2004
Integrins Regulate Rac Targeting by Internalization of Membrane Domains
del Pozo MA, Alderson NB, Kiosses WB, Chiang HH, Anderson RG, Schwartz MA. Integrins Regulate Rac Targeting by Internalization of Membrane Domains. Science 2004, 303: 839-842. PMID: 14764880, DOI: 10.1126/science.1092571.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding SitesCell AdhesionCell LineCell MembraneCells, CulturedCholera ToxinCholesterolG(M1) GangliosideGlycosylphosphatidylinositolsGuanosine TriphosphateHumansIntegrin beta1IntegrinsLiposomesMembrane MicrodomainsMiceNIH 3T3 CellsRac1 GTP-Binding ProteinRatsRecombinant Fusion ProteinsSignal TransductionTransfectionConceptsMembrane domainsLipid raftsLipid raft markersPlasma membrane cholesterolCholesterol-rich membranesCell plasma membraneMembrane targetingAdhesion of cellsSmall GTPRaft markersIntegrin signalsPlasma membraneDownstream effectorsEffector activationMembrane lipidsMembrane cholesterolAnchorage-dependent cellsExtracellular matrixCell detachmentNonadherent cellsInternalizationRaftsCellsTargetingMembrane
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 cellsApoptosisAdhesion to the extracellular matrix regulates the coupling of the small GTPase Rac to its effector PAK
del Pozo M, Price L, Alderson N, Ren X, Schwartz M. Adhesion to the extracellular matrix regulates the coupling of the small GTPase Rac to its effector PAK. The EMBO Journal 2000, 19: 2008-2014. PMID: 10790367, PMCID: PMC305684, DOI: 10.1093/emboj/19.9.2008.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiological TransportCdc42 GTP-Binding ProteinCell AdhesionCell LineCell MembraneCulture Media, Serum-FreeCytoplasmEnzyme ActivationExtracellular MatrixFibronectinsGrowth SubstancesGuanosine TriphosphateIntegrinsMiceMutationMyristic AcidP21-Activated KinasesProtein BindingProtein Serine-Threonine KinasesRac GTP-Binding ProteinsRatsRecombinant Fusion ProteinsTransfectionConceptsSmall GTPase RacExtracellular matrixGTPase RacEffector PAKMembrane-targeting sequenceCell cycle progressionAbility of RacSoluble growth factorsAdherent cellsRac mutantGrowth factorCytoskeletal organizationPAK activationOncogenic transformationGene expressionCycle progressionMembrane fractionCell adhesionNon-adherent cellsRacPAKMembraneCellsAdhesionActivationDetermination of GTP loading on Rho
Ren X, Schwartz M. Determination of GTP loading on Rho. Methods In Enzymology 2000, 325: 264-272. PMID: 11036609, DOI: 10.1016/s0076-6879(00)25448-7.Peer-Reviewed Original ResearchConceptsRho-binding domainGTP-RhoLow molecular weight GTPaseAffinity precipitation assaysActin cytoskeleton organizationGTP loadingCytoskeleton organizationWeight GTPaseGTPase activityRho effectorCell lysatesGTPaseRhoPrecipitation assaysTRBDWestern immunoblottingDomainQuality controlPositive controlAssaysRhotekinEffectorsProtein
1999
Regulation 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