2006
In Vivo Dynamics of Rac-Membrane Interactions
Moissoglu K, Slepchenko BM, Meller N, Horwitz AF, Schwartz MA. In Vivo Dynamics of Rac-Membrane Interactions. Molecular Biology Of The Cell 2006, 17: 2770-2779. PMID: 16597700, PMCID: PMC1474787, DOI: 10.1091/mbc.e06-01-0005.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAnimalsCell MembraneComputer SimulationDiffusionGenes, ReporterGuanine Nucleotide Dissociation InhibitorsKineticsMiceMicroscopy, ConfocalModels, TheoreticalPlasmidsProtein TransportRac GTP-Binding ProteinsRecombinant Fusion ProteinsRecombinant ProteinsRho-Specific Guanine Nucleotide Dissociation InhibitorsConceptsGuanine Nucleotide Dissociation InhibitorGTPase-activating proteinsGTP-RacNucleotide exchange factorsVivo dynamicsSmall hairpin RNADissociation inhibitorMembrane associationExchange factorRac functionGEF Tiam1Hairpin RNARhoGDIPhotobleaching methodRacCytosolOverexpressionMajor routeDissociation rate constantsTiam1RNAProteinDetectable rateMembraneActivation
2002
Zizimin1, a novel Cdc42 activator, reveals a new GEF domain for Rho proteins
Meller N, Irani-Tehrani M, Kiosses WB, Del Pozo MA, Schwartz MA. Zizimin1, a novel Cdc42 activator, reveals a new GEF domain for Rho proteins. Nature Cell Biology 2002, 4: 639-647. PMID: 12172552, DOI: 10.1038/ncb835.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAmino Acid SequenceAnimalsBinding SitesCdc42 GTP-Binding ProteinCloning, MolecularEnzyme ActivationGuanine Nucleotide Exchange FactorsHumansMiceMolecular Sequence DataProtein Structure, TertiaryRho GTP-Binding ProteinsRNA, MessengerSequence Homology, Amino AcidTissue DistributionConceptsGuanine nucleotide exchange factorsCdc42 activatorGEF domainRho family GTPases RacNucleotide exchange factorsCDM proteinsRho proteinsRho familyGTPases RacNew superfamilySequence comparisonCdc42 activationNew proteinsMutational analysisGene expressionBiochemical searchCell migrationProteinDirect interactionCdc42Zizimin1RacActivatorGTPasesDomainIntegrins regulate GTP-Rac localized effector interactions through dissociation of Rho-GDI
Del Pozo MA, Kiosses WB, Alderson NB, Meller N, Hahn KM, Schwartz MA. Integrins regulate GTP-Rac localized effector interactions through dissociation of Rho-GDI. Nature Cell Biology 2002, 4: 232-239. PMID: 11862216, DOI: 10.1038/ncb759.Peer-Reviewed Original Research
2001
Timing of cyclin D1 expression within G1 phase is controlled by Rho
Welsh C, Roovers K, Villanueva J, Liu Y, Schwartz M, Assoian R. Timing of cyclin D1 expression within G1 phase is controlled by Rho. Nature Cell Biology 2001, 3: 950-957. PMID: 11715015, DOI: 10.1038/ncb1101-950.Peer-Reviewed Original Research
2000
Localized Rac Activation Dynamics Visualized in Living Cells
Kraynov V, Chamberlain C, Bokoch G, Schwartz M, Slabaugh S, Hahn K. Localized Rac Activation Dynamics Visualized in Living Cells. Science 2000, 290: 333-337. PMID: 11030651, DOI: 10.1126/science.290.5490.333.Peer-Reviewed Original ResearchConceptsSmall guanosine triphosphatasesSpatio-temporal controlMembrane rufflesGuanosine triphosphatasesSubcellular localizationNucleotide stateRac activationProtein activityDownstream targetsMotile cellsLiving cellsSpatial controlSpatio-temporal dynamicsGradient of activationCellsActivation dynamicsActivationRufflesTriphosphatasesPrecise spatial controlProteinRacLeading edgeApplicable approachLocalized effectDeath Effector Domain Protein PEA-15 Potentiates Ras Activation of Extracellular Signal Receptor-activated Kinase by an Adhesion-independent Mechanism
Ramos J, Hughes P, Renshaw M, Schwartz M, Formstecher E, Chneiweiss H, Ginsberg M. Death Effector Domain Protein PEA-15 Potentiates Ras Activation of Extracellular Signal Receptor-activated Kinase by an Adhesion-independent Mechanism. Molecular Biology Of The Cell 2000, 11: 2863-2872. PMID: 10982386, PMCID: PMC14961, DOI: 10.1091/mbc.11.9.2863.