2016
Force regulated conformational change of integrin αVβ3
Chen Y, Lee H, Tong H, Schwartz M, Zhu C. Force regulated conformational change of integrin αVβ3. Matrix Biology 2016, 60: 70-85. PMID: 27423389, PMCID: PMC5237428, DOI: 10.1016/j.matbio.2016.07.002.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiomechanical PhenomenaBiotinylationCell AdhesionCell LineEndothelial CellsErythrocytesExtracellular MatrixFibronectinsGene ExpressionGlassHumansIntegrin alphaVbeta3KineticsLungMiceMolecular ProbesPoint MutationProtein BindingProtein ConformationSignal TransductionSingle Molecule ImagingConceptsConformational changesTransduce signalsSingle-molecule levelIntegrin functionBiomembrane force probeMolecular machinesPhysiological functionsCell adhesionCell surfaceExtracellular matrixPoint mutationsConformational transitionIntegrinsEssential roleTumor metastasisExtended conformationConformationDynamic equilibriumEctodomainMutationsForce probePhagocytosisMembraneAngiogenesisFunction
2015
Rac1 functions as a reversible tension modulator to stabilize VE-cadherin trans-interaction
Daneshjou N, Sieracki N, van Nieuw Amerongen GP, Conway D, Schwartz M, Komarova Y, Malik A. Rac1 functions as a reversible tension modulator to stabilize VE-cadherin trans-interaction. Journal Of Cell Biology 2015, 208: 23-32. PMID: 25559184, PMCID: PMC4284224, DOI: 10.1083/jcb.201409108.Peer-Reviewed Original ResearchActomyosinAdherens JunctionsAntigens, CDCadherinsCell AdhesionCells, CulturedEndothelial CellsEnzyme ActivationHumansKineticsMicroscopy, FluorescenceMicroscopy, VideoModels, BiologicalMyosin Type IIProtein BindingProtein Kinase InhibitorsProtein MultimerizationProtein StabilityRac1 GTP-Binding ProteinRho-Associated KinasesTime-Lapse ImagingTransfection
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
2001
Activation of integrins in endothelial cells by fluid shear stress mediates Rho‐dependent cytoskeletal alignment
Tzima E, del Pozo M, Shattil S, Chien S, Schwartz M. Activation of integrins in endothelial cells by fluid shear stress mediates Rho‐dependent cytoskeletal alignment. The EMBO Journal 2001, 20: 4639-4647. PMID: 11532928, PMCID: PMC125600, DOI: 10.1093/emboj/20.17.4639.Peer-Reviewed Original ResearchAnimalsAortaCattleCells, CulturedCulture Media, Serum-FreeCytoskeletonEndothelium, VascularExtracellular Matrix ProteinsFibronectinsGreen Fluorescent ProteinsIntegrinsKineticsLuminescent ProteinsProtein ConformationReceptors, VitronectinRecombinant ProteinsRho GTP-Binding ProteinsStress, MechanicalTime FactorsTransfection
1999
Integrin-dependent Tyrosine Phosphorylation and Growth Regulation by Vav
Yron I, Deckert M, Reff M, Munshi A, Schwartz M, Altman A. Integrin-dependent Tyrosine Phosphorylation and Growth Regulation by Vav. Cell Communication & Adhesion 1999, 7: 1-11. PMID: 10228731, DOI: 10.3109/15419069909034388.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsCell AdhesionCell Adhesion MoleculesCell DivisionCHO CellsCricetinaeCytoskeletal ProteinsFibronectinsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesHumansIntegrin beta1Jurkat CellsKineticsOncogene ProteinsPaxillinPhosphoproteinsPhosphorylationPrecipitin TestsProtein-Tyrosine KinasesProto-Oncogene MasProto-Oncogene Proteins c-vavTime FactorsTransfectionTyrosineConceptsRapid phosphorylationIntegrin-dependent tyrosine phosphorylationAdhesion-dependent mannerExchange factor domainB cell antigen receptorAdhesion-dependent increaseIntegrin signal transductionFocal adhesion kinaseExtent of phosphorylationCell surface stimuliCell antigen receptorJurkat T cellsTriton-insoluble fractionVav overexpressionSmall GTPasesBeta 1 integrinRho familyRho GTPasesCytoskeletal organizationSignal transductionAdhesion kinaseTyrosine phosphorylationStress fibersGrowth regulationFactor domain
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 resultsAnchorage
1994
Alpha v integrins mediate the rise in intracellular calcium in endothelial cells on fibronectin even though they play a minor role in adhesion
Schwartz M, Denninghoff K. Alpha v integrins mediate the rise in intracellular calcium in endothelial cells on fibronectin even though they play a minor role in adhesion. Journal Of Biological Chemistry 1994, 269: 11133-11137. PMID: 7512559, DOI: 10.1016/s0021-9258(19)78101-0.Peer-Reviewed Original ResearchConceptsAlpha 5 beta 1Alpha vBeta 1Intracellular calciumEndothelial cellsAnti-integrin monoclonal antibodiesElevation of intracellularAlpha v integrinsAnti-integrin antibodiesMonoclonal antibodiesV integrinsAntibodiesDistinct intracellularAgonistsIntegrin alpha subunitsAdhesion assaysFunction-blocking anti-integrin antibodiesIntegrinsSpecific integrinsCalciumFibronectinAlpha subunitCellsSame cellsIntracellular
1993
A 50-kDa integrin-associated protein is required for integrin-regulated calcium entry in endothelial cells.
