2009
Suppression of RhoG activity is mediated by a syndecan 4–synectin–RhoGDI1 complex and is reversed by PKCα in a Rac1 activation pathway
Elfenbein A, Rhodes JM, Meller J, Schwartz MA, Matsuda M, Simons M. Suppression of RhoG activity is mediated by a syndecan 4–synectin–RhoGDI1 complex and is reversed by PKCα in a Rac1 activation pathway. Journal Of Cell Biology 2009, 186: 75-83. PMID: 19581409, PMCID: PMC2712988, DOI: 10.1083/jcb.200810179.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCarrier ProteinsCluster AnalysisEnzyme ActivationFibroblast Growth Factor 2GTP PhosphohydrolasesGuanine Nucleotide Dissociation InhibitorsHeLa CellsHumansMiceMice, KnockoutModels, BiologicalPhosphorylationPhosphoserineProtein Kinase C-alphaRac1 GTP-Binding ProteinRatsRho GTP-Binding ProteinsRho-Specific Guanine Nucleotide Dissociation InhibitorsSyndecan-4ConceptsFibroblast growth factor-2Polarized activationRac1 activationSmall guanosine triphosphatase Rac1Activation pathwayProtein complexesRac activationPlasma membranePhysiological defectsSyndecan-4RhoGDI1Major regulatorInactive stateGrowth factor 2RhoGRhoG activityProteoglycan receptorsEndothelial migrationTernary complexFactor 2Genetic deletionSynectinRac1PKCalphaActivation
2007
A fluorescence resonance energy transfer activation sensor for Arf6
Hall B, McLean MA, Davis K, Casanova JE, Sligar SG, Schwartz MA. A fluorescence resonance energy transfer activation sensor for Arf6. Analytical Biochemistry 2007, 374: 243-249. PMID: 18162163, PMCID: PMC2277471, DOI: 10.1016/j.ab.2007.11.032.Peer-Reviewed Original ResearchConceptsMembrane targetingPlatelet-derived growth factorARF6 activationFluorescent proteinGreen fluorescent protein derivativesNormal membrane targetingRas family GTPasesDownstream effector proteinsSmall GTPase Arf6Small GTPase activationFluorescent reporter proteinFluorescent protein derivativesEffector proteinsExchange factorGTPase Arf6Effector domainReporter proteinGTPase activationRac activationN-terminusArf6Intact cellsCell migrationNormal regulationProtein
2002
Activation of Rac1 by shear stress in endothelial cells mediates both cytoskeletal reorganization and effects on gene expression
Tzima E, Del Pozo MA, Kiosses WB, Mohamed SA, Li S, Chien S, Schwartz MA. Activation of Rac1 by shear stress in endothelial cells mediates both cytoskeletal reorganization and effects on gene expression. The EMBO Journal 2002, 21: 6791-6800. PMID: 12486000, PMCID: PMC139108, DOI: 10.1093/emboj/cdf688.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCattleCell AdhesionCells, CulturedCytoskeletonDimerizationEnergy TransferEnzyme ActivationGene Expression RegulationGenes, DominantGreen Fluorescent ProteinsGTP PhosphohydrolasesIntercellular Adhesion Molecule-1LeukocytesLuciferasesLuminescent ProteinsMicroscopy, FluorescenceNF-kappa BPlasmidsProtein TransportRac GTP-Binding ProteinsRac1 GTP-Binding ProteinSpectrometry, FluorescenceStress, MechanicalTime FactorsTransfectionConceptsGene expressionFluorescence resonance energy transferSmall GTPase RacActivation of Rac1Endothelial cellsFocal adhesionsCytoskeletal organizationCytoskeletal reorganizationGTPase RacRac1 activationAdhesion receptorsResonance energy transferExtracellular matrixNuclear factor-kappaBNew integrinRac1Hemodynamic shear stressSubsequent expressionFactor-kappaBCell alignmentExpressionUnifying modelHemodynamic forcesCell adhesion molecule-1CellsEffects of cell tension on the small GTPase Rac
Katsumi A, Milanini J, Kiosses WB, del Pozo MA, Kaunas R, Chien S, Hahn KM, Schwartz MA. Effects of cell tension on the small GTPase Rac. Journal Of Cell Biology 2002, 158: 153-164. PMID: 12105187, PMCID: PMC2173027, DOI: 10.1083/jcb.200201105.Peer-Reviewed Original ResearchMeSH KeywordsAmidesAnimalsAzepinesCell LineCell MembraneCell MovementCollagenDose-Response Relationship, DrugEnergy TransferGTP PhosphohydrolasesGuanine Nucleotide Exchange FactorsMicroscopy, FluorescenceMicroscopy, Phase-ContrastMicroscopy, VideoNaphthalenesNeoplasm ProteinsProteinsPseudopodiaPyridinesRac GTP-Binding ProteinsRatsStress, MechanicalTime FactorsT-Lymphoma Invasion and Metastasis-inducing Protein 1Transfection
2000
Cell Adhesion Regulates Ubiquitin-mediated Degradation of the Platelet-derived Growth Factor Receptor β*
Baron V, Schwartz M. Cell Adhesion Regulates Ubiquitin-mediated Degradation of the Platelet-derived Growth Factor Receptor β*. Journal Of Biological Chemistry 2000, 275: 39318-39323. PMID: 11007771, DOI: 10.1074/jbc.m003618200.Peer-Reviewed Original ResearchMeSH KeywordsAdenoviridaeAnimalsBlotting, WesternCell AdhesionCell DivisionCell LineCells, CulturedCysteine EndopeptidasesDose-Response Relationship, DrugDown-RegulationDynaminsEmbryo, MammalianEnzyme InhibitorsFibroblastsFibronectinsGTP PhosphohydrolasesHumansLigandsLysosomesMiceMultienzyme ComplexesPhosphorylationProteasome Endopeptidase ComplexProtein-Tyrosine KinasesReceptors, Platelet-Derived Growth FactorTemperatureTime FactorsTrypsinTyrphostinsUbiquitinsConceptsUbiquitin-dependent pathwayIntegrin-mediated adhesionPlatelet-derived growth factor receptor βPlatelet-derived growth factor receptor betaTyrosine kinase activityGrowth factor receptor βGrowth factor receptor betaProteasome pathwayDetachment of cellsReceptor autophosphorylationKinase activityCellular desensitizationPrimary fibroblastsExtracellular matrixCell detachmentAutophosphorylationProtein levelsCell linesPDGFGrowth factorReceptor betaReceptor βCellsPathwayRecent studies