2014
The docking protein FRS2α is a critical regulator of VEGF receptors signaling
Chen PY, Qin L, Zhuang ZW, Tellides G, Lax I, Schlessinger J, Simons M. The docking protein FRS2α is a critical regulator of VEGF receptors signaling. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 5514-5519. PMID: 24706887, PMCID: PMC3992672, DOI: 10.1073/pnas.1404545111.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsCell MovementDNA PrimersEndothelial CellsGene Expression ProfilingGenetic VectorsHEK293 CellsHuman Umbilical Vein Endothelial CellsHumansImmunoblottingImmunohistochemistryImmunoprecipitationLaser-Doppler FlowmetryLentivirusMembrane ProteinsMiceReal-Time Polymerase Chain ReactionReceptors, Vascular Endothelial Growth FactorSignal TransductionX-Ray MicrotomographyConceptsLymphatic endothelial cell migrationFibroblast growth factor receptor substrate 2Growth factor receptor substrate 2Cognate receptor tyrosine kinasesFactor receptor substrate 2Receptor kinase signalingVascular endothelial growth factorPostnatal vascular developmentReceptor tyrosine kinasesEndothelial cell migrationKinase signalingEndothelial-specific deletionAdult angiogenesisVEGF receptorsTyrosine kinaseCritical regulatorVascular developmentFRS2αSubstrate 2Cell migrationDependent activationCritical roleUnidentified componentsGrowth factorEndothelial growth factor
2012
Syndecan 4 Regulates FGFR1 Signaling in Endothelial Cells by Directing Macropinocytosis
Elfenbein A, Lanahan A, Zhou TX, Yamasaki A, Tkachenko E, Matsuda M, Simons M. Syndecan 4 Regulates FGFR1 Signaling in Endothelial Cells by Directing Macropinocytosis. Science Signaling 2012, 5: ra36. PMID: 22569333, PMCID: PMC3827948, DOI: 10.1126/scisignal.2002495.Peer-Reviewed Original ResearchConceptsFGF receptor 1Mitogen-activated protein kinaseFibroblast growth factor-2MAPK signalingSyndecan-4Inhibition of Rab5Receptor tyrosine kinasesEndothelial cell migrationHeparan sulfate proteoglycanSignal transductionProtein kinaseFGF2 stimulationEndothelial cellsMAPK activationTyrosine kinaseGrowth factor 2Genetic knockoutCell migrationReceptor complexMacropinocytosisClasses of receptorsSignalingRab5Factor 2Sulfate proteoglycan
2007
Synectin‐dependent suppression of basal Rac1 activity is reversed by a signaling pathway involving PKCalpha and RhoG
Elfenbein A, Simons M. Synectin‐dependent suppression of basal Rac1 activity is reversed by a signaling pathway involving PKCalpha and RhoG. The FASEB Journal 2007, 21: lb11-lb12. DOI: 10.1096/fasebj.21.6.lb11-d.Peer-Reviewed Original ResearchFibroblast growth factorEndothelial cellsHigh-affinity tyrosine kinase receptorsLow baseline levelsRac1 activitySerum-starved endothelial cellsHigh-affinity receptorTyrosine kinase receptorsBaseline levelsGrowth factorInhibitor-1Endothelial cell migrationHeparan sulfate proteoglycanDissociation inhibitor 1Kinase receptorsMigratory responseEarly eventsNovel roleSulfate proteoglycanCell migration
2000
Synectin, syndecan‐4 cytoplasmic domain binding PDZ protein, inhibits cell migration
Gao Y, Li M, Chen W, Simons M. Synectin, syndecan‐4 cytoplasmic domain binding PDZ protein, inhibits cell migration. Journal Of Cellular Physiology 2000, 184: 373-379. PMID: 10911369, DOI: 10.1002/1097-4652(200009)184:3<373::aid-jcp12>3.0.co;2-i.Peer-Reviewed Original ResearchConceptsSyndecan-4Cytoplasmic domainSyndecan-4 cytoplasmic domainTwo-hybrid libraryDomain-mediated interactionsNovel binding partnerInhibits cell migrationGene familyPDZ proteinsBinding partnerDependent regulationSynectinImportant regulatorCell adhesionCell migrationCell growthGrowth rateGIPCMigrationRegulatorDomainProteinTransportersOverexpressionNeuropilins