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| pubmed-article:21419339 | lifeskim:mentions | umls-concept:C0034783 | lld:lifeskim |
| pubmed-article:21419339 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:21419339 | lifeskim:mentions | umls-concept:C1150481 | lld:lifeskim |
| pubmed-article:21419339 | lifeskim:mentions | umls-concept:C2254340 | lld:lifeskim |
| pubmed-article:21419339 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:21419339 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:21419339 | lifeskim:mentions | umls-concept:C0920644 | lld:lifeskim |
| pubmed-article:21419339 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:21419339 | pubmed:dateCreated | 2011-3-22 | lld:pubmed |
| pubmed-article:21419339 | pubmed:abstractText | Phosphoinositide 3-kinase ? (PI3K?) is activated by G protein-coupled receptors (GPCRs). We show here that PI3K? inhibits protein phosphatase 2A (PP2A) at the ?-adrenergic receptor (?AR, a GPCR) complex altering G protein coupling. PI3K? inhibition results in significant increase of ?AR-associated phosphatase activity leading to receptor dephosphorylation and resensitization preserving cardiac function. Mechanistically, PI3K? inhibits PP2A activity at the ?AR complex by phosphorylating an intracellular inhibitor of PP2A (I2PP2A) on serine residues 9 and 93, resulting in enhanced binding to PP2A. Indeed, enhanced phosphorylation of ?2ARs is observed with a phosphomimetic I2PP2A mutant that was completely reversed with a mutant mimicking dephosphorylated state. siRNA depletion of endogenous I2PP2A augments PP2A activity despite active PI3K resulting in ?2AR dephosphorylation and sustained signaling. Our study provides the underpinnings of a PI3K?-mediated regulation of PP2A activity that has significant consequences on receptor function with broad implications in cellular signaling. | lld:pubmed |
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| pubmed-article:21419339 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:21419339 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:21419339 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21419339 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:21419339 | pubmed:issn | 1097-4164 | lld:pubmed |
| pubmed-article:21419339 | pubmed:author | pubmed-author:Naga... | lld:pubmed |
| pubmed-article:21419339 | pubmed:author | pubmed-author:GuptaManveen... | lld:pubmed |
| pubmed-article:21419339 | pubmed:author | pubmed-author:MohanMaraduma... | lld:pubmed |
| pubmed-article:21419339 | pubmed:author | pubmed-author:VasudevanNeel... | lld:pubmed |
| pubmed-article:21419339 | pubmed:author | pubmed-author:HussainAfshan... | lld:pubmed |
| pubmed-article:21419339 | pubmed:copyrightInfo | Copyright © 2011 Elsevier Inc. All rights reserved. | lld:pubmed |
| pubmed-article:21419339 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21419339 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:21419339 | pubmed:volume | 41 | lld:pubmed |
| pubmed-article:21419339 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21419339 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21419339 | pubmed:pagination | 636-48 | lld:pubmed |
| pubmed-article:21419339 | pubmed:dateRevised | 2011-9-26 | lld:pubmed |
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| pubmed-article:21419339 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21419339 | pubmed:articleTitle | Inhibition of protein phosphatase 2A activity by PI3K? regulates ?-adrenergic receptor function. | lld:pubmed |
| pubmed-article:21419339 | pubmed:affiliation | Department of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, OH 44195, USA. | lld:pubmed |
| pubmed-article:21419339 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21419339 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:21419339 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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