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
2000
The Molecular Adapter SLP-76 Relays Signals from Platelet Integrin αIIbβ3 to the Actin Cytoskeleton*
Obergfell A, Judd B, del Pozo M, Schwartz M, Koretzky G, Shattil S. The Molecular Adapter SLP-76 Relays Signals from Platelet Integrin αIIbβ3 to the Actin Cytoskeleton*. Journal Of Biological Chemistry 2000, 276: 5916-5923. PMID: 11113155, DOI: 10.1074/jbc.m010639200.Peer-Reviewed Original ResearchMeSH KeywordsActinsAdaptor Proteins, Signal TransducingAnimalsBlood PlateletsCell AdhesionCell Cycle ProteinsCHO CellsCricetinaeCytoskeletonEnzyme PrecursorsFibrinogenHumansIntracellular Signaling Peptides and ProteinsPhosphoproteinsPhosphorylationPlatelet Glycoprotein GPIIb-IIIa ComplexProtein BindingProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-vavPseudopodiaRac GTP-Binding ProteinsSignal TransductionSyk KinaseConceptsSLP-76SLAP-130Lamellipodia formationSLP-76 functionAdhesion-dependent activationCHO cell adhesionCell expression systemSLP-76 phosphorylationChinese hamster ovary cell expression systemSLP-76 expressionSyk tyrosine kinasePlatelet integrin αIIbβ3Sites of adhesionRac effectorPAK kinasesActin cytoskeletonAdherent CHO cellsExchange factorActin rearrangementCytoskeletal reorganizationActin reorganizationTyrosine phosphorylationExpression systemCell spreadingTyrosine kinaseDeath Effector Domain Protein PEA-15 Potentiates Ras Activation of Extracellular Signal Receptor-activated Kinase by an Adhesion-independent Mechanism
Ramos J, Hughes P, Renshaw M, Schwartz M, Formstecher E, Chneiweiss H, Ginsberg M. Death Effector Domain Protein PEA-15 Potentiates Ras Activation of Extracellular Signal Receptor-activated Kinase by an Adhesion-independent Mechanism. Molecular Biology Of The Cell 2000, 11: 2863-2872. PMID: 10982386, PMCID: PMC14961, DOI: 10.1091/mbc.11.9.2863.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAnimalsApoptosis Regulatory ProteinsCell AdhesionCell LineCHO CellsCricetinaeEnzyme ActivationGuanosine TriphosphateHumansIntracellular Signaling Peptides and ProteinsJNK Mitogen-Activated Protein KinasesMAP Kinase Kinase Kinase 1MiceMitogen-Activated Protein KinasesP38 Mitogen-Activated Protein KinasesPhosphoproteinsProtein Serine-Threonine KinasesRas ProteinsRecombinant Fusion ProteinsSignal TransductionConceptsPEA-15 expressionPEA-15ERK activationMitogen-activated protein kinase kinaseMitogen-activated protein kinase pathwayAdhesion-independent mechanismsRas-dependent mannerProtein kinase kinaseRegulation of apoptosisProtein kinase pathwayChinese hamster ovary cellsRas guanosineKinase kinaseRas activationSignal receptorHamster ovary cellsH-RasKinase pathwayERK activityIntegrin activationERK signalingAnchorage dependenceOncogenic processesOvary cellsApoptosis
1999
Integrin-dependent Tyrosine Phosphorylation and Growth Regulation by Vav
Yron I, Deckert M, Reff M, Munshi A, Schwartz M, Altman A. Integrin-dependent Tyrosine Phosphorylation and Growth Regulation by Vav. Cell Communication & Adhesion 1999, 7: 1-11. PMID: 10228731, DOI: 10.3109/15419069909034388.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsCell AdhesionCell Adhesion MoleculesCell DivisionCHO CellsCricetinaeCytoskeletal ProteinsFibronectinsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesHumansIntegrin beta1Jurkat CellsKineticsOncogene ProteinsPaxillinPhosphoproteinsPhosphorylationPrecipitin TestsProtein-Tyrosine KinasesProto-Oncogene MasProto-Oncogene Proteins c-vavTime FactorsTransfectionTyrosineConceptsRapid phosphorylationIntegrin-dependent tyrosine phosphorylationAdhesion-dependent mannerExchange factor domainB cell antigen receptorAdhesion-dependent increaseIntegrin signal transductionFocal adhesion kinaseExtent of phosphorylationCell surface stimuliCell antigen receptorJurkat T cellsTriton-insoluble fractionVav overexpressionSmall GTPasesBeta 1 integrinRho familyRho GTPasesCytoskeletal organizationSignal transductionAdhesion kinaseTyrosine phosphorylationStress fibersGrowth regulationFactor domain
1998
Integrins Regulate the Association and Phosphorylation of Paxillin by c-Abl*
Lewis J, Schwartz M. Integrins Regulate the Association and Phosphorylation of Paxillin by c-Abl*. Journal Of Biological Chemistry 1998, 273: 14225-14230. PMID: 9603926, DOI: 10.1074/jbc.273.23.14225.Peer-Reviewed Original ResearchConceptsC-AblCell adhesionTyrosine kinaseFocal adhesion protein paxillinNon-receptor tyrosine kinasePhosphorylation of paxillinC-Abl kinaseEffects of integrinsFocal adhesionsProtein paxillinIntegrin regulationPaxillinTransient recruitmentKinaseIntegrinsCell functionProteinAdhesionPhosphorylationTyrosineRegulationABLRecruitmentActivationLocalization