimeric GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
16601-10
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pubmed:dateRevised |
2011-7-14
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pubmed:meshHeading |
pubmed-meshheading:11278352-Amino Acid Sequence,
pubmed-meshheading:11278352-Animals,
pubmed-meshheading:11278352-Base Sequence,
pubmed-meshheading:11278352-Brain,
pubmed-meshheading:11278352-CHO Cells,
pubmed-meshheading:11278352-COS Cells,
pubmed-meshheading:11278352-Carrier Proteins,
pubmed-meshheading:11278352-Cercopithecus aethiops,
pubmed-meshheading:11278352-Cricetinae,
pubmed-meshheading:11278352-DNA, Complementary,
pubmed-meshheading:11278352-DNA Primers,
pubmed-meshheading:11278352-GTP-Binding Protein alpha Subunits, Gi-Go,
pubmed-meshheading:11278352-GTP-Binding Protein alpha Subunits, Gs,
pubmed-meshheading:11278352-Gene Library,
pubmed-meshheading:11278352-Glutathione Transferase,
pubmed-meshheading:11278352-Guanosine 5'-O-(3-Thiotriphosphate),
pubmed-meshheading:11278352-Guanosine Diphosphate,
pubmed-meshheading:11278352-Heart Ventricles,
pubmed-meshheading:11278352-Heterotrimeric GTP-Binding Proteins,
pubmed-meshheading:11278352-Humans,
pubmed-meshheading:11278352-Molecular Sequence Data,
pubmed-meshheading:11278352-Myocardium,
pubmed-meshheading:11278352-Organ Specificity,
pubmed-meshheading:11278352-Protein Conformation,
pubmed-meshheading:11278352-RNA, Messenger,
pubmed-meshheading:11278352-Rats,
pubmed-meshheading:11278352-Rats, Sprague-Dawley,
pubmed-meshheading:11278352-Recombinant Fusion Proteins,
pubmed-meshheading:11278352-Sequence Deletion,
pubmed-meshheading:11278352-Transfection
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pubmed:year |
2001
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pubmed:articleTitle |
Identification of a truncated form of the G-protein regulator AGS3 in heart that lacks the tetratricopeptide repeat domains.
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pubmed:affiliation |
Department of Pharmacology, Medical University of South Carolina, Charleston, South Carolina 29425, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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