2005
Endothelial cell activation of the smooth muscle cell phosphoinositide 3-kinase/Akt pathway promotes differentiation
Brown D, Rzucidlo E, Merenick B, Wagner R, Martin K, Powell R. Endothelial cell activation of the smooth muscle cell phosphoinositide 3-kinase/Akt pathway promotes differentiation. Journal Of Vascular Surgery 2005, 41: 509-516. PMID: 15838487, DOI: 10.1016/j.jvs.2004.12.024.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAorta, ThoracicCattleCell DifferentiationCells, CulturedCoculture TechniquesEndothelial CellsMuscle, Smooth, VascularMyocytes, Smooth MusclePhenotypePhosphatidylinositol 3-KinasesProtein Serine-Threonine KinasesProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktSignal TransductionConceptsEC/SMCDifferentiated SMC phenotypeSMC phenotypeSMC differentiationSmooth muscle cellsAkt pathwayProtein markersProtein kinase AktAdenoviral overexpressionContractile protein markersDominant-negative AktEndothelial cellsOpposite endothelial cellsBlood vessel developmentRapid Akt phosphorylationPI3K/Akt pathwayMuscle cellsWestern blottingKinase AktAbility of ECsActive AktPhosphoinositide 3Kinase activityMolecular signalsSynthetic phenotype
2004
Deletion of Ribosomal S6 Kinases Does Not Attenuate Pathological, Physiological, or Insulin-Like Growth Factor 1 Receptor-Phosphoinositide 3-Kinase-Induced Cardiac Hypertrophy
McMullen J, Shioi T, Zhang L, Tarnavski O, Sherwood M, Dorfman A, Longnus S, Pende M, Martin K, Blenis J, Thomas G, Izumo S. Deletion of Ribosomal S6 Kinases Does Not Attenuate Pathological, Physiological, or Insulin-Like Growth Factor 1 Receptor-Phosphoinositide 3-Kinase-Induced Cardiac Hypertrophy. Molecular And Cellular Biology 2004, 24: 6231-6240. PMID: 15226426, PMCID: PMC434247, DOI: 10.1128/mcb.24.14.6231-6240.2004.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibiotics, AntineoplasticAortaCardiomegalyFemaleFetusGene Expression Regulation, DevelopmentalMiceMice, KnockoutMice, TransgenicOrgan SizePhosphatidylinositol 3-KinasesPhysical Conditioning, AnimalReceptor, IGF Type 1Ribosomal Protein S6 Kinases, 90-kDaSignal TransductionSirolimusStress, MechanicalSwimmingConceptsRibosomal S6 kinaseS6 kinaseOverexpression of S6K1PI3K mutantCritical downstream effectorRibosomal proteinsTransgenic miceCardiac hypertrophyDownstream effectorsK mutantS6KsGrowth factor pathwaysGenetic relationshipsPathological stressProtein synthesisCritical effectorS6K1K pathwayIGF1 receptorFactor 1Factor pathwayPhysiological stressInsulin-like growth factor-1Physiological stimuliKinase
2000
Ribosomal S6 Kinase 2 Inhibition by a Potent C-terminal Repressor Domain Is Relieved by Mitogen-activated Protein-Extracellular Signal-regulated Kinase Kinase-regulated Phosphorylation*
Martin K, Schalm S, Romanelli A, Keon K, Blenis J. Ribosomal S6 Kinase 2 Inhibition by a Potent C-terminal Repressor Domain Is Relieved by Mitogen-activated Protein-Extracellular Signal-regulated Kinase Kinase-regulated Phosphorylation*. Journal Of Biological Chemistry 2000, 276: 7892-7898. PMID: 11108720, DOI: 10.1074/jbc.m009972200.Peer-Reviewed Original ResearchMeSH KeywordsButadienesCells, CulturedEnzyme ActivationEpidermal Growth FactorHumansIsoenzymesMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein Kinase KinasesMitogen-Activated Protein KinasesNitrilesPhosphatidylinositol 3-KinasesPhosphorylationRibosomal Protein S6 KinasesConceptsNuclear localization signalLocalization signalPhosphorylation sitesProtein kinaseMitogen-activated protein kinase phosphorylation siteC-terminal nuclear localization signalSerine/threonine protein kinaseProtein kinase phosphorylation siteSignal-regulated kinase kinaseRibosomal S6 kinase 2C-terminal phosphorylation sitesC-terminal repressor domainThreonine protein kinaseKinase phosphorylation siteC-terminal motifMitogen-activated protein kinasePhosphorylation site mutationsS6 kinase 2C-terminal domainKinase kinase inhibitor U0126Ribosomal protein S6C-terminal deletionsC-terminal regionKinase inhibitor U0126Site-specific mutationsRegulation of Ribosomal S6 Kinase 2 by Effectors of the Phosphoinositide 3-Kinase Pathway*
Martin K, Schalm S, Richardson C, Romanelli A, Keon K, Blenis J. Regulation of Ribosomal S6 Kinase 2 by Effectors of the Phosphoinositide 3-Kinase Pathway*. Journal Of Biological Chemistry 2000, 276: 7884-7891. PMID: 11108711, DOI: 10.1074/jbc.m006969200.Peer-Reviewed Original ResearchMeSH KeywordsCdc42 GTP-Binding ProteinCells, CulturedHumansIsoenzymesPhosphatidylinositol 3-KinasesProtein Kinase CRibosomal Protein S6 KinasesConceptsProtein kinase CzetaC-terminusPhosphoinositide-dependent kinase 1Ribosomal S6 kinase 2S6 kinase 2PI3K effectorsRibosomal S6 kinaseRibosomal protein S6Agonist-dependent activationS6 kinaseProtein S6Kinase activityKinase 2Kinase 1Translational capacityS6K2Terminal sequencePhysiological roleImportant regulatorRapamycin (mTOR) pathwayMammalian targetS6K1Basal activationTerminusHomolog
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