2006
Palmitoylation of the EGFR Ligand Spitz by Rasp Increases Spitz Activity by Restricting Its Diffusion
Miura GI, Buglino J, Alvarado D, Lemmon MA, Resh MD, Treisman JE. Palmitoylation of the EGFR Ligand Spitz by Rasp Increases Spitz Activity by Restricting Its Diffusion. Developmental Cell 2006, 10: 167-176. PMID: 16459296, DOI: 10.1016/j.devcel.2005.11.017.Peer-Reviewed Original ResearchMeSH KeywordsAcyltransferasesAnimalsBase SequenceBiological Transport, ActiveCell LineCell MembraneCysteineDNADrosophilaDrosophila ProteinsEpidermal Growth FactorErbB ReceptorsFemaleGenes, InsectIn Vitro TechniquesLigandsMaleMembrane ProteinsModels, BiologicalMutagenesis, Site-DirectedMutationOvaryPalmitic AcidRecombinant ProteinsTransfectionWings, AnimalConceptsEpidermal growth factor receptorDrosophila epidermal growth factor receptorEGFR ligand SpitzPlasma membrane associationN-terminal cysteine residueLigand SpitzMembrane associationWnt familyDevelopmental functionsGrowth factor receptorCysteine residuesBiological functionsLipid modificationPalmitoylationIntracellular proteinsCultured cellsCell membraneFactor receptorSpitzReduced activityVivoTransmembraneHedgehogProteinActivity
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