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
2011
Dynamic molecular processes mediate cellular mechanotransduction
Hoffman BD, Grashoff C, Schwartz MA. Dynamic molecular processes mediate cellular mechanotransduction. Nature 2011, 475: 316-323. PMID: 21776077, PMCID: PMC6449687, DOI: 10.1038/nature10316.Peer-Reviewed Original ResearchConceptsCell adhesion complexesDistinct signaling pathwaysTransduction of forceDynamic molecular processesEmbryonic developmentCellular mechanotransductionPlasma membraneBiochemical signalsAdult physiologySignaling pathwaysCellular responsesSubcellular structuresMolecular processesNumerous diseasesMechanical forcesMuscular dystrophyCytoskeletonTransductionMechanotransductionPathwayPhysiologyDisassemblyRecent workMembraneAssemblySuper-Resolution Microscopy: A New Dimension in Focal Adhesions
Schwartz MA. Super-Resolution Microscopy: A New Dimension in Focal Adhesions. Current Biology 2011, 21: r115-r116. PMID: 21300274, DOI: 10.1016/j.cub.2010.12.025.Peer-Reviewed Original Research
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 proteolysisZizimin1ProteinBindsDomainMembraneGTPasesArf6 and microtubules in adhesion-dependent trafficking of lipid rafts
Balasubramanian N, Scott DW, Castle JD, Casanova JE, Schwartz MA. Arf6 and microtubules in adhesion-dependent trafficking of lipid rafts. Nature Cell Biology 2007, 9: 1381-1391. PMID: 18026091, PMCID: PMC2715295, DOI: 10.1038/ncb1657.Peer-Reviewed Original ResearchConceptsPlasma membraneLipid raftsAnchorage-dependent signalingArf6-dependent mannerCaveolin-dependent internalizationSmall GTPase Arf6Microtubule-dependent traffickingIntegrin-mediated adhesionRecycling endosomesGTPase Arf6Membrane raftsDetachment of cellsCell spreadingF-actinRaftsArf6MicrotubulesEndosomesRac1TraffickingMembraneCellsEndocytosisSignalingPathway
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
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
Adhesion 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
1988
How actin binds and assembles onto plasma membranes from Dictyostelium discoideum.
Schwartz M, Luna E. How actin binds and assembles onto plasma membranes from Dictyostelium discoideum. Journal Of Cell Biology 1988, 107: 201-209. PMID: 3392099, PMCID: PMC2115166, DOI: 10.1083/jcb.107.1.201.Peer-Reviewed Original ResearchConceptsPolymerizationSuccessive monomersMembrane surfacePositive cooperativityActin trimerTight bindingAssembly stateHistidine-40Critical concentrationLow salt bufferDerivativesSalt bufferEthoxyformic anhydrideCooperativitySolutionMonomersMembraneAffinityMultivalencyOligomersAnhydrideActin nucleiBindingCross-linking experimentsActin oligomers
1985
Cell-Cell Contact Proteins in Antigen-Specific and Antigen-Nonspecific Cellular Cytotoxicity
Sitkovsky M, Schwartz M, Eisen H. Cell-Cell Contact Proteins in Antigen-Specific and Antigen-Nonspecific Cellular Cytotoxicity. Advances In Experimental Medicine And Biology 1985, 184: 429-449. PMID: 3875975, DOI: 10.1007/978-1-4684-8326-0_29.Peer-Reviewed Original ResearchConceptsCTL-TC interactionsCytotoxic T lymphocytesLymphocyte function-associated antigenCell-cell contact proteinsPlasma membraneCell surface moleculesTarget cellsContact proteinsMolecular organizationSurface membraneNatural killer cellsSurface moleculesProteinAbsence of complementFunction-associated antigenLyt-5Killer cellsMembraneAntigen-SpecificLyt-2T lymphocytesCellular cytotoxicityLytic mechanismCellsMonoclonal antibodies