2017
Dimerization of Tie2 mediated by its membrane-proximal FNIII domains
Moore JO, Lemmon MA, Ferguson KM. Dimerization of Tie2 mediated by its membrane-proximal FNIII domains. Proceedings Of The National Academy Of Sciences Of The United States Of America 2017, 114: 4382-4387. PMID: 28396397, PMCID: PMC5410832, DOI: 10.1073/pnas.1617800114.Peer-Reviewed Original ResearchConceptsExtracellular regionFNIII domainsResolution X-ray crystal structureMembrane-proximal fibronectin type III domainsDomain-mediated interactionsDifferent cellular contextsLigand-binding regionHigher-order oligomersTie2 activationFibronectin type III domainReceptor tyrosine kinasesTyrosine kinase familyEGF-homology domainThird FNIII domainType III domainPrevious structural studiesStructural studiesHomology domainCellular contextKinase familyDimer interfaceDimerization modeReceptor dimerizationTyrosine kinasePrimary activator
2011
Conditional Peripheral Membrane Proteins: Facing up to Limited Specificity
Moravcevic K, Oxley CL, Lemmon MA. Conditional Peripheral Membrane Proteins: Facing up to Limited Specificity. Structure 2011, 20: 15-27. PMID: 22193136, PMCID: PMC3265387, DOI: 10.1016/j.str.2011.11.012.Peer-Reviewed Original Research
2006
EGF-independent activation of cell-surface EGF receptors harboring mutations found in gefitinib-sensitive lung cancer
Choi SH, Mendrola JM, Lemmon MA. EGF-independent activation of cell-surface EGF receptors harboring mutations found in gefitinib-sensitive lung cancer. Oncogene 2006, 26: 1567-1576. PMID: 16953218, DOI: 10.1038/sj.onc.1209957.Peer-Reviewed Original ResearchConceptsEpidermal growth factor receptorTyrosine kinase domainKinase domainEGF receptorRecent structural studiesSomatic mutationsCell surface EGF receptorsTyrosine kinase activityAbsence of EGFAutoinhibitory interactionsActivation loopErbB family membersGrowth factor receptorTyrosine phosphorylationEGFR tyrosine kinase domainKinase activityNull backgroundMechanistic basisOncogenic mutationsBiochemical propertiesCell surfaceCell lung carcinoma patientsFactor receptorMutationsLung carcinoma patientsPalmitoylation 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
2005
Membrane activity of the phospholipase C-δ1 pleckstrin homology (PH) domain
Flesch FM, Yu JW, Lemmon MA, Burger KN. Membrane activity of the phospholipase C-δ1 pleckstrin homology (PH) domain. Biochemical Journal 2005, 389: 435-441. PMID: 15755258, PMCID: PMC1175121, DOI: 10.1042/bj20041721.Peer-Reviewed Original Research
2004
ErbB3/HER3 does not homodimerize upon neuregulin binding at the cell surface
Berger MB, Mendrola JM, Lemmon MA. ErbB3/HER3 does not homodimerize upon neuregulin binding at the cell surface. FEBS Letters 2004, 569: 332-336. PMID: 15225657, DOI: 10.1016/j.febslet.2004.06.014.Peer-Reviewed Original ResearchGenome-Wide Analysis of Membrane Targeting by S. cerevisiae Pleckstrin Homology Domains
Yu JW, Mendrola JM, Audhya A, Singh S, Keleti D, DeWald DB, Murray D, Emr SD, Lemmon MA. Genome-Wide Analysis of Membrane Targeting by S. cerevisiae Pleckstrin Homology Domains. Molecular Cell 2004, 13: 677-688. PMID: 15023338, DOI: 10.1016/s1097-2765(04)00083-8.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesBlood ProteinsCalcium-Binding ProteinsCell MembraneCytoskeletal ProteinsGene Expression Regulation, FungalGenome, FungalPhosphatidylinositolsPhosphoproteinsProtein BindingProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidConceptsPH domain bindsMembrane targetingPH domainDomain bindsPhosphoinositide-dependent mannerS. cerevisiae genomeSmall protein modulesPleckstrin homology domainProteome-wide analysisFunction of proteinsMembrane recruitmentCerevisiae genomePhosphoinositide bindingPleckstrin homologyHomology domainProtein modulesWide analysisSubcellular localizationHost proteinsBindsLittle specificityPhosphoinositideProteinHigh affinityCommon domainThe p21-activated Protein Kinase-related Kinase Cla4 Is a Coincidence Detector of Signaling by Cdc42 and Phosphatidylinositol 4-Phosphate*
Wild AC, Yu JW, Lemmon MA, Blumer KJ. The p21-activated Protein Kinase-related Kinase Cla4 Is a Coincidence Detector of Signaling by Cdc42 and Phosphatidylinositol 4-Phosphate*. Journal Of Biological Chemistry 2004, 279: 17101-17110. PMID: 14766750, DOI: 10.1074/jbc.m314035200.Peer-Reviewed Original ResearchMeSH KeywordsAllelesAmino Acid SequenceCdc42 GTP-Binding ProteinCell MembraneDose-Response Relationship, DrugEscherichia coliGenotypeGreen Fluorescent ProteinsImmunoblottingKineticsLipid MetabolismLuminescent ProteinsMitosisModels, GeneticMolecular Sequence DataMutationP21-Activated KinasesPhosphatidylinositol PhosphatesPlasmidsPoint MutationProtein BindingProtein Serine-Threonine KinasesProtein Structure, TertiaryRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSignal TransductionSurface Plasmon ResonanceTemperatureConceptsPleckstrin homologyPH domainRho-type GTPase Cdc42P21-activated protein kinaseMitotic exit networkPlasma membrane poolSignal transduction pathwaysPhosphoinositide speciesGolgi poolCell morphogenesisEukaryotic cellsGTPase Cdc42Cdc42 bindingKinase mutantsMammalian cellsCla4Protein kinaseTransduction pathwaysCoincidence detectorMembrane poolPlasma membraneCdc42Kinase activityPI4PBiological processes
