| pubmed-article:15684423 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15684423 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:15684423 | lifeskim:mentions | umls-concept:C0035687 | lld:lifeskim |
| pubmed-article:15684423 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:15684423 | lifeskim:mentions | umls-concept:C0036720 | lld:lifeskim |
| pubmed-article:15684423 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:15684423 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:15684423 | lifeskim:mentions | umls-concept:C0002345 | lld:lifeskim |
| pubmed-article:15684423 | lifeskim:mentions | umls-concept:C1419996 | lld:lifeskim |
| pubmed-article:15684423 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:15684423 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:15684423 | lifeskim:mentions | umls-concept:C2827447 | lld:lifeskim |
| pubmed-article:15684423 | lifeskim:mentions | umls-concept:C0662902 | lld:lifeskim |
| pubmed-article:15684423 | pubmed:issue | 14 | lld:pubmed |
| pubmed-article:15684423 | pubmed:dateCreated | 2005-4-4 | lld:pubmed |
| pubmed-article:15684423 | pubmed:abstractText | Insulin regulates alternative splicing of PKCbetaII mRNA by phosphorylation of SRp40 via a phosphatidylinositol 3-kinase pathway (Patel, N. A., Chalfant, C. E., Watson, J. E., Wyatt, J. R., Dean, N. M., Eichler, D. C., and Cooper, D. C. (2001) J. Biol. Chem. 276, 22648-22654). Transient transfection of constitutively active Akt2 kinase promotes PKCbetaII exon inclusion. Serine/arginine-rich (SR) RNA-binding proteins regulating the selection of alternatively spliced exons are potential substrates of Akt kinase because many of them contain RXRXX(S/T) motifs. Here we show that Akt2 kinase phosphorylated SRp40 in vivo and in vitro. Mutation of Ser86 on SRp40 blocked in vitro phosphorylation. In control Akt2(+/+) fibroblasts, insulin treatment increased the phosphorylation of endogenous SR proteins, but their phosphorylation state remained unaltered by insulin in fibroblasts from Akt2(-/-) mice. Levels of PKCbetaII protein were up-regulated by insulin in Akt2(+/+) cells; however, only very low levels of PKCbetaII were detected in Akt2(-/-) cells and did not change following insulin treatment. Endogenous PKCbetaI and -betaII mRNA levels in Akt2(+/+) and Akt2(-/-) gastrocnemius muscle tissues were compared using quantitative real time PCR. The results indicated a 54% decrease in the expression of PKCbetaII levels in Akt(-/-), whereas PKCbetaI levels remained unchanged in both samples. Further, transfection of Akt2(-/-) cells with a PKCbetaII splicing minigene revealed defective betaII exon inclusion. Co-transfection of the mutated SRp40 attenuated betaII exon inclusion. This study provides in vitro and in vivo evidence showing Akt2 kinase directly phosphorylated SRp40, thereby connecting the insulin, PI 3-kinase/Akt pathway with phosphorylation of a site on a nuclear splicing protein promoting exon inclusion. This model is upheld in Akt2-deficient mice with insulin resistance leading to diabetes mellitus. | lld:pubmed |
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| pubmed-article:15684423 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15684423 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15684423 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15684423 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:15684423 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:15684423 | pubmed:author | pubmed-author:BaeSun SikSS | lld:pubmed |
| pubmed-article:15684423 | pubmed:author | pubmed-author:KanekoSatoshi... | lld:pubmed |
| pubmed-article:15684423 | pubmed:author | pubmed-author:BirnbaumMorri... | lld:pubmed |
| pubmed-article:15684423 | pubmed:author | pubmed-author:ChengJin QJQ | lld:pubmed |
| pubmed-article:15684423 | pubmed:author | pubmed-author:PatelNiketa... | lld:pubmed |
| pubmed-article:15684423 | pubmed:author | pubmed-author:ChappellDavid... | lld:pubmed |
| pubmed-article:15684423 | pubmed:author | pubmed-author:WatsonJames... | lld:pubmed |
| pubmed-article:15684423 | pubmed:author | pubmed-author:CooperDenise... | lld:pubmed |
| pubmed-article:15684423 | pubmed:author | pubmed-author:ApostolatosHe... | lld:pubmed |
| pubmed-article:15684423 | pubmed:author | pubmed-author:DavidowitzKar... | lld:pubmed |
| pubmed-article:15684423 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15684423 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:15684423 | pubmed:volume | 280 | lld:pubmed |
| pubmed-article:15684423 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15684423 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15684423 | pubmed:pagination | 14302-9 | lld:pubmed |
| pubmed-article:15684423 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:15684423 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15684423 | pubmed:articleTitle | Molecular and genetic studies imply Akt-mediated signaling promotes protein kinase CbetaII alternative splicing via phosphorylation of serine/arginine-rich splicing factor SRp40. | lld:pubmed |
| pubmed-article:15684423 | pubmed:affiliation | Department of Biochemistry, University of South Florida College of Medicine, Tampa, Florida 33612, USA. | lld:pubmed |
| pubmed-article:15684423 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15684423 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15684423 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:15684423 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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