2010
Myosin II directly binds and inhibits Dbl family guanine nucleotide exchange factors: a possible link to Rho family GTPases
Lee CS, Choi CK, Shin EY, Schwartz MA, Kim EG. Myosin II directly binds and inhibits Dbl family guanine nucleotide exchange factors: a possible link to Rho family GTPases. Journal Of Cell Biology 2010, 190: 663-674. PMID: 20713598, PMCID: PMC2928003, DOI: 10.1083/jcb.201003057.Peer-Reviewed Original ResearchMeSH KeywordsActomyosinAnimalsBinding SitesCdc42 GTP-Binding ProteinCell AdhesionCell MovementEnzyme ActivationGuanine Nucleotide Exchange FactorsHumansJurkat CellsMiceMyosin Type IINIH 3T3 CellsPlatelet-Derived Growth FactorProtein BindingRac1 GTP-Binding ProteinRatsRecombinant Fusion ProteinsRho GTP-Binding ProteinsRho Guanine Nucleotide Exchange FactorsRNA, Small InterferingConceptsFocal complex formationDbl family guanineMyosin IIExchange factorFamily guanineATPase activityNonmuscle myosin IIComplex formationGEF activitySpatiotemporal regulationRho familyCdc42 GTPasesAdhesion dynamicsRho GTPasesCdc42 activationLamellipodial protrusionCell protrusionsActomyosin contractionGEFNIH3T3 fibroblastsFunctional linkCell migrationGTPasesCatalytic siteHomology modulesMatrix-Specific Protein Kinase A Signaling Regulates p21-Activated Kinase Activation by Flow in Endothelial Cells
Funk SD, Yurdagul A, Green JM, Jhaveri KA, Schwartz MA, Orr AW. Matrix-Specific Protein Kinase A Signaling Regulates p21-Activated Kinase Activation by Flow in Endothelial Cells. Circulation Research 2010, 106: 1394-1403. PMID: 20224042, PMCID: PMC2862370, DOI: 10.1161/circresaha.109.210286.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnti-Inflammatory AgentsBasement MembraneCattleCdc42 GTP-Binding ProteinCells, CulturedCyclic AMP-Dependent Protein KinasesEndothelial CellsEnzyme ActivationEnzyme ActivatorsHumansIloprostInflammationInflammation MediatorsInjections, IntraperitonealIntegrinsMaleMechanotransduction, CellularMiceMice, Inbred C57BLNF-kappa BP21-Activated KinasesPhosphorylationProtein Kinase InhibitorsPulsatile FlowRac GTP-Binding ProteinsRegional Blood FlowStress, MechanicalTime FactorsTransfectionConceptsInflammatory gene expressionNF-kappaB activationInflammatory signalingEndothelial cellsProstacyclin analogue iloprostBasement membrane proteinsBlood flow patternsPKA-dependent inhibitionInflammatory pathwaysAnalogue iloprostGene expressionKappaB activationNF-kappaB.Subendothelial extracellular matrixNuclear factorPAK activationBasement membrane
2009
Rho GDP Dissociation Inhibitor 2 Suppresses Metastasis via Unconventional Regulation of RhoGTPases
Moissoglu K, McRoberts KS, Meier JA, Theodorescu D, Schwartz MA. Rho GDP Dissociation Inhibitor 2 Suppresses Metastasis via Unconventional Regulation of RhoGTPases. Cancer Research 2009, 69: 2838-2844. PMID: 19276387, PMCID: PMC2701105, DOI: 10.1158/0008-5472.can-08-1397.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsCdc42 GTP-Binding ProteinCell AdhesionGuanine Nucleotide Dissociation InhibitorsHumansLung NeoplasmsMiceRac1 GTP-Binding ProteinRho GTP-Binding ProteinsRho Guanine Nucleotide Dissociation Inhibitor betaRhoA GTP-Binding ProteinRho-Specific Guanine Nucleotide Dissociation InhibitorsTumor Suppressor ProteinsUrinary Bladder NeoplasmsVinculinConceptsRho GTPasesFamily of proteinsGDP dissociation inhibitor 2Rho GDP dissociation inhibitor 2Dissociation inhibitor 2Membrane targetingMembrane associationPoint mutantsMetastasis suppressorRac1 activityGTPasesMetastasis suppressionInhibitor 2Suppress metastasisRhoGDI2ProteinSuppression correlatesRhoGDI1Weak inhibitorInhibitionRhoGTPasesMutantsMetastasis inhibitionStrong inhibitionSuppressor
2007
Function of the N-terminus of zizimin1: autoinhibition and membrane targeting
Meller N, Westbrook MJ, Shannon JD, Guda C, Schwartz MA. Function of the N-terminus of zizimin1: autoinhibition and membrane targeting. Biochemical Journal 2007, 409: 525-533. PMID: 17935486, PMCID: PMC2740492, DOI: 10.1042/bj20071263.Peer-Reviewed Original ResearchConceptsGEF domainCZH proteinsRho family small GTPasesPH domain bindsCdc42-specific GEFMultiple cellular functionsBasis of homologyN-terminal regionSmall GTPasesDomain bindsGEF activityRho proteinsCellular functionsRho-GEFsNovel functionN-terminusCritical regulatorStructural domainsLimited proteolysisZizimin1ProteinBindsDomainMembraneGTPases
