| pubmed-article:11078882 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11078882 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:11078882 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:11078882 | lifeskim:mentions | umls-concept:C0033634 | lld:lifeskim |
| pubmed-article:11078882 | lifeskim:mentions | umls-concept:C0597298 | lld:lifeskim |
| pubmed-article:11078882 | lifeskim:mentions | umls-concept:C1335204 | lld:lifeskim |
| pubmed-article:11078882 | lifeskim:mentions | umls-concept:C1418440 | lld:lifeskim |
| pubmed-article:11078882 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:11078882 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:11078882 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:11078882 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:11078882 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:11078882 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:11078882 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:11078882 | pubmed:dateCreated | 2000-12-5 | lld:pubmed |
| pubmed-article:11078882 | pubmed:abstractText | The multi-site phosphorylation of the protein kinase C (PKC) superfamily plays an important role in the regulation of these enzymes. One of the key phosphorylation sites required for the activation of all PKC isoforms lies in the T-loop of the kinase domain. Recent in vitro and transfection experiments indicate that phosphorylation of this residue can be mediated by the 3-phosphoinositide-dependent protein kinase-1 (PDK1). In this study, we demonstrate that in embryonic stem (ES) cells lacking PDK1 (PDK1-/- cells), the intracellular levels of endogenously expressed PKCalpha, PKCbetaI, PKCgamma, PKCdelta, PKCepsilon, and PKC-related kinase-1 (PRK1) are vastly reduced compared to control ES cells (PDK1+/+ cells). The levels of PKCzeta and PRK2 protein are only moderately reduced in the PDK1-/- ES cells. We demonstrate that in contrast to PKCzeta expressed PDK1+/+ ES cells, PKCzeta in ES cells lacking PDK1 is not phosphorylated at its T-loop residue. This provides the first genetic evidence that PKCzeta is a physiological substrate for PDK1. In contrast, PRK2 is still partially phosphorylated at its T-loop in PDK1-/- cells, indicating the existence of a PDK1-independent mechanism for the phosphorylation of PRK2 at this residue. | lld:pubmed |
| pubmed-article:11078882 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11078882 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11078882 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11078882 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11078882 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11078882 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11078882 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11078882 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11078882 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11078882 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11078882 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:11078882 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:11078882 | pubmed:author | pubmed-author:WilliamsM RMR | lld:pubmed |
| pubmed-article:11078882 | pubmed:author | pubmed-author:AlessiD RDR | lld:pubmed |
| pubmed-article:11078882 | pubmed:author | pubmed-author:BalendranAA | lld:pubmed |
| pubmed-article:11078882 | pubmed:author | pubmed-author:HareG RGR | lld:pubmed |
| pubmed-article:11078882 | pubmed:author | pubmed-author:KielochAA | lld:pubmed |
| pubmed-article:11078882 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11078882 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:11078882 | pubmed:volume | 484 | lld:pubmed |
| pubmed-article:11078882 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11078882 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11078882 | pubmed:pagination | 217-23 | lld:pubmed |
| pubmed-article:11078882 | pubmed:dateRevised | 2009-4-7 | lld:pubmed |
| pubmed-article:11078882 | pubmed:meshHeading | pubmed-meshheading:11078882... | lld:pubmed |
| pubmed-article:11078882 | pubmed:meshHeading | pubmed-meshheading:11078882... | lld:pubmed |
| pubmed-article:11078882 | pubmed:meshHeading | pubmed-meshheading:11078882... | lld:pubmed |
| pubmed-article:11078882 | pubmed:meshHeading | pubmed-meshheading:11078882... | lld:pubmed |
| pubmed-article:11078882 | pubmed:meshHeading | pubmed-meshheading:11078882... | lld:pubmed |
| pubmed-article:11078882 | pubmed:meshHeading | pubmed-meshheading:11078882... | lld:pubmed |
| pubmed-article:11078882 | pubmed:meshHeading | pubmed-meshheading:11078882... | lld:pubmed |
| pubmed-article:11078882 | pubmed:meshHeading | pubmed-meshheading:11078882... | lld:pubmed |
| pubmed-article:11078882 | pubmed:meshHeading | pubmed-meshheading:11078882... | lld:pubmed |
| pubmed-article:11078882 | pubmed:meshHeading | pubmed-meshheading:11078882... | lld:pubmed |
| pubmed-article:11078882 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11078882 | pubmed:articleTitle | Further evidence that 3-phosphoinositide-dependent protein kinase-1 (PDK1) is required for the stability and phosphorylation of protein kinase C (PKC) isoforms. | lld:pubmed |
| pubmed-article:11078882 | pubmed:affiliation | MRC Protein Phosphorylation, MSI/WTB complex, University of Dundee, Dow Street, DD1 5EH, Dundee, UK. | lld:pubmed |
| pubmed-article:11078882 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11078882 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:5585 | entrezgene:pubmed | pubmed-article:11078882 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11078882 | lld:pubmed |
