2020
Structural Insights into Pseudokinase Domains of Receptor Tyrosine Kinases
Sheetz JB, Mathea S, Karvonen H, Malhotra K, Chatterjee D, Niininen W, Perttilä R, Preuss F, Suresh K, Stayrook SE, Tsutsui Y, Radhakrishnan R, Ungureanu D, Knapp S, Lemmon MA. Structural Insights into Pseudokinase Domains of Receptor Tyrosine Kinases. Molecular Cell 2020, 79: 390-405.e7. PMID: 32619402, PMCID: PMC7543951, DOI: 10.1016/j.molcel.2020.06.018.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBaculoviridaeBinding SitesCell Adhesion MoleculesCell LineCloning, MolecularCrystallography, X-RayGene ExpressionHumansMiceModels, MolecularPrecursor Cells, B-LymphoidProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsProtein Kinase InhibitorsReceptor Protein-Tyrosine KinasesReceptor Tyrosine Kinase-like Orphan ReceptorsReceptors, Eph FamilyRecombinant ProteinsSf9 CellsSmall Molecule LibrariesSpodopteraStructural Homology, ProteinSubstrate SpecificityConceptsInsulin receptor kinasePseudokinase domainReceptor tyrosine kinasesTyrosine kinaseNon-catalytic functionsATP-binding pocketType II inhibitorsDomain plasticityActivation loopReceptor kinaseInactive conformationStructural insightsPseudokinasesATP siteStructural comparisonAromatic residuesKinaseAlternative interactionsApparent lackImportant roleDomainWntMotifROR1Residues
2017
Molecular determinants of KA1 domain-mediated autoinhibition and phospholipid activation of MARK1 kinase.
Emptage RP, Lemmon MA, Ferguson KM. Molecular determinants of KA1 domain-mediated autoinhibition and phospholipid activation of MARK1 kinase. Biochemical Journal 2017, 474: 385-398. PMID: 27879374, PMCID: PMC5317272, DOI: 10.1042/bcj20160792.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsBinding SitesCloning, MolecularEnzyme AssaysEscherichia coliGene ExpressionHumansKineticsMitogen-Activated Protein Kinase 1Models, MolecularPeptidesPhospholipidsProtein BindingProtein Interaction Domains and MotifsProtein Structure, SecondaryRecombinant ProteinsScattering, Small AngleSubstrate SpecificityX-Ray DiffractionConceptsKA1 domainMAP/microtubule affinity-regulating kinasesMicrotubule affinity-regulating kinaseGroup of kinasesIntramolecular autoinhibitory interactionAnionic phospholipid bindingAnionic phospholipidsSite-directed mutagenesisAutoinhibitory interactionsRegulatory modulesAutoinhibitory roleProtein modulesMembrane-bound targetsRelated kinasesBind membranesFamily kinasesKinase domainProtein kinasePhospholipid activationC-terminusRegulatory mechanismsPhospholipid bindingMechanistic basisKinaseAutoinhibitory activity
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 ResearchSvp1p 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 specificityEffectorsProteinPhosphatidylinositolVacuolesEukaryotesCellsMutantsLocalisesGolgiHomologuesMVBGenes
1994
Thermodynamic 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 AcidTyrosine