2009
The Juxtamembrane Region of the EGF Receptor Functions as an Activation Domain
Brewer M, Choi SH, Alvarado D, Moravcevic K, Pozzi A, Lemmon MA, Carpenter G. The Juxtamembrane Region of the EGF Receptor Functions as an Activation Domain. Molecular Cell 2009, 34: 641-651. PMID: 19560417, PMCID: PMC2719887, DOI: 10.1016/j.molcel.2009.04.034.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding SitesCarcinoma, Non-Small-Cell LungCell LineCell Transformation, NeoplasticChlorocebus aethiopsCOS CellsCrystallography, X-RayDimerizationErbB ReceptorsHumansMiceModels, MolecularMutagenesis, Site-DirectedMutationNIH 3T3 CellsPhosphorylationProtein Structure, TertiaryTyrosineConceptsEpidermal growth factor receptorActivation domainJuxtamembrane regionJM regionGrowth factor receptorIntracellular juxtamembrane regionEGF receptor functionAlanine-scanning mutagenesisFactor receptorTyrosine kinase activationAsymmetric dimerTyrosine kinase domainAutoinhibitory interactionsKinase domainCellular transformationScanning mutagenesisKinase activationEGFR activationC-lobeXenograft assayCancer mutationsC-terminal 19 residuesCrystallographic approachReceptor functionExtensive contacts
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
2003
Loss of Phosphatidylinositol 3-Phosphate Binding by the C-terminal Tiam-1 Pleckstrin Homology Domain Prevents in Vivo Rac1 Activation without Affecting Membrane Targeting*
Baumeister MA, Martinu L, Rossman KL, Sondek J, Lemmon MA, Chou MM. Loss of Phosphatidylinositol 3-Phosphate Binding by the C-terminal Tiam-1 Pleckstrin Homology Domain Prevents in Vivo Rac1 Activation without Affecting Membrane Targeting*. Journal Of Biological Chemistry 2003, 278: 11457-11464. PMID: 12525493, DOI: 10.1074/jbc.m211901200.Peer-Reviewed Original Research
2001
The Single Transmembrane Domains of ErbB Receptors Self-associate in Cell Membranes*
Mendrola JM, Berger MB, King MC, Lemmon MA. The Single Transmembrane Domains of ErbB Receptors Self-associate in Cell Membranes*. Journal Of Biological Chemistry 2001, 277: 4704-4712. PMID: 11741943, DOI: 10.1074/jbc.m108681200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceCell MembraneChloramphenicol O-AcetyltransferaseDimerizationDNA Mutational AnalysisErbB ReceptorsEscherichia coliGenetic VectorsGlutamic AcidHumansLigandsMaltoseModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutationProtein Structure, TertiaryReceptor Protein-Tyrosine KinasesReceptor, ErbB-2Receptor, ErbB-3Receptor, ErbB-4Recombinant Fusion ProteinsSequence Homology, Amino AcidValineConceptsTM domain interactionsTM domainReceptor tyrosine kinasesEpidermal growth factor receptorGrowth factor receptorDomain interactionsSingle transmembrane alpha-helixReceptor dimersTyrosine kinaseExtracellular domainErbB receptor functionEscherichia coli cell membraneSingle transmembrane domainTransmembrane alpha-helixErbB receptorsCell membraneLimited mutational analysisFactor receptorGlutamic acid mutationTransmembrane domainGxxxG motifDomain dimerMutational analysisAlpha-helixErythropoietin receptor
1997
Specific role for the PH domain of dynamin‐1 in the regulation of rapid endocytosis in adrenal chromaffin cells
Artalejo C, Lemmon M, Schlessinger J, Palfrey H. Specific role for the PH domain of dynamin‐1 in the regulation of rapid endocytosis in adrenal chromaffin cells. The EMBO Journal 1997, 16: 1565-1574. PMID: 9130701, PMCID: PMC1169760, DOI: 10.1093/emboj/16.7.1565.Peer-Reviewed Original ResearchMeSH KeywordsAdrenal MedullaAmino Acid SequenceAnimalsBlood ProteinsCattleChromaffin CellsDynamin IDynaminsEndocytosisGenetic VariationGTP PhosphohydrolasesHumansModels, StructuralMolecular Sequence DataMutagenesis, Site-DirectedPatch-Clamp TechniquesPhosphoproteinsPolymerase Chain ReactionProtein Structure, SecondaryRecombinant ProteinsSequence Homology, Amino AcidConceptsPH domainDynamin 1Rapid endocytosisPleckstrin homology domainAmino acidsDynamin PH domainIsolated PH domainTypes of endocytosisChromaffin cellsHomology domainDynamin 2Mutational studiesEquivalent residuesEndocytotic processDifferent isoformsAdrenal chromaffin cellsEndocytosisDynaminVariable loopScission eventsSpecific roleCellsKey roleDomainIsoforms
1996
Thermodynamic Studies of SHC Phosphotyrosine Interaction Domain Recognition of the NPXpY Motif (∗)
Mandiyan V, O'Brien R, Zhou M, Margolis B, Lemmon M, Sturtevant J, Schlessinger J. Thermodynamic Studies of SHC Phosphotyrosine Interaction Domain Recognition of the NPXpY Motif (∗). Journal Of Biological Chemistry 1996, 271: 4770-4775. PMID: 8617744, DOI: 10.1074/jbc.271.9.4770.Peer-Reviewed Original ResearchAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAmino Acid SequenceBinding SitesCalorimetryErbB ReceptorsGlutathione TransferaseMolecular Sequence DataMutagenesis, Site-DirectedPeptide FragmentsPhosphotyrosinePoint MutationProtein BiosynthesisProteinsRecombinant Fusion ProteinsShc Signaling Adaptor ProteinsSrc Homology DomainsThermodynamics