2016
ERK and p38 MAPK Activities Determine Sensitivity to PI3K/mTOR Inhibition via Regulation of MYC and YAP
Muranen T, Selfors L, Hwang J, Gallegos L, Coloff J, Thoreen C, Kang S, Sabatini D, Mills G, Brugge J. ERK and p38 MAPK Activities Determine Sensitivity to PI3K/mTOR Inhibition via Regulation of MYC and YAP. Cancer Research 2016, 76: 7168-7180. PMID: 27913436, PMCID: PMC5161652, DOI: 10.1158/0008-5472.can-16-0155.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsBlotting, WesternCell Line, TumorCell ProliferationDrug Resistance, NeoplasmExtracellular Signal-Regulated MAP KinasesFemaleFluorescent Antibody TechniqueHeterograftsHumansMAP Kinase Signaling SystemMiceMice, Inbred NODMicroscopy, ConfocalNeoplasms, ExperimentalP38 Mitogen-Activated Protein KinasesPhosphoinositide-3 Kinase InhibitorsPhosphoproteinsProtein Kinase InhibitorsProto-Oncogene MasProto-Oncogene Proteins c-mycSignal TransductionTOR Serine-Threonine KinasesTranscription FactorsYAP-Signaling ProteinsConceptsPI3K/mTOR inhibitorMTOR inhibitorsTumor cellsPI3K/mTOR pathwayCell-targeted therapiesTranscriptional regulator c-MycPI3K/mTORAnimal tumor modelsUpregulation of MYCChronic inhibitionInhibition of p38Cellular signaling mechanismsTumor growthMTOR pathwayTumor modelAberrant activationTherapyStress kinase p38C-MycKinase p38InhibitionConstitutive ERK activityAttractive targetContext-dependent mechanismsProliferation arrest
2012
A unifying model for mTORC1-mediated regulation of mRNA translation
Thoreen CC, Chantranupong L, Keys HR, Wang T, Gray NS, Sabatini DM. A unifying model for mTORC1-mediated regulation of mRNA translation. Nature 2012, 485: 109-113. PMID: 22552098, PMCID: PMC3347774, DOI: 10.1038/nature11083.Peer-Reviewed Original Research5' Untranslated RegionsAnimalsBase SequenceCell Line, TumorEukaryotic Initiation Factor-4EEukaryotic Initiation Factor-4GGene Expression RegulationHumansMaleMechanistic Target of Rapamycin Complex 1MiceModels, BiologicalMultiprotein ComplexesNaphthyridinesNucleotide MotifsPhosphorylationProstatic NeoplasmsProtein BindingProtein BiosynthesisProteinsRibosomesRNA, MessengerTOR Serine-Threonine Kinases
2006
mSin1 Is Necessary for Akt/PKB Phosphorylation, and Its Isoforms Define Three Distinct mTORC2s
Frias M, Thoreen C, Jaffe J, Schroder W, Sculley T, Carr S, Sabatini D. mSin1 Is Necessary for Akt/PKB Phosphorylation, and Its Isoforms Define Three Distinct mTORC2s. Current Biology 2006, 16: 1865-1870. PMID: 16919458, DOI: 10.1016/j.cub.2006.08.001.Peer-Reviewed Original ResearchConceptsAkt/PKBSerine/threonine kinaseAkt/PKB phosphorylationDistinct multiprotein complexesAssembly of mTORC2Multiprotein complexesThreonine kinaseAlternative splicingPKB phosphorylationMTORC2PKBMammalian targetCell growthMSin1KinaseIsoformsImportant roleSplicingComplexesPhosphorylationRapamycinProteinDifferent signalsRegulationMetabolism