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
1994
Integrins as Signal Transducing Receptors
Schwartz M. Integrins as Signal Transducing Receptors. 1994, 33-47. DOI: 10.1016/b978-0-08-091729-0.50007-3.Peer-Reviewed Original ResearchSignal transducing receptorsExtracellular matrixProtein kinase CCell functionIntracellular second messengerRole of integrinsCytoskeletal organizationInositol lipidsCell shapeSecond messengerKinase CAnchorage-dependent cellsSuch messengersCell typesContact of cellsOnly adhesionIntegrinsMessengerActivation of plateletsCellsCytoskeletonRecent dataReceptorsAdhesionDifferentiation
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