| pubmed-article:10930578 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10930578 | lifeskim:mentions | umls-concept:C0285558 | lld:lifeskim |
| pubmed-article:10930578 | lifeskim:mentions | umls-concept:C1705328 | lld:lifeskim |
| pubmed-article:10930578 | lifeskim:mentions | umls-concept:C1705341 | lld:lifeskim |
| pubmed-article:10930578 | lifeskim:mentions | umls-concept:C0030016 | lld:lifeskim |
| pubmed-article:10930578 | lifeskim:mentions | umls-concept:C0812228 | lld:lifeskim |
| pubmed-article:10930578 | lifeskim:mentions | umls-concept:C1518792 | lld:lifeskim |
| pubmed-article:10930578 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:10930578 | pubmed:dateCreated | 2000-9-7 | lld:pubmed |
| pubmed-article:10930578 | 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. | lld:pubmed |
| pubmed-article:10930578 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10930578 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10930578 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10930578 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10930578 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10930578 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:10930578 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:10930578 | pubmed:author | pubmed-author:HemmingsB ABA | lld:pubmed |
| pubmed-article:10930578 | pubmed:author | pubmed-author:IngleyEE | lld:pubmed |
| pubmed-article:10930578 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10930578 | pubmed:day | 4 | lld:pubmed |
| pubmed-article:10930578 | pubmed:volume | 478 | lld:pubmed |
| pubmed-article:10930578 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10930578 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10930578 | pubmed:pagination | 253-9 | lld:pubmed |
| pubmed-article:10930578 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:10930578 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10930578 | pubmed:articleTitle | PKB/Akt interacts with inosine-5' monophosphate dehydrogenase through its pleckstrin homology domain. | lld:pubmed |
| pubmed-article:10930578 | pubmed:affiliation | Friedrich Miescher-Institut, Basel, Switzerland. | lld:pubmed |
| pubmed-article:10930578 | pubmed:publicationType | Journal Article | lld:pubmed |
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