2002
A Fragment of Paxillin Binds the α4Integrin Cytoplasmic Domain (Tail) and Selectively Inhibits α4-Mediated Cell Migration*
Liu S, Kiosses WB, Rose DM, Slepak M, Salgia R, Griffin JD, Turner CE, Schwartz MA, Ginsberg MH. A Fragment of Paxillin Binds the α4Integrin Cytoplasmic Domain (Tail) and Selectively Inhibits α4-Mediated Cell Migration*. Journal Of Biological Chemistry 2002, 277: 20887-20894. PMID: 11919182, DOI: 10.1074/jbc.m110928200.Peer-Reviewed Original ResearchConceptsCytoplasmic domainPaxillin interactionCell migrationIntegrin-mediated cell adhesionIntegrin alpha subunitsEnhanced cell migrationPaxillin bindingFunctional responseFocal adhesionsCellular functionsPaxillinCardiac developmentAlanine substitutionsMutational analysisAdaptor moleculeAcid regionAlpha subunitBiological processesCell spreadingCellular responsesCell adhesionIntegrin subunitsSubunitsTernary complexFragments
2001
Increased filamin binding to β-integrin cytoplasmic domains inhibits cell migration
Calderwood D, Huttenlocher A, Kiosses W, Rose D, Woodside D, Schwartz M, Ginsberg M. Increased filamin binding to β-integrin cytoplasmic domains inhibits cell migration. Nature Cell Biology 2001, 3: 1060-1068. PMID: 11781567, DOI: 10.1038/ncb1201-1060.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SubstitutionAnimalsBinding SitesCell MovementCell PolarityCHO CellsContractile ProteinsCricetinaeCytoplasmCytoskeletonFibronectinsFilaminsFocal AdhesionsHumansIntegrin beta ChainsIntegrinsIsoleucineJurkat CellsMicrofilament ProteinsProtein Structure, TertiaryRecombinant Fusion ProteinsTalinValineConceptsFocal adhesion formationFilamin bindingCell migrationMembrane protrusionsMatrix assemblyIntegrin-dependent cell migrationFibronectin matrix assemblyAmino acid substitutionsInhibits cell migrationAnimal developmentActin cytoskeletonIntegrin tailsBiochemical signalsAdhesion receptorsFilaminCell polarizationTalinAcid substitutionsExtracellular matrixAdhesion formationTailBindingAssemblyMigrationSelective lossIntegrins and cell proliferationregulation of cyclin-dependent kinases via cytoplasmic signaling pathways
Schwartz M, Assoian R. Integrins and cell proliferationregulation of cyclin-dependent kinases via cytoplasmic signaling pathways. Journal Of Cell Science 2001, 114: 2553-2560. PMID: 11683383, DOI: 10.1242/jcs.114.14.2553.Peer-Reviewed Original ResearchConceptsCyclin-dependent kinasesG1 phase cyclin-dependent kinasesPhase cyclin-dependent kinasesCell cycle progressionCycle progressionCytoplasmic signaling pathwaysIntegrin-dependent signalsMammalian cellsGrowth factor receptorSignaling pathwaysERK pathwayCell adhesionExtracellular matrixDiverse arrayFactor receptorCyclin D1KinaseRegulationPathwayGrowth factorIntegrinsRecent advancesIntegrated controlReceptorsAdhesion
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
1997
Affinity Modulation of Platelet Integrin αIIbβ3 by β3-Endonexin, a Selective Binding Partner of the β3 Integrin Cytoplasmic Tail
Kashiwagi H, Schwartz M, Eigenthaler M, Davis K, Ginsberg M, Shattil S. Affinity Modulation of Platelet Integrin αIIbβ3 by β3-Endonexin, a Selective Binding Partner of the β3 Integrin Cytoplasmic Tail. Journal Of Cell Biology 1997, 137: 1433-1443. PMID: 9182673, PMCID: PMC2132534, DOI: 10.1083/jcb.137.6.1433.Peer-Reviewed Original ResearchConceptsGreen fluorescent proteinIntegrin cytoplasmic tailsCytoplasmic tailSuch protein-protein interactionsSelective binding partnerΒ3 integrin cytoplasmic tailProtein-protein interactionsAffinity modulationFibrinogen-dependent aggregationPlatelet integrin αIIbβ3Β3-endonexinBinding partnerEnergy-dependent fashionAcid proteinH-RasIntegrin alphaIIbbeta3Adhesive functionMetabolic regulationFluorescent proteinBeta3 tailIntegrin αIIbβ3Cell lysatesCHO cellsAffinity stateSurface expressionSuppression of Integrin Activation: A Novel Function of a Ras/Raf-Initiated MAP Kinase Pathway
