| pubmed-article:17335965 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17335965 | lifeskim:mentions | umls-concept:C1335190 | lld:lifeskim |
| pubmed-article:17335965 | lifeskim:mentions | umls-concept:C1705807 | lld:lifeskim |
| pubmed-article:17335965 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:17335965 | lifeskim:mentions | umls-concept:C0812228 | lld:lifeskim |
| pubmed-article:17335965 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:17335965 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:17335965 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:17335965 | pubmed:dateCreated | 2007-3-26 | lld:pubmed |
| pubmed-article:17335965 | pubmed:abstractText | A single nucleotide polymorphism in the partitioning defective protein-6alpha (Par6alpha) promoter is coupled with lower Par6alpha expression and better insulin sensitivity, whereas overexpression of Par6alpha in C2C12 myoblasts inhibits insulin-induced protein kinase B/Akt1 activation and glycogen synthesis. Here we show that a direct interaction of Par6alpha with atypical protein kinase C (aPKC) is crucial for this inhibition. A DeltaPB1-Par6alpha deletion mutant that does not interact with aPKC neither increased aPKC activity nor interfered with insulin-induced Akt1 activation in C2C12 cells. Further, T34 phosphorylation of Akt1 through aPKC is important for inhibition of Akt1. When Par6alpha was overexpressed, activation of wild-type Akt1 (-59.3%; p=0.049), but not T34A-Akt1 (+2.9%, p=0.41) was reduced after insulin stimulation. The resistance of T34A-Akt1 to Par6alpha/aPKC-mediated inhibition was also reflected by reconstitution of insulin-induced glycogen synthesis. In summary, Par6alpha-mediated inhibition of insulin-dependent glycogen synthesis in C2C12 cells depends on the direct interaction of Par6alpha with aPKC and on aPKC-mediated T34 phosphorylation of Akt1. | lld:pubmed |
| pubmed-article:17335965 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17335965 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17335965 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17335965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17335965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17335965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17335965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17335965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17335965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17335965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17335965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17335965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17335965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17335965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17335965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17335965 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17335965 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17335965 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:17335965 | pubmed:issn | 0303-7207 | lld:pubmed |
| pubmed-article:17335965 | pubmed:author | pubmed-author:LammersRR | lld:pubmed |
| pubmed-article:17335965 | pubmed:author | pubmed-author:MelzerMM | lld:pubmed |
| pubmed-article:17335965 | pubmed:author | pubmed-author:WeyrichPP | lld:pubmed |
| pubmed-article:17335965 | pubmed:author | pubmed-author:HennigeA MAM | lld:pubmed |
| pubmed-article:17335965 | pubmed:author | pubmed-author:HäringH-UHU | lld:pubmed |
| pubmed-article:17335965 | pubmed:author | pubmed-author:NeuschelerDD | lld:pubmed |
| pubmed-article:17335965 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17335965 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:17335965 | pubmed:volume | 268 | lld:pubmed |
| pubmed-article:17335965 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17335965 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17335965 | pubmed:pagination | 30-6 | lld:pubmed |
| pubmed-article:17335965 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:17335965 | pubmed:meshHeading | pubmed-meshheading:17335965... | lld:pubmed |
| pubmed-article:17335965 | pubmed:meshHeading | pubmed-meshheading:17335965... | lld:pubmed |
| pubmed-article:17335965 | pubmed:meshHeading | pubmed-meshheading:17335965... | lld:pubmed |
| pubmed-article:17335965 | pubmed:meshHeading | pubmed-meshheading:17335965... | lld:pubmed |
| pubmed-article:17335965 | pubmed:meshHeading | pubmed-meshheading:17335965... | lld:pubmed |
| pubmed-article:17335965 | pubmed:meshHeading | pubmed-meshheading:17335965... | lld:pubmed |
| pubmed-article:17335965 | pubmed:meshHeading | pubmed-meshheading:17335965... | lld:pubmed |
| pubmed-article:17335965 | pubmed:meshHeading | pubmed-meshheading:17335965... | lld:pubmed |
| pubmed-article:17335965 | pubmed:meshHeading | pubmed-meshheading:17335965... | lld:pubmed |
| pubmed-article:17335965 | pubmed:meshHeading | pubmed-meshheading:17335965... | lld:pubmed |
| pubmed-article:17335965 | pubmed:meshHeading | pubmed-meshheading:17335965... | lld:pubmed |
| pubmed-article:17335965 | pubmed:meshHeading | pubmed-meshheading:17335965... | lld:pubmed |
| pubmed-article:17335965 | pubmed:meshHeading | pubmed-meshheading:17335965... | lld:pubmed |
| pubmed-article:17335965 | pubmed:meshHeading | pubmed-meshheading:17335965... | lld:pubmed |
| pubmed-article:17335965 | pubmed:meshHeading | pubmed-meshheading:17335965... | lld:pubmed |
| pubmed-article:17335965 | pubmed:meshHeading | pubmed-meshheading:17335965... | lld:pubmed |
| pubmed-article:17335965 | pubmed:meshHeading | pubmed-meshheading:17335965... | lld:pubmed |
| pubmed-article:17335965 | pubmed:meshHeading | pubmed-meshheading:17335965... | lld:pubmed |
| pubmed-article:17335965 | pubmed:meshHeading | pubmed-meshheading:17335965... | lld:pubmed |
| pubmed-article:17335965 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17335965 | pubmed:articleTitle | The Par6alpha/aPKC complex regulates Akt1 activity by phosphorylating Thr34 in the PH-domain. | lld:pubmed |
| pubmed-article:17335965 | pubmed:affiliation | Department of Internal Medicine IV, University of Tübingen, Otfried-Müller-Str. 10, D-72076 Tübingen, Germany. | lld:pubmed |
| pubmed-article:17335965 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17335965 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:207 | entrezgene:pubmed | pubmed-article:17335965 | lld:entrezgene |
| entrez-gene:5583 | entrezgene:pubmed | pubmed-article:17335965 | lld:entrezgene |
| entrez-gene:5590 | entrezgene:pubmed | pubmed-article:17335965 | lld:entrezgene |
| entrez-gene:50855 | entrezgene:pubmed | pubmed-article:17335965 | lld:entrezgene |
| entrez-gene:56513 | entrezgene:pubmed | pubmed-article:17335965 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:17335965 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:17335965 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:17335965 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:17335965 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:17335965 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17335965 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17335965 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17335965 | lld:pubmed |
