2015
Targeting NCK-Mediated Endothelial Cell Front-Rear Polarity Inhibits Neovascularization
Dubrac A, Genet G, Ola R, Zhang F, Pibouin-Fragner L, Han J, Zhang J, Thomas JL, Chedotal A, Schwartz MA, Eichmann A. Targeting NCK-Mediated Endothelial Cell Front-Rear Polarity Inhibits Neovascularization. Circulation 2015, 133: 409-421. PMID: 26659946, PMCID: PMC4729599, DOI: 10.1161/circulationaha.115.017537.Peer-Reviewed Original ResearchConceptsFront-rear polaritySprouting angiogenesisSignal integration mechanismImportant drug targetsNck adaptorsCytoskeletal dynamicsEndothelial cell migrationEmbryonic developmentAngiogenesis defectsPAK2 activationVessel sproutsNumber of diseasesBlood vessel growthDrug targetsCell migrationPostnatal retinaAngiogenic growthNckNck1AdaptorVessel growthKey processesEndothelial cellsPathological ocular neovascularizationInhibits neovascularization
2011
Light‐Triggered Myosin Activation for Probing Dynamic Cellular Processes
Goguen BN, Hoffman BD, Sellers JR, Schwartz MA, Imperiali B. Light‐Triggered Myosin Activation for Probing Dynamic Cellular Processes. Angewandte Chemie International Edition 2011, 50: 5667-5670. PMID: 21542072, PMCID: PMC3406609, DOI: 10.1002/anie.201100674.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntibodiesChlorocebus aethiopsCOS CellsLightMicroscopy, FluorescenceMolecular Sequence DataMyosinsPeptidesPhosphorylationPhosphoserineConceptsDynamic cellular processes
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
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 interactionCdc42Zizimin1RacActivatorGTPasesDomain
1999
Mutational Analysis of Cell Cycle Inhibition by Integrin β1C *
Meredith J, Kiosses W, Takada Y, Schwartz M. Mutational Analysis of Cell Cycle Inhibition by Integrin β1C *. Journal Of Biological Chemistry 1999, 274: 8111-8116. PMID: 10075712, DOI: 10.1074/jbc.274.12.8111.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceAnimalsCells, CulturedDNA Mutational AnalysisDNA ReplicationDose-Response Relationship, DrugHumansIntegrin beta1MiceMice, Inbred C3HMolecular Sequence DataMutagenesis, Site-DirectedReceptors, Interleukin-2Recombinant Fusion ProteinsStructure-Activity RelationshipConceptsCytoplasmic domainGreen fluorescent protein fusion proteinFluorescent protein fusion proteinProtein fusion proteinMembrane-proximal regionCell cycle progressionAnalysis of deletionsHuman interleukin-2 receptorBeta5 cytoplasmic domainsMembrane targetingMouse 10T1/2 cellsGrowth inhibitionCell cycle inhibitionTransmembrane domainLow expression levelsProstate epithelial cellsAcid domainCytoplasmic variantsTac subunitMutational analysisCycle progressionFusion proteinIntact receptorCell line DU145Human endothelial cell line
1995
Integrin signaling: roles for the cytoplasmic tails of αIIbβ3 in the tyrosine phosphorylation of pp125FAK
Leong L, Hughes P, Schwartz M, Ginsberg M, Shattil S. Integrin signaling: roles for the cytoplasmic tails of αIIbβ3 in the tyrosine phosphorylation of pp125FAK. Journal Of Cell Science 1995, 108: 3817-3825. PMID: 8719888, DOI: 10.1242/jcs.108.12.3817.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell Adhesion MoleculesCHO CellsCricetinaeCytoplasmEnzyme ActivationFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesMolecular Sequence DataMutagenesisPhosphorylationPlatelet Glycoprotein GPIIb-IIIa ComplexProtein-Tyrosine KinasesSignal TransductionConceptsAlpha IIbCytoplasmic tailTruncation mutantsFAK phosphorylationCytoplasmic tail truncation mutantsMembrane-proximal portionProtein tyrosine kinasesMembrane-distal portionExtent of phosphorylationLatter mutantTyrosine phosphorylationPersistent phosphorylationCell spreadingMutantsTyrosine kinaseCellular responsesExtracellular portionPhosphorylationCell adhesionFAKAdhesive ligandsCHO cellsPp125FAKAdditional mutationsBeta 3Inhibition of Cell Cycle Progression by the Alternatively Spliced Integrin β1C
Meredith J, Takada Y, Fornaro M, Languino L, Schwartz M. Inhibition of Cell Cycle Progression by the Alternatively Spliced Integrin β1C. Science 1995, 269: 1570-1572. PMID: 7545312, DOI: 10.1126/science.7545312.Peer-Reviewed Original ResearchMapping 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
1994
Differing structural requirements for GTPase-activating protein responsiveness and NADPH oxidase activation by Rac.
Xu X, Barry D, Settleman J, Schwartz M, Bokoch G. Differing structural requirements for GTPase-activating protein responsiveness and NADPH oxidase activation by Rac. Journal Of Biological Chemistry 1994, 269: 23569-23574. PMID: 8089125, DOI: 10.1016/s0021-9258(17)31553-3.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceBinding, CompetitiveDNA PrimersEnzyme ActivationGTPase-Activating ProteinsGTP-Binding ProteinsIn Vitro TechniquesMolecular Sequence DataNADH, NADPH OxidoreductasesNADPH OxidasesProteinsRac GTP-Binding ProteinsRas GTPase-Activating ProteinsRecombinant ProteinsStructure-Activity RelationshipConceptsGTPase-activating proteinsEffector domainFunction of RacGTP/GDP stateInteraction of RasDouble mutationNADPH oxidase activationGAP bindingActin cytoskeletonMembrane rufflingActin assemblyOxidase activationGTP hydrolysisRac-GTPGDP stateWild typeSuperoxide-forming NADPH oxidaseInteraction sitesProtein responsivenessProteinResidues 12MutationsRacRac2Phagocytic leukocytes