2015
Comparison of Saccharomyces cerevisiae F-BAR Domain Structures Reveals a Conserved Inositol Phosphate Binding Site
Moravcevic K, Alvarado D, Schmitz KR, Kenniston JA, Mendrola JM, Ferguson KM, Lemmon MA. Comparison of Saccharomyces cerevisiae F-BAR Domain Structures Reveals a Conserved Inositol Phosphate Binding Site. Structure 2015, 23: 352-363. PMID: 25620000, PMCID: PMC4319572, DOI: 10.1016/j.str.2014.12.009.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesCrystallography, X-RayGreen Fluorescent ProteinsGTPase-Activating ProteinsHeLa CellsHumansInositol PhosphatesModels, MolecularMolecular Sequence DataProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSpecies SpecificityConceptsF-BAR domainLipid-binding specificityMembrane-binding propertiesNumerous functional studiesPhosphate binding siteUnappreciated determinantF-BARDomain bindsCell signalingCurved membranesMembrane interactionsFunctional studiesRgd1pBinding sitesX-ray crystal structureInositol phosphatesDomain structureDomainHof1pPhospholipidsRhoGAPCytokinesisEndocytosisPhosphoinositideSignaling
2013
Receptor tyrosine kinases with intracellular pseudokinase domains
Mendrola JM, Shi F, Park JH, Lemmon MA. Receptor tyrosine kinases with intracellular pseudokinase domains. Biochemical Society Transactions 2013, 41: 1029-1036. PMID: 23863174, PMCID: PMC3777422, DOI: 10.1042/bst20130104.Peer-Reviewed Original ResearchConceptsWeak kinase activityKinase activitySignificant kinase activityReceptor tyrosine kinasesPseudokinase domainHuman proteomeProtein kinaseImportant residuesWnt receptorsTyrosine kinaseEGFR familyKinaseFunctional studiesRTKPseudokinasesPseudokinaseProteomeReceptorsWntNew lightErbB3MutationsResiduesActivityRecent work
2010
Kinase Associated-1 Domains Drive MARK/PAR1 Kinases to Membrane Targets by Binding Acidic Phospholipids
Moravcevic K, Mendrola JM, Schmitz KR, Wang YH, Slochower D, Janmey PA, Lemmon MA. Kinase Associated-1 Domains Drive MARK/PAR1 Kinases to Membrane Targets by Binding Acidic Phospholipids. Cell 2010, 143: 966-977. PMID: 21145462, PMCID: PMC3031122, DOI: 10.1016/j.cell.2010.11.028.Peer-Reviewed Original ResearchConceptsKA1 domainBud neck localizationMembrane association domainAcidic phospholipidsImportance of phosphatidylserineAssociation domainMembrane associationMembrane localizationProtein kinaseC2 domainC-terminusMembrane targetsKinaseIntact proteinAnionic phospholipidsX-ray crystallographyNeck localizationPhosphatidylserinePhospholipidsCrucial roleDomainMembrane surfaceLocalizationTerminusRegulator
2006
The Dbs PH domain contributes independently to membrane targeting and regulation of guanine nucleotide-exchange activity
Baumeister MA, Rossman KL, Sondek J, Lemmon MA. The Dbs PH domain contributes independently to membrane targeting and regulation of guanine nucleotide-exchange activity. Biochemical Journal 2006, 400: 563-572. PMID: 17007612, PMCID: PMC1698603, DOI: 10.1042/bj20061020.Peer-Reviewed Original ResearchArgos Mutants Define an Affinity Threshold for Spitz Inhibition in Vivo *
Alvarado D, Evans TA, Sharma R, Lemmon MA, Duffy JB. Argos Mutants Define an Affinity Threshold for Spitz Inhibition in Vivo *. Journal Of Biological Chemistry 2006, 281: 28993-29001. PMID: 16870613, DOI: 10.1074/jbc.m603782200.Peer-Reviewed Original Research
2004
Svp1p defines a family of phosphatidylinositol 3,5‐bisphosphate effectors