2005
Zizimin2: a novel, DOCK180‐related Cdc42 guanine nucleotide exchange factor expressed predominantly in lymphocytes
Nishikimi A, Meller N, Uekawa N, Isobe K, Schwartz MA, Maruyama M. Zizimin2: a novel, DOCK180‐related Cdc42 guanine nucleotide exchange factor expressed predominantly in lymphocytes. FEBS Letters 2005, 579: 1039-1046. PMID: 15710388, DOI: 10.1016/j.febslet.2005.01.006.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsCdc42 GTP-Binding ProteinCell LineCloning, MolecularEnzyme ActivationGene Expression ProfilingGuanine Nucleotide Exchange FactorsLymphocytesMiceMolecular Sequence DataProtein BindingProtein IsoformsProtein Structure, TertiaryRac GTP-Binding ProteinsSequence AlignmentSubstrate Specificity
2004
Rho signalling at a glance
Schwartz M. Rho signalling at a glance. Journal Of Cell Science 2004, 117: 5457-5458. PMID: 15509861, DOI: 10.1242/jcs.01582.Peer-Reviewed Original ResearchAnimalsCdc42 GTP-Binding ProteinFeedback, PhysiologicalHumansIntracellular Signaling Peptides and ProteinsProtein Serine-Threonine KinasesProtein TransportProteinsRac GTP-Binding ProteinsReceptors, Cell SurfaceRho GTP-Binding ProteinsRho-Associated KinasesSignal TransductionWiskott-Aldrich Syndrome ProteinThe Novel Cdc42 Guanine Nucleotide Exchange Factor, Zizimin1, Dimerizes via the Cdc42-binding CZH2 Domain*
Meller N, Irani-Tehrani M, Ratnikov BI, Paschal BM, Schwartz MA. The Novel Cdc42 Guanine Nucleotide Exchange Factor, Zizimin1, Dimerizes via the Cdc42-binding CZH2 Domain*. Journal Of Biological Chemistry 2004, 279: 37470-37476. PMID: 15247287, DOI: 10.1074/jbc.m404535200.Peer-Reviewed Original ResearchConceptsExchange factorCdc42 Guanine Nucleotide Exchange FactorGuanine nucleotide exchange factorsRho family small GTPasesDomain-containing proteinsNucleotide exchange factorsMultiple cellular processesCDM proteinsCZH proteinsSmall GTPasesRho proteinsCellular processesCdc42 activationRho-GEFsCdc42Acid regionHomology analysisCritical regulatorZizimin1ProteinPositive cooperativityMutation analysisDimerizationDock180GTPases
2003
Localized Cdc42 Activation, Detected Using a Novel Assay, Mediates Microtubule Organizing Center Positioning in Endothelial Cells in Response to Fluid Shear Stress*
Tzima E, Kiosses WB, del Pozo MA, Schwartz MA. Localized Cdc42 Activation, Detected Using a Novel Assay, Mediates Microtubule Organizing Center Positioning in Endothelial Cells in Response to Fluid Shear Stress*. Journal Of Biological Chemistry 2003, 278: 31020-31023. PMID: 12754216, DOI: 10.1074/jbc.m301179200.Peer-Reviewed Original ResearchConceptsMicrotubule organizing centerCdc42 activityCdc42 activationFluid shear stressSmall GTPase Cdc42Protein kinase CzetaGTPase Cdc42Early embryosEndothelial cellsIntegrin dynamicsOrganizing centerCdc42Extracellular matrixLocalized activationFluorescence energy transferMTOC localizationVascular endothelial cellsSingle cellsNovel assayCellsActivationPar6CzetaGolgiEmbryosGuanine Exchange-Dependent and -Independent Effects of Vav1 on Integrin-Induced T Cell Spreading
del Pozo MA, Schwartz MA, Hu J, Kiosses WB, Altman A, Villalba M. Guanine Exchange-Dependent and -Independent Effects of Vav1 on Integrin-Induced T Cell Spreading. The Journal Of Immunology 2003, 170: 41-47. PMID: 12496381, DOI: 10.4049/jimmunol.170.1.41.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCdc42 GTP-Binding ProteinCell Cycle ProteinsCell SizeCells, CulturedDrug SynergismEnzyme ActivationFibronectinsGuanine Nucleotide Exchange FactorsHumansHybridomasIntegrinsJNK Mitogen-Activated Protein KinasesJurkat CellsMiceMitogen-Activated Protein KinasesP21-Activated KinasesPhosphorylationProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-vavRac GTP-Binding ProteinsT-Lymphocytes
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
Stimulation 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 activationAdhesion 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 cellsRacPAKMembraneCellsAdhesionActivation
1998
Activation 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