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
1994
The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells
Chong L, Traynor-Kaplan A, Bokoch G, Schwartz M. The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells. Cell 1994, 79: 507-513. PMID: 7954816, DOI: 10.1016/0092-8674(94)90259-3.Peer-Reviewed Original ResearchMeSH KeywordsADP Ribose TransferasesAnimalsBotulinum ToxinsCalciumCell AdhesionCells, CulturedDrosophila ProteinsFibroblastsGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)IntegrinsLovastatinMembrane ProteinsMiceMicroinjectionsPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol PhosphatesPhosphotransferases (Alcohol Group Acceptor)Platelet-Derived Growth FactorRecombinant ProteinsSignal TransductionThrombinConceptsPlatelet-derived growth factorBotulinum C3 exoenzymeSmall GTPPIP2 synthesisC3 exoenzymePIP2 hydrolysisProduction of phosphatidylinositolIntegrin-mediated adhesionEffects of RhoTreatment of cellsCalcium mobilizationActin cytoskeletonDiminished calcium mobilizationMammalian cellsProtein RhoPIP2 levelsCell lysatesGTP gamma SGTPRhoPhosphatidylinositolExoenzymeGamma SGrowth factorNonadherent cells
1992
Adhesion is required for protein kinase C-dependent activation of the Na+/H+ antiporter by platelet-derived growth factor.
Schwartz M, Lechene C. Adhesion is required for protein kinase C-dependent activation of the Na+/H+ antiporter by platelet-derived growth factor. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 6138-6141. PMID: 1378621, PMCID: PMC402137, DOI: 10.1073/pnas.89.13.6138.Peer-Reviewed Original ResearchMeSH KeywordsAcid-Base EquilibriumAnimalsCarrier ProteinsCell AdhesionCells, CulturedExtracellular MatrixHydrogen-Ion ConcentrationIn Vitro TechniquesMiceNaphthalenesPlatelet-Derived Growth FactorPolycyclic CompoundsProtein Kinase CSignal TransductionSodium-Hydrogen ExchangersTetradecanoylphorbol AcetateConceptsProtein kinase CPlatelet-derived growth factorKinase CAdherent cellsGrowth factorExtracellular matrix proteinsPKC-dependent pathwayElevation of intracellularMatrix proteinsAnchorage-dependent cellsCell adhesionDependent activationPKC activationAntiporterPhorbol esterSolid substratumPharmacological inhibitionC3H 10T1/2 cellsCellsActivationPathwayIntracellular pHAdhesionProteinIntegrins