Dove SK, Piper RC, McEwen RK, Yu JW, King MC, Hughes DC, Thuring J, Holmes AB, Cooke FT, Michell RH, Parker PJ, Lemmon MA. Svp1p defines a family of phosphatidylinositol 3,5‐bisphosphate effectors. The EMBO Journal 2004, 23: 1922-1933. PMID: 15103325, PMCID: PMC404323, DOI: 10.1038/sj.emboj.7600203.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAutophagy-Related ProteinsBase SequenceCloning, MolecularEndosomesEscherichia coliGene ComponentsGenetic VectorsGreen Fluorescent ProteinsMembrane ProteinsMolecular Sequence DataPhosphatidylinositol PhosphatesPhosphotransferases (Alcohol Group Acceptor)PlasmidsProtein BindingProtein FoldingProtein TransportRhinovirusSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSequence Analysis, DNAVacuolesConceptsFamily of phosphatidylinositolSaccharomyces cerevisiae mutantsDrosophila homologueCerevisiae mutantsMembrane recyclingVesicle recyclingVacuole enlargementVacuole membraneMultivesicular bodiesRelated proteinsLysosomal compartmentMarker proteinsExquisite specificityEffectorsProteinPhosphatidylinositolVacuolesEukaryotesCellsMutantsLocalisesGolgiHomologuesMVBGenesThe 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 receptorAll Phox Homology (PX) Domains from Saccharomyces cerevisiae Specifically Recognize Phosphatidylinositol 3-Phosphate*
Yu J, Lemmon M. All Phox Homology (PX) Domains from Saccharomyces cerevisiae Specifically Recognize Phosphatidylinositol 3-Phosphate*. Journal Of Biological Chemistry 2001, 276: 44179-44184. PMID: 11557775, DOI: 10.1074/jbc.m108811200.Peer-Reviewed Original Research
2000
Crystal Structure of Fibroblast Growth Factor 9 Reveals Regions Implicated in Dimerization and Autoinhibition*
Plotnikov A, Eliseenkova A, Ibrahimi O, Shriver Z, Sasisekharan R, Lemmon M, Mohammadi M. Crystal Structure of Fibroblast Growth Factor 9 Reveals Regions Implicated in Dimerization and Autoinhibition*. Journal Of Biological Chemistry 2000, 276: 4322-4329. PMID: 11060292, DOI: 10.1074/jbc.m006502200.Peer-Reviewed Original ResearchStructural Basis for Discrimination of 3-Phosphoinositides by Pleckstrin Homology Domains
Ferguson K, Kavran J, Sankaran V, Fournier E, Isakoff S, Skolnik E, Lemmon M. Structural Basis for Discrimination of 3-Phosphoinositides by Pleckstrin Homology Domains. Molecular Cell 2000, 6: 373-384. PMID: 10983984, DOI: 10.1016/s1097-2765(00)00037-x.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceBinding SitesBlood ProteinsCrystallography, X-RayFatty AcidsHydrogen BondingInositol PhosphatesLipoproteinsModels, MolecularMolecular Sequence DataPhosphatidylinositol 3-KinasesPhosphatidylinositolsProtein Structure, SecondarySequence AlignmentSequence Homology, Amino AcidSignal TransductionSrc Homology DomainsSubstrate SpecificityConceptsPleckstrin homology domainPH domainHomology domainDifferent PH domainsPhosphoinositide specificityMembrane recruitmentProtein modulesCellular signalingStructural basisHost proteinsSecond messengerMajor PIAmino acidsX-ray crystal structureProteinDomainPhosphoinositideHead groupsSignalingMessengerBindsCrystal structureRecruitment
1998
The Pleckstrin Homology Domains of Dynamin Isoforms Require Oligomerization for High Affinity Phosphoinositide Binding*
Klein D, Lee A, Frank D, Marks M, Lemmon M. The Pleckstrin Homology Domains of Dynamin Isoforms Require Oligomerization for High Affinity Phosphoinositide Binding*. Journal Of Biological Chemistry 1998, 273: 27725-27733. PMID: 9765310, DOI: 10.1074/jbc.273.42.27725.Peer-Reviewed Original Research
