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 factorDifferential TAM receptor–ligand–phospholipid interactions delimit differential TAM bioactivities
Lew ED, Oh J, Burrola PG, Lax I, Zagórska A, Través PG, Schlessinger J, Lemke G. Differential TAM receptor–ligand–phospholipid interactions delimit differential TAM bioactivities. ELife 2014, 3: e03385. PMID: 25265470, PMCID: PMC4206827, DOI: 10.7554/elife.03385.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxl Receptor Tyrosine KinaseBone Marrow CellsCell LineC-Mer Tyrosine KinaseEmbryo, MammalianFemaleFibroblastsGene Expression RegulationHEK293 CellsHumansIntercellular Signaling Peptides and ProteinsMaleMiceMice, Inbred C57BLMice, KnockoutPhagocytosisPhosphatidylserinesPrimary Cell CultureProtein SProto-Oncogene ProteinsReceptor Protein-Tyrosine KinasesRecombinant ProteinsSignal TransductionConceptsActivation of MerWild-type affinityReceptor tyrosine kinasesCellular physiologyReceptor-ligand engagementTAM receptor tyrosine kinasesGenetic analysisLigand specificityTyrosine kinaseLigand engagementPhospholipid phosphatidylserineGla domainPhospholipid interactionsDifferential activityProtein SAxlGas6PhosphatidylserinePhagocytosisPredominant roleKinasePhysiologyRegulationActivationReceptors