2011
JNK2 Promotes Endothelial Cell Alignment under Flow
Hahn C, Wang C, Orr AW, Coon BG, Schwartz MA. JNK2 Promotes Endothelial Cell Alignment under Flow. PLOS ONE 2011, 6: e24338. PMID: 21909388, PMCID: PMC3164210, DOI: 10.1371/journal.pone.0024338.Peer-Reviewed Original ResearchConceptsMitogen-activated protein kinase c-Jun N-terminal kinaseProtein kinase c-Jun N-terminal kinaseC-Jun N-terminal kinaseActin stress fibersN-terminal kinaseFocal adhesionsBasement membrane proteinsMembrane proteinsLaminar shear stressStress fibersGene expressionJNK activityIntegrin activationJNK2 activationEndothelial cell alignmentJNK activationActivated JNKExtracellular matrixInflammatory gene expressionCell alignmentUnexpected connectionEndothelial cellsActivationPathwayCells
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
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