2009
Suppression of RhoG activity is mediated by a syndecan 4–synectin–RhoGDI1 complex and is reversed by PKCα in a Rac1 activation pathway
Elfenbein A, Rhodes JM, Meller J, Schwartz MA, Matsuda M, Simons M. Suppression of RhoG activity is mediated by a syndecan 4–synectin–RhoGDI1 complex and is reversed by PKCα in a Rac1 activation pathway. Journal Of Cell Biology 2009, 186: 75-83. PMID: 19581409, PMCID: PMC2712988, DOI: 10.1083/jcb.200810179.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCarrier ProteinsCluster AnalysisEnzyme ActivationFibroblast Growth Factor 2GTP PhosphohydrolasesGuanine Nucleotide Dissociation InhibitorsHeLa CellsHumansMiceMice, KnockoutModels, BiologicalPhosphorylationPhosphoserineProtein Kinase C-alphaRac1 GTP-Binding ProteinRatsRho GTP-Binding ProteinsRho-Specific Guanine Nucleotide Dissociation InhibitorsSyndecan-4ConceptsFibroblast growth factor-2Polarized activationRac1 activationSmall guanosine triphosphatase Rac1Activation pathwayProtein complexesRac activationPlasma membranePhysiological defectsSyndecan-4RhoGDI1Major regulatorInactive stateGrowth factor 2RhoGRhoG activityProteoglycan receptorsEndothelial migrationTernary complexFactor 2Genetic deletionSynectinRac1PKCalphaActivation
2001
c-Abl Tyrosine Kinase Binds and Phosphorylates Phospholipid Scramblase 1*
Sun J, Zhao J, Schwartz M, Wang J, Wiedmer T, Sims P. c-Abl Tyrosine Kinase Binds and Phosphorylates Phospholipid Scramblase 1*. Journal Of Biological Chemistry 2001, 276: 28984-28990. PMID: 11390389, DOI: 10.1074/jbc.m102505200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino Acid SubstitutionAnimalsBinding SitesCarrier ProteinsCell LineCells, CulturedFibroblastsGenes, ablGlutathione TransferaseHumansMembrane ProteinsMiceMice, KnockoutMutagenesis, Site-DirectedPhospholipid Transfer ProteinsPhospholipidsPhosphorylationProtein BindingProto-Oncogene Proteins c-ablRecombinant Fusion ProteinsRepetitive Sequences, Amino AcidSrc Homology DomainsTransfectionTyrosineConceptsPhospholipid scramblase 1SH3 domainC-AblAbl SH3 domainTyr phosphorylationMultiple proline-rich motifsScramblase 1Plasma membrane proteinsC-Abl bindsProline-rich motifDomain-binding siteProline-rich segmentDNA-damaging agent cisplatinC-Abl kinasePlasma membrane phospholipidsTandem repeat sequencesMutation of TyrCell linesCisplatin-induced phosphorylationKinase bindsGenotoxic stressMembrane proteinsDifferent SH3 domainsTransbilayer movementRepeat sequences
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 activationDetermination of GTP loading on Rho
Ren X, Schwartz M. Determination of GTP loading on Rho. Methods In Enzymology 2000, 325: 264-272. PMID: 11036609, DOI: 10.1016/s0076-6879(00)25448-7.Peer-Reviewed Original ResearchConceptsRho-binding domainGTP-RhoLow molecular weight GTPaseAffinity precipitation assaysActin cytoskeleton organizationGTP loadingCytoskeleton organizationWeight GTPaseGTPase activityRho effectorCell lysatesGTPaseRhoPrecipitation assaysTRBDWestern immunoblottingDomainQuality controlPositive controlAssaysRhotekinEffectorsProtein
1994
Immunolocalization of anion exchanger AE2 and cation exchanger NHE-1 in distinct adjacent cells of gastric mucosa
Stuart-Tilley A, Sardet C, Pouyssegur J, Schwartz M, Brown D, Alper S. Immunolocalization of anion exchanger AE2 and cation exchanger NHE-1 in distinct adjacent cells of gastric mucosa. American Journal Of Physiology 1994, 266: c559-c568. PMID: 8141271, DOI: 10.1152/ajpcell.1994.266.2.c559.Peer-Reviewed Original ResearchConceptsBasolateral membraneExchanger proteinParietal cellsExchanger NHE-1Isoform-specific antibodiesMucous neck cellsNHE-1Secretory machineryTransporter proteinsNeck cellsMolecular identityHigh abundanceMucous cellsCarbonic anhydrase IICell typesAnion exchanger 2Cellular dispositionProteinAnion exchanger AE2Surface mucous cellsMorphological evidenceAdjacent cellsBand 3Exchanger 2Mucous neck
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 antibodies
1992
Adhesion is required for protein kinase C-dependent activation of the Na+/H+ antiporter by platelet-derived growth factor.
Schwartz M, Lechene C. Adhesion is required for protein kinase C-dependent activation of the Na+/H+ antiporter by platelet-derived growth factor. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 6138-6141. PMID: 1378621, PMCID: PMC402137, DOI: 10.1073/pnas.89.13.6138.Peer-Reviewed Original ResearchMeSH KeywordsAcid-Base EquilibriumAnimalsCarrier ProteinsCell AdhesionCells, CulturedExtracellular MatrixHydrogen-Ion ConcentrationIn Vitro TechniquesMiceNaphthalenesPlatelet-Derived Growth FactorPolycyclic CompoundsProtein Kinase CSignal TransductionSodium-Hydrogen ExchangersTetradecanoylphorbol AcetateConceptsProtein kinase CPlatelet-derived growth factorKinase CAdherent cellsGrowth factorExtracellular matrix proteinsPKC-dependent pathwayElevation of intracellularMatrix proteinsAnchorage-dependent cellsCell adhesionDependent activationPKC activationAntiporterPhorbol esterSolid substratumPharmacological inhibitionC3H 10T1/2 cellsCellsActivationPathwayIntracellular pHAdhesionProteinIntegrins
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 factorFibronectin
1990
pH regulation in spread cells and round cells.
Schwartz M, Cragoe E, Lechene C. pH regulation in spread cells and round cells. Journal Of Biological Chemistry 1990, 265: 1327-1332. PMID: 2153127, DOI: 10.1016/s0021-9258(19)40017-3.Peer-Reviewed Original Research