2006
Essential Role for Rac in Heregulin β1 Mitogenic Signaling: a Mechanism That Involves Epidermal Growth Factor Receptor and Is Independent of ErbB4
Yang C, Liu Y, Lemmon MA, Kazanietz MG. Essential Role for Rac in Heregulin β1 Mitogenic Signaling: a Mechanism That Involves Epidermal Growth Factor Receptor and Is Independent of ErbB4. Molecular And Cellular Biology 2006, 26: 831-842. PMID: 16428439, PMCID: PMC1347034, DOI: 10.1128/mcb.26.3.831-842.2006.Peer-Reviewed Original ResearchMeSH KeywordsAntibodies, BlockingBreast NeoplasmsCell MovementCell ProliferationEnzyme ActivationErbB ReceptorsFemaleHumansNeoplasm ProteinsNeuregulin-1Phosphatidylinositol 3-KinasesPhosphoinositide-3 Kinase InhibitorsProtein Kinase InhibitorsProto-Oncogene Proteins c-aktReceptor, ErbB-2Receptor, ErbB-3Receptor, ErbB-4RNA InterferenceSrc-Family KinasesTumor Cells, CulturedConceptsExtracellular signal-regulated kinaseHeregulin beta1RNA interferenceBreast cancer cellsCancer cellsActin cytoskeleton reorganizationDepletion of Rac1Activation of RacInactivation of RacTransactivation of EGFRSignal-regulated kinaseErbB receptor inhibitorsEpidermal growth factor receptorRho GTPasesMitogenic signalingRac activationRac GTPaseEpidermal growth factorGrowth factor receptorCytoskeleton reorganizationDownstream effectorsMitogenic activityCancer cell proliferationERK activationBreast cancer cell proliferation
1997
Two EGF molecules contribute additively to stabilization of the EGFR dimer
Lemmon M, Bu Z, Ladbury J, Zhou M, Pinchasi D, Lax I, Engelman D, Schlessinger J. Two EGF molecules contribute additively to stabilization of the EGFR dimer. The EMBO Journal 1997, 16: 281-294. PMID: 9029149, PMCID: PMC1169635, DOI: 10.1093/emboj/16.2.281.Peer-Reviewed Original ResearchConceptsEpidermal growth factorReceptor dimerizationEGF moleculesPrecise molecular detailsHuman growth hormone receptorReceptor-receptor interactionsGrowth factorInterferon-gamma receptorEGFR dimersSignaling eventsMolecular detailsReceptor oligomerizationGrowth hormone receptorExtracellular domainEGFR familyCell surfaceMonomer bindsSubsequent associationDimerizationHormone receptorsTitration calorimetrySmall-angle X-ray scatteringBindingReceptorsMultivalent binding
1994
Regulation of signal transduction and signal diversity by receptor oligomerization
Lemmon M, Schlessinger J. Regulation of signal transduction and signal diversity by receptor oligomerization. Trends In Biochemical Sciences 1994, 19: 459-463. PMID: 7855887, DOI: 10.1016/0968-0004(94)90130-9.Peer-Reviewed Original ResearchConceptsReceptor oligomerizationProtein tyrosine kinase activityTyrosine kinase activityDiversity of ligandsGrowth factorCytoplasmic domainSignal transductionEpidermal growth factorKinase activityExtracellular domainDifferent complementsSame receptor familySignal diversityReceptor familyIndividual receptorsOligomerizationHeterodimerizationDiversityAccessory moleculesReceptorsImportant roleSH2TransmembraneTransductionDomain