| pubmed-article:15262962 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15262962 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:15262962 | lifeskim:mentions | umls-concept:C0212694 | lld:lifeskim |
| pubmed-article:15262962 | lifeskim:mentions | umls-concept:C0285558 | lld:lifeskim |
| pubmed-article:15262962 | lifeskim:mentions | umls-concept:C1705328 | lld:lifeskim |
| pubmed-article:15262962 | lifeskim:mentions | umls-concept:C1705341 | lld:lifeskim |
| pubmed-article:15262962 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
| pubmed-article:15262962 | lifeskim:mentions | umls-concept:C0812228 | lld:lifeskim |
| pubmed-article:15262962 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:15262962 | lifeskim:mentions | umls-concept:C0598629 | lld:lifeskim |
| pubmed-article:15262962 | pubmed:issue | 39 | lld:pubmed |
| pubmed-article:15262962 | pubmed:dateCreated | 2004-9-20 | lld:pubmed |
| pubmed-article:15262962 | pubmed:abstractText | Full activation of protein kinase B (PKB)/Akt requires phosphorylation on Thr-308 and Ser-473 by 3-phosphoinositide-dependent kinase-1 (PDK1) and Ser-473 kinase (S473K), respectively. Although PDK1 has been well characterized, the identification of the S473K remains controversial. A major PKB Ser-473 kinase activity was purified from the membrane fraction of HEK293 cells and found to be DNA-dependent protein kinase (DNA-PK). DNA-PK co-localized and associated with PKB at the plasma membrane. In vitro, DNA-PK phosphorylated PKB on Ser-473, resulting in a approximately 10-fold enhancement of PKB activity. Knockdown of DNA-PK by small interfering RNA inhibited Ser-473 phosphorylation induced by insulin and pervanadate. DNA-PK-deficient glioblastoma cells did not respond to insulin at the level of Ser-473 phosphorylation; this effect was restored by complementation with the human PRKDC gene. We conclude that DNA-PK is a long sought after kinase responsible for the Ser-473 phosphorylation step in the activation of PKB. | lld:pubmed |
| pubmed-article:15262962 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15262962 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15262962 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:15262962 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:15262962 | pubmed:author | pubmed-author:HemmingsBrian... | lld:pubmed |
| pubmed-article:15262962 | pubmed:author | pubmed-author:HessDanielD | lld:pubmed |
| pubmed-article:15262962 | pubmed:author | pubmed-author:CronPeterP | lld:pubmed |
| pubmed-article:15262962 | pubmed:author | pubmed-author:FengJianhuaJ | lld:pubmed |
| pubmed-article:15262962 | pubmed:author | pubmed-author:ParkJongsunJ | lld:pubmed |
| pubmed-article:15262962 | pubmed:copyrightInfo | Copyright 2004 American Society for Biochemistry and Molecular Biology, Inc. | lld:pubmed |
| pubmed-article:15262962 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15262962 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:15262962 | pubmed:volume | 279 | lld:pubmed |
| pubmed-article:15262962 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15262962 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15262962 | pubmed:pagination | 41189-96 | lld:pubmed |
| pubmed-article:15262962 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:15262962 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15262962 | pubmed:articleTitle | Identification of a PKB/Akt hydrophobic motif Ser-473 kinase as DNA-dependent protein kinase. | lld:pubmed |
| pubmed-article:15262962 | pubmed:affiliation | Friedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, Basel CH-4058, Switzerland. | lld:pubmed |
| pubmed-article:15262962 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15262962 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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