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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
1987-4-17
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pubmed:abstractText |
Membranes of Dictyostelium discoideum cells were incubated under phosphorylation conditions and washed, and the effects on cAMP binding to chemotactic receptors in the absence and presence of guanosine 5'-O-(3-thiotriphosphate) (GTP gamma S) were investigated. Most experiments were done with adenosine 5'-O-(3-thiotriphosphate) (ATP gamma S), which is a good substrate for many kinases, but the product, protein phosphorothioate, is not easily hydrolyzed by phosphatases. Pretreatment of membranes under phosphorylating conditions with MgATP gamma S alters the site heterogeneity of the cAMP-binding forms, without a significant effect on the total number of binding sites. A similar effect was induced by GTP gamma S under nonphosphorylation conditions. The effects of MgATP gamma S were rapid (t1/2 = 1 min), irreversible, and not induced by Mg2+ or ATP gamma S alone or by magnesium adenylyl imidodiphosphate and magnesium adenylyl (beta, gamma-methylene)diphosphate. MgATP induced a smaller inhibition than MgATP gamma S, which was potentiated by the addition of exogenous cAMP-dependent protein kinase. The effect of MgATP was rapidly reversible; reversibility was reduced by the phosphatase inhibitor NaF. These results suggest that the effects of MgATP gamma S are mediated by an endogenous protein kinase. The major 35S-thiophosphorylated band detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis was a protein with Mr = 36,000. The phosphorylation of a protein with the molecular weight of the cAMP receptor (Mr = 40,000-45,000) was not observed.
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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/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP,
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/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/Thionucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/adenosine 5'-O-(3-thiotriphosphate)
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
262
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3239-43
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:3029106-Adenosine Triphosphate,
pubmed-meshheading:3029106-Chemotaxis,
pubmed-meshheading:3029106-Cyclic AMP,
pubmed-meshheading:3029106-Dictyostelium,
pubmed-meshheading:3029106-GTP-Binding Proteins,
pubmed-meshheading:3029106-Guanosine 5'-O-(3-Thiotriphosphate),
pubmed-meshheading:3029106-Guanosine Triphosphate,
pubmed-meshheading:3029106-Kinetics,
pubmed-meshheading:3029106-Magnesium,
pubmed-meshheading:3029106-Phosphorylation,
pubmed-meshheading:3029106-Protein Kinases,
pubmed-meshheading:3029106-Receptors, Cyclic AMP,
pubmed-meshheading:3029106-Thionucleotides
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pubmed:year |
1987
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pubmed:articleTitle |
Alteration of receptor/G-protein interaction by putative endogenous protein kinase activity in Dictyostelium discoideum membranes.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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