2017
La-related protein 1 (LARP1) repression of TOP mRNA translation is mediated through its cap-binding domain and controlled by an adjacent regulatory region
Philippe L, Vasseur JJ, Debart F, Thoreen CC. La-related protein 1 (LARP1) repression of TOP mRNA translation is mediated through its cap-binding domain and controlled by an adjacent regulatory region. Nucleic Acids Research 2017, 46: gkx1237-. PMID: 29244122, PMCID: PMC5814973, DOI: 10.1093/nar/gkx1237.Peer-Reviewed Original ResearchMeSH KeywordsAutoantigensBase SequenceBinding SitesBinding, CompetitiveCell-Free SystemComputational BiologyEukaryotic Initiation Factor-4FGene Expression RegulationHEK293 CellsHumansMechanistic Target of Rapamycin Complex 1Models, GeneticPolyribosomesProtein BindingProtein BiosynthesisProtein Interaction Domains and MotifsPyrimidinesRibonucleoproteinsRNA, MessengerConceptsTOP mRNA translationAdjacent regulatory regionsMRNA translationCap-binding domainCap structureRegulatory regionsEukaryotic initiation factor 4FMRNA 5' cap structureIntrinsic repressive activityTerminal oligopyrimidine motifsInitiation factor 4FMRNA 5' endsC-terminal halfGrowth-related mRNAsTOP mRNAsRepressive activityTranslation factorsMRNA targetsCoordinated changesGene expressionLARP1Cell growthProtein 1Top sequenceMRNA
2009
An ATP-competitive Mammalian Target of Rapamycin Inhibitor Reveals Rapamycin-resistant Functions of mTORC1*
Thoreen CC, Kang SA, Chang JW, Liu Q, Zhang J, Gao Y, Reichling LJ, Sim T, Sabatini DM, Gray NS. An ATP-competitive Mammalian Target of Rapamycin Inhibitor Reveals Rapamycin-resistant Functions of mTORC1*. Journal Of Biological Chemistry 2009, 284: 8023-8032. PMID: 19150980, PMCID: PMC2658096, DOI: 10.1074/jbc.m900301200.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAdenosine TriphosphateAnimalsAntibiotics, AntineoplasticAutophagyCarrier ProteinsCell Cycle ProteinsCell ProliferationCell SurvivalCells, CulturedDrug Resistance, NeoplasmEukaryotic Initiation FactorsImmunosuppressive AgentsMechanistic Target of Rapamycin Complex 1MiceMice, KnockoutMultienzyme ComplexesMultiprotein ComplexesPhosphoproteinsPhosphorylationPhosphotransferases (Alcohol Group Acceptor)Protein BiosynthesisProteinsRNA CapsSirolimusTOR Serine-Threonine KinasesTranscription FactorsConceptsRapamycin-resistant phosphorylationATP-competitive mammalian targetMammalian targetATP-competitive mTOR inhibitorsCell growthCap-dependent translationImpairs cell growthSuppression of autophagyDistinct complexesRapamycin kinaseCatalytic subunitKinase activityMTORC1 inhibitorMTORC2 inhibitionRapamycinAnti-cancer agentsDirect inhibitorMTOR inhibitorsInhibitorsProliferationMTORC2Torin1KinaseComplexesPhosphorylation
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