2014
Targeting aPKC disables oncogenic signaling by both the EGFR and the proinflammatory cytokine TNFα in glioblastoma
Kusne Y, Carrera-Silva EA, Perry AS, Rushing EJ, Mandell EK, Dietrich JD, Errasti AE, Gibbs D, Berens ME, Loftus JC, Hulme C, Yang W, Lu Z, Aldape K, Sanai N, Rothlin CV, Ghosh S. Targeting aPKC disables oncogenic signaling by both the EGFR and the proinflammatory cytokine TNFα in glioblastoma. Science Signaling 2014, 7: ra75. PMID: 25118327, PMCID: PMC4486020, DOI: 10.1126/scisignal.2005196.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCarcinogenesisDrug Delivery SystemsEnzyme-Linked Immunosorbent AssayEpidermal Growth FactorErbB ReceptorsErlotinib HydrochlorideFlow CytometryFluorescent Antibody TechniqueGlioblastomaHumansImmunoblottingImmunohistochemistryImmunoprecipitationKaplan-Meier EstimateMiceNF-kappa BParacrine CommunicationProtein Kinase CQuinazolinesReverse Transcriptase Polymerase Chain ReactionSignal TransductionTumor Necrosis Factor-alphaConceptsAtypical protein kinase CEpidermal growth factor receptorEGFR kinase inhibitorsHuman glioblastoma tumor cellsReceptor tyrosine kinasesProtein kinase CTNFα-dependent activationKinase inhibitorsTranscription factor nuclear factor κBGlioblastoma tumor cellsGrowth factor receptorKinase activityMolecular approachesTyrosine kinaseKinase CNuclear factor κBFactor receptorGlioblastoma microenvironmentFactor κBProinflammatory cytokine TNFαAbundanceTumor necrosis factorGlioblastoma therapyTumor growthGrade IV glioblastomaThe PAR complex controls the spatiotemporal dynamics of F-actin and the MTOC in directionally migrating leukocytes
Crespo CL, Vernieri C, Keller PJ, Garrè M, Bender JR, Wittbrodt J, Pardi R. The PAR complex controls the spatiotemporal dynamics of F-actin and the MTOC in directionally migrating leukocytes. Journal Of Cell Science 2014, 127: 4381-4395. PMID: 25179599, PMCID: PMC4197085, DOI: 10.1242/jcs.146217.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActinsAdaptor Proteins, Signal TransducingAnimalsAnimals, Genetically ModifiedCarrier ProteinsCell MovementCell PolarityCells, CulturedLeukocytesMicrotubule-Organizing CenterMultiprotein ComplexesMutationOryziasProtein Kinase CProtein Transportrho-Associated KinasesZebrafishZebrafish ProteinsConceptsAtypical protein kinase CMicrotubule organizing centerPAR-6Par complexPAR-3Protein kinase CRegulated interactionFish larvaeMyeloid cellsGenetic manipulationPolarizing cuesKinase activationCytoskeletal changesF-actinKinase COrganizing centerFunctional polarizationRho kinase activationThree-dimensional environmentTraction forceCellsSpatiotemporal dynamicsLeukocyte migrationMigrationComplexes
2013
Competing molecular interactions of aPKC isoforms regulate neuronal polarity
Parker SS, Mandell EK, Hapak SM, Maskaykina IY, Kusne Y, Kim JY, Moy JK, St. John PA, Wilson JM, Gothard KM, Price TJ, Ghosh S. Competing molecular interactions of aPKC isoforms regulate neuronal polarity. Proceedings Of The National Academy Of Sciences Of The United States Of America 2013, 110: 14450-14455. PMID: 23940317, PMCID: PMC3761571, DOI: 10.1073/pnas.1301588110.Peer-Reviewed Original ResearchConceptsAtypical protein kinase CNeuronal polarityAPKC isoformsProtein kinase CCell polarityPolarized neuronsAlternative transcriptsKinase CPar3Supernumerary axonsIsoformsEmbryonic hippocampal neuronsMolecular interactionsOverexpressionPresumptive axonsMolecular modelHippocampal neuronsPolarityPKMTranscriptsRegulatorIntermolecular competitionInteractsNeuronsDisruptsRap1 and Canoe/afadin are essential for establishment of apical–basal polarity in the Drosophila embryo
