2010
Spatial control of EGF receptor activation by reversible dimerization on living cells
Chung I, Akita R, Vandlen R, Toomre D, Schlessinger J, Mellman I. Spatial control of EGF receptor activation by reversible dimerization on living cells. Nature 2010, 464: 783-787. PMID: 20208517, DOI: 10.1038/nature08827.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsCell Line, TumorCell PolarityCell SurvivalCHO CellsCricetinaeCricetulusDiffusionEnzyme ActivationEnzyme StabilityEpidermal Growth FactorErbB ReceptorsGene Expression RegulationGRB2 Adaptor ProteinHumansKineticsLigandsProtein MultimerizationProtein TransportSignal TransductionThermodynamicsConceptsLigand bindingEpidermal growth factor receptor moleculeType I receptor kinaseEGF receptor activationDimer formationReceptor kinaseReceptor dimerizationDimerization dynamicsReceptor dimersLiving cellsReceptor moleculesCell marginsDimer populationSpatial controlHuman carcinomasConformation changeDimerizationCell centerReceptor activationRate of dissociationCellsBindingActivationKinaseReversible dimerization
2005
The Abl/Arg substrate ArgBP2/nArgBP2 coordinates the function of multiple regulatory mechanisms converging on the actin cytoskeleton
Cestra G, Toomre D, Chang S, De Camilli P. The Abl/Arg substrate ArgBP2/nArgBP2 coordinates the function of multiple regulatory mechanisms converging on the actin cytoskeleton. Proceedings Of The National Academy Of Sciences Of The United States Of America 2005, 102: 1731-1736. PMID: 15659545, PMCID: PMC547834, DOI: 10.1073/pnas.0409376102.Peer-Reviewed Original ResearchConceptsActin cytoskeletonCOOH-terminal SH3 domainFocal adhesion proteinsBrain-specific splice variantCell adhesion sitesMultiple regulatory mechanismsUbiquitin ligase CblNH2-terminal regionArg tyrosine kinasesActin rufflesWAVE isoformsAdaptor proteinScaffold proteinSH3 domainTyrosine phosphorylationRegulatory proteinsAdhesion proteinsStress fibersRegulatory mechanismsTyrosine kinaseCytoskeletonDomain domainSplice variantsNeuronal synapsesProtein