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAnimalsApoptosis Regulatory ProteinsCell AdhesionCell LineCHO CellsCricetinaeEnzyme ActivationGuanosine TriphosphateHumansIntracellular Signaling Peptides and ProteinsJNK Mitogen-Activated Protein KinasesMAP Kinase Kinase Kinase 1MiceMitogen-Activated Protein KinasesP38 Mitogen-Activated Protein KinasesPhosphoproteinsProtein Serine-Threonine KinasesRas ProteinsRecombinant Fusion ProteinsSignal TransductionConceptsPEA-15 expressionPEA-15ERK activationMitogen-activated protein kinase kinaseMitogen-activated protein kinase pathwayAdhesion-independent mechanismsRas-dependent mannerProtein kinase kinaseRegulation of apoptosisProtein kinase pathwayChinese hamster ovary cellsRas guanosineKinase kinaseRas activationSignal receptorHamster ovary cellsH-RasKinase pathwayERK activityIntegrin activationERK signalingAnchorage dependenceOncogenic processesOvary cellsApoptosisStimulation of Fascin Spikes by Thrombospondin-1 Is Mediated by the Gtpases Rac and Cdc42
Adams J, Schwartz M. Stimulation of Fascin Spikes by Thrombospondin-1 Is Mediated by the Gtpases Rac and Cdc42. Journal Of Cell Biology 2000, 150: 807-822. PMID: 10953005, PMCID: PMC2175285, DOI: 10.1083/jcb.150.4.807.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsActinsAnimalsBridged Bicyclo Compounds, HeterocyclicCarrier ProteinsCdc42 GTP-Binding ProteinCell AdhesionCell LineDepsipeptidesFibronectinsMiceMicrofilament ProteinsMuscle, SkeletalPeptides, CyclicRac GTP-Binding ProteinsRecombinant ProteinsStress, MechanicalThiazolesThiazolidinesThrombospondin 1TransfectionVinculinConceptsActin cytoskeletal organizationCytoskeletal organizationThrombospondin-1Matrix glycoprotein thrombospondin-1Actin-bundling protein fascinRho family GTPasesF-actin turnoverDominant-negative RacLocalization of fascinF-actin microspikesCell migration responseMotility of cellsGlycoprotein thrombospondin-1GTPases RacImportant physiological stimulusActive mutantComponent downstreamProtein fascinCdc42C2C12 myoblastsCell adhesionCell migrationBiochemical assaysExtracellular matrixProlonged activationThe c-Abl tyrosine kinase contributes to the transient activation of MAP kinase in cells plated on fibronectin
Renshaw M, Lewis J, Schwartz M. The c-Abl tyrosine kinase contributes to the transient activation of MAP kinase in cells plated on fibronectin. Oncogene 2000, 19: 3216-3219. PMID: 10918577, DOI: 10.1038/sj.onc.1203667.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAdaptor Proteins, Signal TransducingAnimalsCell Culture TechniquesEnzyme ActivationFibronectinsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesGRB2 Adaptor ProteinMAP Kinase Signaling SystemMiceMitogen-Activated Protein Kinase 1Mitogen-Activated Protein KinasesProteinsProtein-Tyrosine KinasesProto-Oncogene Proteins c-abl
1999
Focal Adhesion Kinase Mediates the Integrin Signaling Requirement for Growth Factor Activation of Map Kinase
Renshaw M, Price L, Schwartz M. Focal Adhesion Kinase Mediates the Integrin Signaling Requirement for Growth Factor Activation of Map Kinase. Journal Of Cell Biology 1999, 147: 611-618. PMID: 10545504, PMCID: PMC2151196, DOI: 10.1083/jcb.147.3.611.Peer-Reviewed Original Research3T3 CellsAnimalsCell AdhesionCell Adhesion MoleculesCell DivisionCell Line, TransformedCell Transformation, NeoplasticEnzyme ActivationFibroblastsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesGene DeletionGenes, DominantGrowth SubstancesIntegrin beta1MiceMitogen-Activated Protein Kinase 1Oncogene Protein pp60(v-src)Protein-Tyrosine KinasesRas ProteinsRecombinant Fusion ProteinsSignal TransductionTransfectionRegulation of the small GTP‐binding protein Rho by cell adhesion and the cytoskeleton
Ren X, Kiosses W, Alexander Schwartz M. Regulation of the small GTP‐binding protein Rho by cell adhesion and the cytoskeleton. The EMBO Journal 1999, 18: 578-585. PMID: 9927417, PMCID: PMC1171150, DOI: 10.1093/emboj/18.3.578.Peer-Reviewed Original ResearchConceptsFocal adhesionsRho activationRho activityExtracellular matrixSmall GTPProtein RhoLysophosphatidic acidStress fibersCell adhesionRho-dependent mannerActin stress fibersHigh Rho activitySwiss 3T3 cellsNegative feedback loopAdherent cellsCytoskeletal structuresSoluble factorsCytochalasin DRhoGTPPresence of serumCellsActivationRegulationAdhesion
1998
An activated Rac mutant functions as a dominant negative for membrane ruffling
