1996
Transformation by Rho exchange factor oncogenes is mediated by activation of an integrin‐dependent pathway.
Schwartz M, Toksoz D, Khosravi‐Far R. Transformation by Rho exchange factor oncogenes is mediated by activation of an integrin‐dependent pathway. The EMBO Journal 1996, 15: 6525-6530. PMID: 8978679, PMCID: PMC452477, DOI: 10.1002/j.1460-2075.1996.tb01043.x.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsA Kinase Anchor ProteinsAdaptor Proteins, Signal TransducingAnimalsCalciumCell DivisionCell Transformation, NeoplasticGTP-Binding ProteinsGuanine Nucleotide Exchange FactorsIntegrinsKineticsMiceMinor Histocompatibility AntigensModels, BiologicalOncogenesPhosphatidylinositol 4,5-DiphosphateProto-Oncogene ProteinsRetroviridae Proteins, OncogenicRho GTP-Binding ProteinsSignal TransductionThrombinConceptsConstitutive activationCell growthIntegrin signal transductionSmall GTPase RhoIntegrin-dependent pathwaySignal transductionSignaling eventsGrowth factor receptorGTPase RhoSerum-dependent growthAnchorage independenceFactor receptorPathwayOncogeneUncontrolled growthRhoActivationImportant mediatorTumor cellsGrowthTransductionTransmit signalDblGrowth resultsAnchorage
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
1993
Adhesion to fibronectin stimulates inositol lipid synthesis and enhances PDGF-induced inositol lipid breakdown.
McNamee H, Ingber D, Schwartz M. Adhesion to fibronectin stimulates inositol lipid synthesis and enhances PDGF-induced inositol lipid breakdown. Journal Of Cell Biology 1993, 121: 673-678. PMID: 8387531, PMCID: PMC2119575, DOI: 10.1083/jcb.121.3.673.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell AdhesionCell LineFibroblastsFibronectinsMethacrylatesMicePhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol PhosphatesPlatelet-Derived Growth FactorProtein Kinase C