Schwartz M, Brown E, Fazeli B. A 50-kDa integrin-associated protein is required for integrin-regulated calcium entry in endothelial cells. Journal Of Biological Chemistry 1993, 268: 19931-19934. PMID: 8376355, DOI: 10.1016/s0021-9258(20)80675-9.Peer-Reviewed Original ResearchConceptsIntegrin-associated proteinExtracellular matrix proteinsMatrix proteinsEndothelial cellsIAP functionTransmembrane domainTyrosine phosphorylationPrimary sequenceEndothelial cell adhesionCell adhesionMembrane channelsProteinAnti-integrin antibodiesCalcium entryCellsIntracellular pHIon transportInflux of Ca2Activation of neutrophilsActivationCalcium channelsCalcium influxPhosphorylationNeutrophil functionMonoclonal antibodiesIntegrin beta 1- and beta 3-mediated endothelial cell migration is triggered through distinct signaling mechanisms.
Leavesley D, Schwartz M, Rosenfeld M, Cheresh D. Integrin beta 1- and beta 3-mediated endothelial cell migration is triggered through distinct signaling mechanisms. Journal Of Cell Biology 1993, 121: 163-170. PMID: 7681432, PMCID: PMC2119781, DOI: 10.1083/jcb.121.1.163.Peer-Reviewed Original ResearchConceptsExtracellular calciumBeta 3Extracellular calcium sourcesAlpha v beta 3Alpha 2 beta 1Absence of cytokinesNa/H antiporterBeta 1 mAbIntracellular calciumCalcium influxIntegrin alpha 2 beta 1Specific influxBeta 1Distinct signaling mechanismsEndothelial cell migrationGrowth factorMeasurable riseDistinct intracellularRespective integrinsH antiporterCellular migrationCell migrationCell contactCalciumMAbs
1991
Insoluble fibronectin activates the Na/H antiporter by clustering and immobilizing integrin alpha 5 beta 1, independent of cell shape.
Schwartz M, Lechene C, Ingber D. Insoluble fibronectin activates the Na/H antiporter by clustering and immobilizing integrin alpha 5 beta 1, independent of cell shape. Proceedings Of The National Academy Of Sciences Of The United States Of America 1991, 88: 7849-7853. PMID: 1652767, PMCID: PMC52401, DOI: 10.1073/pnas.88.17.7849.Peer-Reviewed Original ResearchConceptsIntegrin alpha 5 beta 1Alpha 5 beta 1Cell shapeInsoluble extracellular matrix moleculesNa/H antiporterExtracellular matrix receptorsInsoluble fibronectinSurface-adsorbed fibronectinSoluble growth factorsExtracellular matrix moleculesH antiporterCell surface receptorsTransmembrane receptorsGrowth factor receptorBeta 1Matrix receptorsGrowth controlAnchorage-dependent cellsMatrix moleculesAntiporterFactor receptorSuppress growthSoluble mitogensGrowth factorFibronectinBinding of actin to liver cell membranes: the state of membrane-bound actin.
Tranter M, Sugrue S, Schwartz M. Binding of actin to liver cell membranes: the state of membrane-bound actin. Journal Of Cell Biology 1991, 112: 891-901. PMID: 1705560, PMCID: PMC2288875, DOI: 10.1083/jcb.112.5.891.Peer-Reviewed Original Research
1990
Radiolabel‐transfer cross‐linking demonstrates that protein 4.1 binds to the N‐terminal region of β spectrin and to actin in binary interactions
BECKER P, SCHWARTZ M, MORROW J, Samuel E. Radiolabel‐transfer cross‐linking demonstrates that protein 4.1 binds to the N‐terminal region of β spectrin and to actin in binary interactions. The FEBS Journal 1990, 193: 827-836. PMID: 2249696, DOI: 10.1111/j.1432-1033.1990.tb19406.x.Peer-Reviewed Original Research
1989
Evidence for a direct, nucleotide-sensitive interaction between actin and liver cell membranes.
Tranter M, Sugrue S, Schwartz M. Evidence for a direct, nucleotide-sensitive interaction between actin and liver cell membranes. Journal Of Cell Biology 1989, 109: 2833-2840. PMID: 2592407, PMCID: PMC2115935, DOI: 10.1083/jcb.109.6.2833.Peer-Reviewed Original Research
1986
Binding and assembly of actin filaments by plasma membranes from Dictyostelium discoideum.
Schwartz M, Luna E. Binding and assembly of actin filaments by plasma membranes from Dictyostelium discoideum. Journal Of Cell Biology 1986, 102: 2067-2075. PMID: 2423531, PMCID: PMC2114255, DOI: 10.1083/jcb.102.6.2067.Peer-Reviewed Original Research