Schwartz M, Meredith J, Kiosses W. An activated Rac mutant functions as a dominant negative for membrane ruffling. Oncogene 1998, 17: 625-629. PMID: 9704928, DOI: 10.1038/sj.onc.1201977.Peer-Reviewed Original ResearchActivation of Rac and Cdc42 by Integrins Mediates Cell Spreading
Price L, Leng J, Schwartz M, Bokoch G. Activation of Rac and Cdc42 by Integrins Mediates Cell Spreading. Molecular Biology Of The Cell 1998, 9: 1863-1871. PMID: 9658176, PMCID: PMC25428, DOI: 10.1091/mbc.9.7.1863.Peer-Reviewed Original Research
1997
Growth factor activation of MAP kinase requires cell adhesion
Renshaw M, Ren X, Schwartz M. Growth factor activation of MAP kinase requires cell adhesion. The EMBO Journal 1997, 16: 5592-5599. PMID: 9312018, PMCID: PMC1170191, DOI: 10.1093/emboj/16.18.5592.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAnimalsCalcium-Calmodulin-Dependent Protein KinasesCell AdhesionCell Transformation, NeoplasticEnzyme ActivationExtracellular Matrix ProteinsGenes, rasKineticsMAP Kinase Kinase Kinase 1MiceMitogen-Activated Protein Kinase 1Platelet-Derived Growth FactorProtein Serine-Threonine KinasesProto-Oncogene Proteins c-rafProto-OncogenesConceptsCell adhesionGrowth factor-regulated pathwaysMAP kinase ERK2Mutants of RasActivation of ERK2MAP kinase pathwayRas-transformed cellsGrowth factor activationExtracellular matrix proteinsSoluble growth factorsAnchorage-independent growthKinase ERK2Growth factorMAP kinaseOncogenic growthEndogenous RasKinase pathwayOncogenic activationMEK activityMatrix proteinsMajor regulatorERK2Factor activationRafMEK
1996
Integrin regulation of c-Abl tyrosine kinase activity and cytoplasmic–nuclear transport
Lewis J, Baskaran R, Taagepera S, Schwartz M, Wang J. Integrin regulation of c-Abl tyrosine kinase activity and cytoplasmic–nuclear transport. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 15174-15179. PMID: 8986783, PMCID: PMC26376, DOI: 10.1073/pnas.93.26.15174.Peer-Reviewed Original ResearchConceptsNuclear c-AblC-AblKinase activityC-Abl tyrosine kinase activityTyrosine kinaseCell adhesionCell cycle signalsCytoplasmic-nuclear transportExtracellular matrix protein fibronectinNonreceptor tyrosine kinaseCytoplasmic c-AblC-Abl activationC-Abl activityMatrix protein fibronectinTyrosine kinase activityC-abl protooncogeneMin of adhesionIntegrin regulationSubcellular localizationIntegrin signalsFocal contactsCytoplasmic poolTransient recruitmentSubcellular distributionProtein fibronectinTransformation 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 resultsAnchoragePhysical association of the small GTPase Rho with a 68-kDa phosphatidylinositol 4-phosphate 5-kinase in Swiss 3T3 cells.
Ren X, Bokoch G, Traynor-Kaplan A, Jenkins G, Anderson R, Schwartz M. Physical association of the small GTPase Rho with a 68-kDa phosphatidylinositol 4-phosphate 5-kinase in Swiss 3T3 cells. Molecular Biology Of The Cell 1996, 7: 435-442. PMID: 8868471, PMCID: PMC275895, DOI: 10.1091/mbc.7.3.435.Peer-Reviewed Original Research
1995
Mapping in vivo associations of cytoplasmic proteins with integrin beta 1 cytoplasmic domain mutants.
Lewis J, Schwartz M. Mapping in vivo associations of cytoplasmic proteins with integrin beta 1 cytoplasmic domain mutants. Molecular Biology Of The Cell 1995, 6: 151-160. PMID: 7540435, PMCID: PMC275825, DOI: 10.1091/mbc.6.2.151.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsActininAmino Acid SequenceAnimalsBinding SitesCell Adhesion MoleculesChickensCytoplasmCytoskeletal ProteinsFluorescent Antibody TechniqueFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesIntegrin beta1IntegrinsMacromolecular SubstancesMiceMolecular Sequence DataMutagenesisProtein-Tyrosine KinasesRecombinant ProteinsSequence DeletionTalinVinculinConceptsFocal adhesion kinaseBeta 1 integrinC-terminusCytoplasmic proteinsF-actinMutant beta 1Entire cytoplasmic domainCytoplasmic domain mutantsSpecific cytoskeletal proteinsBeta 1Wild-type integrinCultured mouse fibroblastsBeta 1 integrin subunitActin cytoskeletonFocal adhesionsCytoplasmic domainDomain mutantsAdhesion kinaseAlpha-actininTrigger intracellularVivo associationCytoskeletal proteinsTalinFocal contactsAmino acids