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 roleDomainIsoformsDimerization of the p185neu transmembrane domain is necessary but not sufficient for transformation
Burke C, Lemmon M, Coren B, Engelman D, Stern D. Dimerization of the p185neu transmembrane domain is necessary but not sufficient for transformation. Oncogene 1997, 14: 687-696. PMID: 9038376, DOI: 10.1038/sj.onc.1200873.Peer-Reviewed Original ResearchConceptsReceptor tyrosine kinasesTransmembrane domainEpidermal growth factor receptorSignal transductionWild-type domainSecond-site mutationsPosition 664Dimerization domainGrowth factor receptorTyrosine kinaseGlycophorin AFactor receptorValine substitutionDimerizationMutationsTransductionGlutamic acidDomainWeak dimerizationMutantsKinaseSignalingProteinEGFChimeras
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 StatementsThermodynamic 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
1995
Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain
Ferguson K, Lemmon M, Schlessinger J, Sigler P. Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. Cell 1995, 83: 1037-1046. PMID: 8521504, DOI: 10.1016/0092-8674(95)90219-8.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesBlood ProteinsCrystallography, X-RayInositol 1,4,5-TrisphosphateIsoenzymesMolecular ConformationMolecular Sequence DataPhospholipase C gammaPhosphoproteinsProtein ConformationRatsSequence AlignmentSequence Homology, Amino AcidSpectrinType C PhospholipasesConceptsPleckstrin homology domainHigh-affinity complexHomology domainPH domainPhospholipase C-delta 1C-delta 1Affinity complexHead group specificityMembrane targetingLoss of functionSignaling proteinsDomain foldsMutational changesBtk mutantsRegulatory functionsAmino acidsX-ray crystal structureBeta 2Beta 1/beta 2InositolDomainMutantsComplexesProteinTrisphosphate
1994
Crystal structure at 2.2 Å resolution of the pleckstrin homology domain from human dynamin
Ferguson K, Lemmon M, Schlessinger J, Sigler P. Crystal structure at 2.2 Å resolution of the pleckstrin homology domain from human dynamin. Cell 1994, 79: 199-209. PMID: 7954789, DOI: 10.1016/0092-8674(94)90190-2.Peer-Reviewed Original ResearchThermodynamic studies of tyrosyl-phosphopeptide binding to the SH2 domain of p56lck.
Lemmon MA, Ladbury JE. Thermodynamic studies of tyrosyl-phosphopeptide binding to the SH2 domain of p56lck. Biochemistry 1994, 33: 5070-6. PMID: 7513553, DOI: 10.1021/bi00183a010.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsBinding SitesCalorimetryCloning, MolecularConserved SequenceErbB ReceptorsEscherichia coliLymphocyte Specific Protein Tyrosine Kinase p56(lck)LymphocytesMolecular Sequence DataPeptide FragmentsPhosphopeptidesPhosphotyrosineProtein-Tyrosine KinasesRecombinant ProteinsSequence Homology, Amino AcidTyrosineA dimerization motif for transmembrane α–helices
Lemmon M, Treutlein H, Adams P, Brünger A, Engelman D. A dimerization motif for transmembrane α–helices. Nature Structural & Molecular Biology 1994, 1: 157-163. PMID: 7656033, DOI: 10.1038/nsb0394-157.Peer-Reviewed Original ResearchConceptsTransmembrane α-helicesHydrophobic transmembrane α-helicesSpecific helix-helix interactionsΑ-helixIntegral membrane proteinsHelix-helix interactionsHelix-helix interfaceDimerization motifSpecific dimerizationMembrane proteinsHelix associationFunctional analysisAmino acidsSuch motifsLipid bilayersMotifParticular motifsFoldingDimerizationSuch interactionsComplex membranesProteinOligomerizationVariety of systemsInteraction