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dc.contributor.authorBoulbes, Delphine
dc.contributor.authorChen, Chien-Hung
dc.contributor.authorShaikenov, Tattym
dc.contributor.authorAgarwal, Nitin K.
dc.contributor.authorPeterson, Timothy R.
dc.contributor.authorAddona, Terri A.
dc.contributor.authorKeshishian, Hasmik
dc.contributor.authorCarr, Steven A.
dc.contributor.authorMagnuson, Mark A.
dc.contributor.authorSabatini, David M.
dc.contributor.authorSarbassov, Dos D.
dc.date.accessioned2012-11-01T17:08:38Z
dc.date.available2012-11-01T17:08:38Z
dc.date.issued2010-05
dc.identifier.issn1541-7786
dc.identifier.issn1557-3125
dc.identifier.urihttp://hdl.handle.net/1721.1/74546
dc.descriptionavailable in PMC 2012 January 1.en_US
dc.description.abstractIn animal cells, growth factors coordinate cell proliferation and survival by regulating the phosphoinositide 3-kinase/Akt signaling pathway. Deregulation of this signaling pathway is common in a variety of human cancers. The PI3K-dependent signaling kinase complex defined as mammalian target of rapamycin complex 2 (mTORC2) functions as a regulatory Ser-473 kinase of Akt. We find that activation of mTORC2 by growth factor signaling is linked to the specific phosphorylation of its component rictor on Thr-1135. The phosphorylation of this site is induced by the growth factor stimulation and expression of the oncogenic forms of ras or PI3K. Rictor phosphorylation is sensitive to the inhibition of PI3K, mTOR, or expression of integrin-linked kinase. The substitution of wild-type rictor with its specific phospho-mutants in rictor null mouse embryonic fibroblasts did not alter the growth factor–dependent phosphorylation of Akt, indicating that the rictor Thr-1135 phosphorylation is not critical in the regulation of the mTORC2 kinase activity. We found that this rictor phosphorylation takes place in the mTORC2-deficient cells, suggesting that this modification might play a role in the regulation of not only mTORC2 but also the mTORC2-independent function of rictor. Mol Cancer Res; 8(6); 896–906.en_US
dc.description.sponsorshipUniversity of Texas M.D. Anderson Cancer Center (Fellow Trust fund)en_US
dc.description.sponsorshipAmerican Cancer Society (M.D. Anderson Cancer Center Breast Specialized Programs of Research Excellence (RSG-09-026-01CCG01))en_US
dc.description.sponsorshipNational Institutes of Health (U.S.) (NIH grant CA133522)en_US
dc.description.sponsorshipNational Institutes of Health (U.S.) (NIH grant AI104389)en_US
dc.language.isoen_US
dc.publisherAmerican Association for Cancer Researchen_US
dc.relation.isversionofhttp://dx.doi.org/10.1158/1541-7786.MCR-09-0409en_US
dc.rightsCreative Commons Attribution-Noncommercial-Share Alike 3.0en_US
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/3.0/en_US
dc.sourcePMCen_US
dc.titleRictor Phosphorylation on the THR-1135 Site Does Not Require Mammalian Target of Rapamycin Complex 2en_US
dc.typeArticleen_US
dc.identifier.citationBoulbes, D. et al. “Rictor Phosphorylation on the Thr-1135 Site Does Not Require Mammalian Target of Rapamycin Complex 2.” Molecular Cancer Research 8.6 (2010): 896–906. Web.en_US
dc.contributor.departmentDavid H. Koch Institute for Integrative Cancer Research at MITen_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Biologyen_US
dc.contributor.departmentWhitehead Institute for Biomedical Researchen_US
dc.contributor.mitauthorPeterson, Timothy R.
dc.contributor.mitauthorSabatini, David M.
dc.relation.journalMolecular Cancer Researchen_US
dc.eprint.versionAuthor's final manuscripten_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dspace.orderedauthorsBoulbes, D.; Chen, C.-H.; Shaikenov, T.; Agarwal, N. K.; Peterson, T. R.; Addona, T. A.; Keshishian, H.; Carr, S. A.; Magnuson, M. A.; Sabatini, D. M.; Sarbassov, D. D.en
dc.identifier.orcidhttps://orcid.org/0000-0002-1446-7256
mit.licenseOPEN_ACCESS_POLICYen_US


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