| pubmed-article:16919458 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16919458 | lifeskim:mentions | umls-concept:C0285558 | lld:lifeskim |
| pubmed-article:16919458 | lifeskim:mentions | umls-concept:C1705328 | lld:lifeskim |
| pubmed-article:16919458 | lifeskim:mentions | umls-concept:C1705341 | lld:lifeskim |
| pubmed-article:16919458 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:16919458 | lifeskim:mentions | umls-concept:C0597298 | lld:lifeskim |
| pubmed-article:16919458 | lifeskim:mentions | umls-concept:C0812228 | lld:lifeskim |
| pubmed-article:16919458 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:16919458 | pubmed:dateCreated | 2006-9-18 | lld:pubmed |
| pubmed-article:16919458 | pubmed:abstractText | The mammalian target of rapamycin (mTOR) is a serine/threonine kinase that participates in at least two distinct multiprotein complexes, mTORC1 and mTORC2 . These complexes play important roles in the regulation of cell growth, proliferation, survival, and metabolism. mTORC2 is a hydrophobic motif kinase for the cell-survival protein Akt/PKB and, here, we identify mSin1 as a component of mTORC2 but not mTORC1. mSin1 is necessary for the assembly of mTORC2 and for its capacity to phosphorylate Akt/PKB. Alternative splicing generates at least five isoforms of the mSin1 protein , three of which assemble into mTORC2 to generate three distinct mTORC2s. Even though all mTORC2s can phosphorylate Akt/PKB in vitro, insulin regulates the activity of only two of them. Thus, we propose that cells contain several mTORC2 flavors that may phosphorylate Akt/PKB in response to different signals. | lld:pubmed |
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| pubmed-article:16919458 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16919458 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16919458 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16919458 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16919458 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:16919458 | pubmed:issn | 0960-9822 | lld:pubmed |
| pubmed-article:16919458 | pubmed:author | pubmed-author:SabatiniDavid... | lld:pubmed |
| pubmed-article:16919458 | pubmed:author | pubmed-author:CarrSteven... | lld:pubmed |
| pubmed-article:16919458 | pubmed:author | pubmed-author:ThoreenCarson... | lld:pubmed |
| pubmed-article:16919458 | pubmed:author | pubmed-author:SculleyTomT | lld:pubmed |
| pubmed-article:16919458 | pubmed:author | pubmed-author:JaffeJacob... | lld:pubmed |
| pubmed-article:16919458 | pubmed:author | pubmed-author:SchroderWayne... | lld:pubmed |
| pubmed-article:16919458 | pubmed:author | pubmed-author:FriasMaria... | lld:pubmed |
| pubmed-article:16919458 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16919458 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:16919458 | pubmed:volume | 16 | lld:pubmed |
| pubmed-article:16919458 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16919458 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16919458 | pubmed:pagination | 1865-70 | lld:pubmed |
| pubmed-article:16919458 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:16919458 | pubmed:meshHeading | pubmed-meshheading:16919458... | lld:pubmed |
| pubmed-article:16919458 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16919458 | pubmed:articleTitle | mSin1 is necessary for Akt/PKB phosphorylation, and its isoforms define three distinct mTORC2s. | lld:pubmed |
| pubmed-article:16919458 | pubmed:affiliation | Whitehead Institute for Biomedical Research and Department of Biology, Massachusetts Institute of Technology, Nine Cambridge Center, Cambridge, Massachusetts 02142, USA. | lld:pubmed |
| pubmed-article:16919458 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16919458 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16919458 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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