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
2000
The Role of the Pleckstrin Homology Domain in Membrane Targeting and Activation of Phospholipase Cβ1 *
Razzini G, Brancaccio A, Lemmon M, Guarnieri S, Falasca M. The Role of the Pleckstrin Homology Domain in Membrane Targeting and Activation of Phospholipase Cβ1 *. Journal Of Biological Chemistry 2000, 275: 14873-14881. PMID: 10809731, DOI: 10.1074/jbc.275.20.14873.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAndrostadienesAnimalsCell MembraneChromonesCOS CellsCulture Media, Serum-FreeEnzyme ActivationEnzyme InhibitorsGlutathione TransferaseGreen Fluorescent ProteinsGrowth SubstancesGTP-Binding ProteinsHeLa CellsHumansIsoenzymesLuminescent ProteinsMiceMicroscopy, ConfocalMicroscopy, FluorescenceMorpholinesPhosphatidylinositolsPhospholipase C betaPolymerase Chain ReactionRatsRecombinant Fusion ProteinsSrc Homology DomainsTransfectionType C PhospholipasesWortmanninConceptsPlasma membrane localizationPleckstrin homology domainMembrane localizationSerum-starved cellsPlasma membraneMembrane targetingLysophosphatidic acidHomology domainGreen fluorescent protein fusion proteinFluorescent protein fusion proteinProtein fusion proteinIsolated PH domainActivation of PLCbetaStimulation of cellsPH domainPhospholipase Cβ1Gbetagamma subunitsBetagamma subunitsAmino terminusWortmannin pretreatmentFusion proteinG proteinsActivation of phospholipaseFluorescence microscopyPhosphoinositide
1998
Phosphatidylinositol-4,5-bisphosphate is required for endocytic coated vesicle formation
Jost M, Simpson F, Kavran J, Lemmon M, Schmid S. Phosphatidylinositol-4,5-bisphosphate is required for endocytic coated vesicle formation. Current Biology 1998, 8: 1399-1404. PMID: 9889104, DOI: 10.1016/s0960-9822(98)00022-0.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex 2Adaptor Proteins, Vesicular TransportBiotinCell MembraneClathrinEndocytosisEndosomesHumansIsoenzymesMutagenesisNeomycinNerve Tissue ProteinsPhosphatidylinositol 4,5-DiphosphatePhospholipase C deltaPhosphoproteinsProtein BindingTransferrinTumor Cells, CulturedType C PhospholipasesConceptsCoated vesicle formationEndocytic coated vesicle formationVesicle formationPleckstrin homology domainClathrin-coated vesiclesInvolvement of phosphatidylinositolReceptor-mediated endocytosisBind phosphatidylinositolGTPase dynaminAP2 complexProtein playersEndocytic motifEndocytic machineryHomology domainPH domainCoat assemblyInositol polyphosphateHigh-specificity probesGTPase activityInositol lipidsPhosphatidylinositolFirst direct evidenceDirect evidenceClathrinEndocytosisIdentification and analysis of PH domain‐containing targets of phosphatidylinositol 3‐kinase using a novel in vivo assay in yeast
Isakoff S, Cardozo T, Andreev J, Li Z, Ferguson K, Abagyan R, Lemmon M, Aronheim A, Skolnik E. Identification and analysis of PH domain‐containing targets of phosphatidylinositol 3‐kinase using a novel in vivo assay in yeast. The EMBO Journal 1998, 17: 5374-5387. PMID: 9736615, PMCID: PMC1170863, DOI: 10.1093/emboj/17.18.5374.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBlood ProteinsCell MembraneConsensus SequenceConserved SequenceFungal ProteinsModels, MolecularMutationPhosphatidylinositol 3-KinasesPhosphatidylinositol PhosphatesPhosphoproteinsProtein BindingRas ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiaeSecond Messenger SystemsSequence Homology, Amino AcidConceptsPI3K productsPH domainNon-permissive temperaturePH domain-containing proteinsRas exchange factorK productDomain-containing proteinsPleckstrin homology domainExchange factorHomology domainYeast SaccharomycesNovel cDNAConsensus sequenceFusion proteinSecond messengerCellular responsesPI3KAmino acidsHigh affinityYeastYeast growthProteinPhosphatidylinositolNovel assayPowerful approach
1996
PH Domains: Diverse Sequences with a Common Fold Recruit Signaling Molecules to the Cell Surface
Lemmon M, Ferguson K, Schlessinger J. PH Domains: Diverse Sequences with a Common Fold Recruit Signaling Molecules to the Cell Surface. Cell 1996, 85: 621-624. PMID: 8646770, DOI: 10.1016/s0092-8674(00)81022-3.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus Statements
1994
Specificity and promiscuity in membrane helix interactions
Lemmon M, Engelman D. Specificity and promiscuity in membrane helix interactions. Quarterly Reviews Of Biophysics 1994, 27: 157-218. PMID: 7984776, DOI: 10.1017/s0033583500004522.Peer-Reviewed Original ResearchConceptsIntegral membrane proteinsTransmembrane α-helicesMembrane proteinsΑ-helixMembrane protein foldingMembrane-spanning portionTransmembrane helix associationHelix-helix interactionsParticular helicesProtein foldingHelix associationHelix interactionsProsthetic groupLipid bilayersCharge-charge interactionsStereochemical fitFoldingProteinAccessible statesSpecificityOligomerizationInteractionPromiscuityHelixAssembly