Choi W, Harris NJ, Sumigray KD, Peifer M. Rap1 and Canoe/afadin are essential for establishment of apical–basal polarity in the Drosophila embryo. Molecular Biology Of The Cell 2013, 24: 945-963. PMID: 23363604, PMCID: PMC3608504, DOI: 10.1091/mbc.e12-10-0736.Peer-Reviewed Original ResearchMeSH KeywordsAdherens JunctionsAnimalsCell LineCell PolarityCell ShapeCytoskeletonDrosophila melanogasterDrosophila ProteinsEmbryo, NonmammalianGreen Fluorescent ProteinsIntracellular Signaling Peptides and ProteinsMicroscopy, ConfocalModels, BiologicalMutationProtein Kinase Crap1 GTP-Binding ProteinsRNA InterferenceConceptsAtypical protein kinase CCanoe/AfadinPolarity establishmentPolarity cuesDrosophila embryosAdherens junctionsApical-basal cell polarityBazooka/Par3Apical-basal polarityAbsence of Rap1Columnar cell shapeSmall GTPase Rap1Protein kinase CCell polarityBazookaGTPase Rap1Protein networkRap1Cell shapeLinear pathwaySuperb modelKinase COrgan architectureAfadinCytoskeleton
2007
Par3 functions in the biogenesis of the primary cilium in polarized epithelial cells
Sfakianos J, Togawa A, Maday S, Hull M, Pypaert M, Cantley L, Toomre D, Mellman I. Par3 functions in the biogenesis of the primary cilium in polarized epithelial cells. Journal Of Cell Biology 2007, 179: 1133-1140. PMID: 18070914, PMCID: PMC2140027, DOI: 10.1083/jcb.200709111.Peer-Reviewed Original ResearchConceptsPrimary ciliaAtypical protein kinase CIntraflagellar transport particlesBasolateral membrane domainsMicrotubule-dependent transportProtein kinase CEpithelial cellsMembrane biogenesisPDZ proteinsMembrane domainsMembrane proteinsPar complexMicrotubule motorsCiliary membraneVectorial movementPar3 functionsKinesin-2Kinase CPar3Additional roleJunctional complexesCrumbs3Apical surfaceBiogenesisCilia
2003
Molecular Mechanisms of Insulin Resistance in IRS-2-Deficient Hepatocytes
Valverde A, Burks D, Fabregat I, Fisher T, Carretero J, White M, Benito M. Molecular Mechanisms of Insulin Resistance in IRS-2-Deficient Hepatocytes. Diabetes 2003, 52: 2239-2248. PMID: 12941762, DOI: 10.2337/diabetes.52.9.2239.Peer-Reviewed Original ResearchMeSH KeywordsAdenoviridaeAnimalsAnimals, NewbornAntigens, Polyomavirus TransformingCell Line, TransformedFemaleForkhead Box Protein O1Forkhead Transcription FactorsGluconeogenesisGlucose-6-PhosphataseGlycogen SynthaseGlycogen Synthase Kinase 3HepatocytesHypoglycemic AgentsInsulinInsulin Receptor Substrate ProteinsInsulin ResistanceIntracellular Signaling Peptides and ProteinsIsoenzymesMaleMiceMice, Mutant StrainsPhosphatidylinositol 3-KinasesPhosphatidylinositol PhosphatesPhosphoenolpyruvate Carboxykinase (GTP)PhosphoproteinsPregnancyProtein Kinase CProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktRetroviridaeSignal TransductionTranscription FactorsConceptsGluconeogenic gene expressionIRS-2Gene expressionPrimary hepatocytesAtypical protein kinase CIRS-1-associated phosphatidylinositolIRS-1 tyrosine phosphorylationInsulin-induced phosphatidylinositolTranslocation of phosphatidylinositolInsulin receptor substrateGlycogen synthase kinaseProtein kinase CActivation of AktDownstream phosphatidylinositolTyrosine phosphorylationPlasma membraneReceptor substrateGlycogen synthase activityMolecular mechanismsSynthase kinaseInsulin stimulationKinase CHepatocyte cell linePhosphatidylinositolFunctional insulin
1999
p70 S6 Kinase Is Regulated by Protein Kinase Cζ and Participates in a Phosphoinositide 3-Kinase-Regulated Signalling Complex
Romanelli A, Martin K, Toker A, Blenis J. p70 S6 Kinase Is Regulated by Protein Kinase Cζ and Participates in a Phosphoinositide 3-Kinase-Regulated Signalling Complex. Molecular And Cellular Biology 1999, 19: 2921-2928. PMID: 10082559, PMCID: PMC84086, DOI: 10.1128/mcb.19.4.2921.Peer-Reviewed Original ResearchConceptsP70 S6 kinasePDK-1Protein kinase CS6 kinaseGrowth factor-independent mannerK activationPhosphoinositide-dependent kinase 1Atypical protein kinase CC-terminal truncation mutantsPDK-1 activationProtein kinase CζFactor-independent mannerThreonine 389Pseudosubstrate domainSignaling ComplexGrowth factorSequential phosphorylationTruncation mutantsCoexpression experimentsEpidermal growth factorCatalytic loopUpstream regulatorKinase 1PKC isoformsKinase C
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