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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-2
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pubmed:dateCreated |
1989-8-29
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pubmed:abstractText |
After ADP-ribosylation by cholera toxin which promotes dissociation of the subunits, the alpha-subunit of Gs (Gs alpha) remained strongly associated with plasma membranes of wild-type S49 cells, since its interaction with the membrane was insensitive to 1 M KCl. Its association with the membrane was partially disrupted by 6 M urea and totally abolished by treatment with alkali at pH greater than or equal to 11.5. In vitro translated Gs alpha could interact with plasma membranes from the cyc- mutant of S49 cells as revealed by its cosedimentation with the membrane fraction and incubation of reconstituted membranes with GTP gamma S did not alter anchorage of Gs alpha. The characteristics of the association of in vitro translated Gs alpha with cyc- membranes after GTP gamma S treatment, i.e. sensitivity to 1 M KCl, 6 M urea and alkali treatment, were very similar to those described for the ADP-ribosylated form in wild-type membranes. Restoration of the coupling between the adrenergic receptor and adenylate cyclase further confirmed the vectorial reconstitution of cyc- membranes by in vitro translated alpha-subunit of Gs.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
251
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
230-6
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:2502436-Adenosine Diphosphate Ribose,
pubmed-meshheading:2502436-Adenylate Cyclase,
pubmed-meshheading:2502436-Animals,
pubmed-meshheading:2502436-Cell Membrane,
pubmed-meshheading:2502436-Enzyme Activation,
pubmed-meshheading:2502436-GTP-Binding Proteins,
pubmed-meshheading:2502436-Guanosine 5'-O-(3-Thiotriphosphate),
pubmed-meshheading:2502436-Guanosine Triphosphate,
pubmed-meshheading:2502436-Humans,
pubmed-meshheading:2502436-Hydrogen-Ion Concentration,
pubmed-meshheading:2502436-Isoproterenol,
pubmed-meshheading:2502436-Lymphoma,
pubmed-meshheading:2502436-Mice,
pubmed-meshheading:2502436-Molecular Weight,
pubmed-meshheading:2502436-Mutation,
pubmed-meshheading:2502436-NAD,
pubmed-meshheading:2502436-Osmolar Concentration,
pubmed-meshheading:2502436-Protein Biosynthesis,
pubmed-meshheading:2502436-RNA, Messenger,
pubmed-meshheading:2502436-Thionucleotides,
pubmed-meshheading:2502436-Tumor Cells, Cultured
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pubmed:year |
1989
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pubmed:articleTitle |
Reconstitution of cyc- S49 membranes by in vitro translated Gs alpha. Membrane anchorage and functional implications.
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pubmed:affiliation |
Centre CNRS-INSERM de Pharmacologie-Endocrinologie, Montpellier, France.
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pubmed:publicationType |
Journal Article
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