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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2000-9-7
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pubmed:abstractText |
The pleckstrin homology (PH) domain of the protooncogenic serine/threonine protein kinase PKB/Akt can bind phosphoinositides. A yeast-based two-hybrid system was employed which identified inosine-5' monophosphate dehydrogenase (IMPDH) type II as specifically interacting with PKB/Akts PH domain. IMPDH catalyzes the rate-limiting step of de novo guanosine-triphosphate (GTP) biosynthesis. Using purified fusion proteins, PKB/Akts PH domain and IMPDH associated in vitro and this association moderately activated IMPDH. Purified PKB/Akt also associated with IMPDH in vitro. We could specifically pull-down PKB/Akt or IMPDH from mammalian cell lysates using glutathione-S-transferase (GST)-IMPDH or GST-PH domain fusion proteins, respectively. Additionally, PKB/Akt and IMPDH could be co-immunoprecipitated from COS cell lysates and active PKB/Akt could phosphorylate IMPDH in vitro. These results implicate PKB/Akt in the regulation of GTP biosynthesis through its interaction with IMPDH, which is involved in providing the GTP pool used by signal transducing G-proteins.
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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/AKT1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Blood Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/IMP Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-akt,
http://linkedlifedata.com/resource/pubmed/chemical/platelet protein P47
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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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 |
4
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pubmed:volume |
478
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
253-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10930578-Animals,
pubmed-meshheading:10930578-Binding Sites,
pubmed-meshheading:10930578-Blood Proteins,
pubmed-meshheading:10930578-Cell Line,
pubmed-meshheading:10930578-Enzyme Activation,
pubmed-meshheading:10930578-GTP-Binding Proteins,
pubmed-meshheading:10930578-Guanosine Triphosphate,
pubmed-meshheading:10930578-Humans,
pubmed-meshheading:10930578-IMP Dehydrogenase,
pubmed-meshheading:10930578-Models, Biological,
pubmed-meshheading:10930578-Phosphoproteins,
pubmed-meshheading:10930578-Phosphorylation,
pubmed-meshheading:10930578-Precipitin Tests,
pubmed-meshheading:10930578-Protein Binding,
pubmed-meshheading:10930578-Protein Structure, Tertiary,
pubmed-meshheading:10930578-Protein-Serine-Threonine Kinases,
pubmed-meshheading:10930578-Proto-Oncogene Proteins,
pubmed-meshheading:10930578-Proto-Oncogene Proteins c-akt,
pubmed-meshheading:10930578-Sequence Deletion,
pubmed-meshheading:10930578-Sequence Homology, Amino Acid,
pubmed-meshheading:10930578-Transfection,
pubmed-meshheading:10930578-Two-Hybrid System Techniques
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pubmed:year |
2000
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pubmed:articleTitle |
PKB/Akt interacts with inosine-5' monophosphate dehydrogenase through its pleckstrin homology domain.
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pubmed:affiliation |
Friedrich Miescher-Institut, Basel, Switzerland.
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pubmed:publicationType |
Journal Article
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