2023
FN (Fibronectin)-Integrin α5 Signaling Promotes Thoracic Aortic Aneurysm in a Mouse Model of Marfan Syndrome
Chen M, Cavinato C, Hansen J, Tanaka K, Ren P, Hassab A, Li D, Youshao E, Tellides G, Iyengar R, Humphrey J, Schwartz M. FN (Fibronectin)-Integrin α5 Signaling Promotes Thoracic Aortic Aneurysm in a Mouse Model of Marfan Syndrome. Arteriosclerosis Thrombosis And Vascular Biology 2023, 43: e132-e150. PMID: 36994727, PMCID: PMC10133209, DOI: 10.1161/atvbaha.123.319120.Peer-Reviewed Original ResearchConceptsContractile gene expressionSmooth muscle cellsGene expressionMgR miceWild-type smooth muscle cellsMarfan miceAortic aneurysmMouse modelMarfan syndromeMouse aortic smooth muscle cellsPathogenesis of TAACytoplasmic domainVascular smooth muscle cellsThoracic aortic aneurysmAortic smooth muscle cellsCultured smooth muscle cellsNF-kB activationNF-kB inhibitionMolecular mechanismsIntegrin α2ECM remodelingElastic fiber integrityPhenotypic modulationMarfan's aneurysmsMgR/
2018
Talin as a mechanosensitive signaling hub
Goult BT, Yan J, Schwartz MA. Talin as a mechanosensitive signaling hub. Journal Of Cell Biology 2018, 217: 3776-3784. PMID: 30254032, PMCID: PMC6219721, DOI: 10.1083/jcb.201808061.Peer-Reviewed Original ResearchConceptsSignaling hubsExtracellular matrixRod domainTalin rod domainIntegrin β subunitsDifferent protein interactionsLong rod domainSwitch-like behaviorActin cytoskeletonCytoplasmic domainCytoplasmic proteinsProtein interactionsHelical bundleGlobular head domainTalin functionTransmembrane receptorsHelix bundleΒ-subunitHead domainIntegrin familyTalinCell adhesionIndividual domainsRecent evidenceDomain
2017
VE-Cadherin Phosphorylation Regulates Endothelial Fluid Shear Stress Responses through the Polarity Protein LGN
Conway DE, Coon BG, Budatha M, Arsenovic PT, Orsenigo F, Wessel F, Zhang J, Zhuang Z, Dejana E, Vestweber D, Schwartz MA. VE-Cadherin Phosphorylation Regulates Endothelial Fluid Shear Stress Responses through the Polarity Protein LGN. Current Biology 2017, 27: 2219-2225.e5. PMID: 28712573, PMCID: PMC5667920, DOI: 10.1016/j.cub.2017.06.020.Peer-Reviewed Original ResearchConceptsSrc family kinasesProtein LGNCytoplasmic tyrosinesVE-cadherinVascular endothelial growth factor receptorVE-cadherin functionJunctional complexesRespective cytoplasmic domainsBlood vessel developmentVE-cadherin phosphorylationTransduce forcesTransduce signalsCytoplasmic domainFamily kinasesBlood vessel remodelingGrowth factor receptorVEGFR activationPECAM-1Stress responseComplex consistingFluid shear stressVessel developmentFlow-dependent vascular remodelingSpecific poolPhosphorylation
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
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
1997
Suppression 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
The Regulation of Growth and Intracellular Signaling by Integrins
Meredith J, Winitz S, Lewis J, Hess S, Ren X, Renshaw M, Schwartz M. The Regulation of Growth and Intracellular Signaling by Integrins. Endocrine Reviews 1996, 17: 207-220. PMID: 8771356, DOI: 10.1210/edrv-17-3-207.Peer-Reviewed Original ResearchConceptsReceptor cytoplasmic domainIntegrin-ligand bindingShort cytoplasmic regionLarge extracellular domainRegulation of growthExtracellular matrix proteinsCell surface receptorsDomain bindsCytoplasmic domainDifferent α subunitsTransmembrane regionTransmembrane receptorsCytoplasmic regionCytoskeletal proteinsKinase activationGene expressionΑ-subunitDifferent β subunitsExtracellular domainIntracellular signalingΒ-subunitAdhesion receptorsMatrix proteinsCell migrationCell growth
1995
Mapping 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