Hughes P, Renshaw M, Pfaff M, Forsyth J, Keivens V, Schwartz M, Ginsberg M. Suppression of Integrin Activation: A Novel Function of a Ras/Raf-Initiated MAP Kinase Pathway. Cell 1997, 88: 521-530. PMID: 9038343, DOI: 10.1016/s0092-8674(00)81892-9.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcium-Calmodulin-Dependent Protein KinasesCell SizeCHO CellsCricetinaeCytoplasmDNA, ComplementaryEndoribonucleasesEnzyme ActivationExtracellular Matrix ProteinsFibronectinsFlow CytometryFungal ProteinsGene Expression Regulation, EnzymologicIntegrinsProtein BiosynthesisProtein Serine-Threonine KinasesProtein Structure, TertiaryProto-Oncogene ProteinsProto-Oncogene Proteins c-rafRas ProteinsRecombinant Fusion ProteinsTranscription, GeneticConceptsMAP kinase pathwayKinase pathwayIntegrin activationBeta-subunit cytoplasmic domainH-RasTranscription-independent functionsSubunit cytoplasmic domainERK MAP kinase pathwayIntegrin affinity stateCell adhesion receptorsIntegrin cell adhesion receptorsActivation of integrinsNegative feedback loopSmall GTPCytoplasmic domainEffector kinaseIntegrin phosphorylationRaf-1Novel functionIntegrin functionNegative regulatorAdhesion receptorsProtein synthesisMRNA transcriptionDistinct alpha
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 fibronectin
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 3Mapping 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
1993
Spreading of human endothelial cells on fibronectin or vitronectin triggers elevation of intracellular free calcium.
Schwartz M. Spreading of human endothelial cells on fibronectin or vitronectin triggers elevation of intracellular free calcium. Journal Of Cell Biology 1993, 120: 1003-1010. PMID: 7679387, PMCID: PMC2200079, DOI: 10.1083/jcb.120.4.1003.Peer-Reviewed Original ResearchConceptsCalcium channelsBasal levelsVoltage-independent calcium channelsEndothelial cellsVoltage-dependent calcium channelsIntracellular free calciumElevation of pHiNa-Ca exchangerHuman endothelial cellsBeta 1 integrinIntracellular calciumFura-2Extracellular calciumFree calciumSubunit antibodiesSame antibodyIntracellular pHSteady-state levelsAntibodiesElevationCalciumCellsHigh steady-state levelsInvolvementIntegrins
1990
Control of intracellular pH and growth by fibronectin in capillary endothelial cells.
Ingber D, Prusty D, Frangioni J, Cragoe E, Lechene C, Schwartz M. Control of intracellular pH and growth by fibronectin in capillary endothelial cells. Journal Of Cell Biology 1990, 110: 1803-1811. PMID: 2159481, PMCID: PMC2200182, DOI: 10.1083/jcb.110.5.1803.Peer-Reviewed Original ResearchCytoplasmic pH and anchorage-independent growth induced by v-Ki-ras, v-src or polyoma middle T.
Schwartz M, Rupp E, Frangioni J, Lechene C. Cytoplasmic pH and anchorage-independent growth induced by v-Ki-ras, v-src or polyoma middle T. Oncogene 1990, 5: 55-8. PMID: 2181378.Peer-Reviewed Original ResearchConceptsAnchorage-independent growthNormal cellsCytoplasmic pHPolyoma middle T oncogeneRas-transformed cellsCell linesExtracellular matrix proteinsMiddle T oncogeneV-SrcSrc oncogeneTissue culture plasticMatrix proteinsCellular requirementsCell growthControl growthOncogeneV-KiAlkaline pHiSeries of cellsCulture plasticGrowth factorCellsGrowthRAMutants
1989
Effect of cell spreading on cytoplasmic pH in normal and transformed fibroblasts.
Schwartz M, Both G, Lechene C. Effect of cell spreading on cytoplasmic pH in normal and transformed fibroblasts. Proceedings Of The National Academy Of Sciences Of The United States Of America 1989, 86: 4525-4529. PMID: 2734302, PMCID: PMC287303, DOI: 10.1073/pnas.86.12.4525.Peer-Reviewed Original Research