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
Genome-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 domain
2000
Signal-dependent membrane targeting by pleckstrin homology (PH) domains
LEMMON M, FERGUSON K. Signal-dependent membrane targeting by pleckstrin homology (PH) domains. Biochemical Journal 2000, 350: 1-18. DOI: 10.1042/bj3500001.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsPleckstrin homology domainPH domainHomology domainSignal-dependent recruitmentSmall protein modulesDifferent protein ligandsMost PH domainsGreen fluorescent proteinMembrane associationProtein modulesCellular signalingDynamin 1Cytoskeletal rearrangementsCell signalingOligomeric statePlasma membraneMembrane bindingStructural basisHost proteinsFluorescent proteinProtein ligandsPhysiological functionsPhysiological roleAmino acidsPhosphoinositideStructural 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
Specificity and Promiscuity in Phosphoinositide Binding by Pleckstrin Homology Domains*
Kavran J, Klein D, Lee A, Falasca M, Isakoff S, Skolnik E, Lemmon M. Specificity and Promiscuity in Phosphoinositide Binding by Pleckstrin Homology Domains*. Journal Of Biological Chemistry 1998, 273: 30497-30508. PMID: 9804818, DOI: 10.1074/jbc.273.46.30497.Peer-Reviewed Original ResearchConceptsPleckstrin homology domainPH domainGrp1 PH domainD-myo-inositolParticular phosphoinositidesPhosphoinositide bindingHomology domainDependent membrane recruitmentDifferent PH domainsPH domain bindsSmall protein modulesSoluble inositol phosphatesMembrane recruitmentDomain bindsProtein modulesSpecific phosphoinositideMammalian cellsPlasma membraneSingle speciesAbundant speciesMultiple phosphoinositidesCellular membranesPhosphoinositidePI 3Clear specificity
1997
Regulatory recruitment of signalling molecules to the cell membrane by pleckstrinhomology domains
M.A. L, M. F, J. S, K. F. Regulatory recruitment of signalling molecules to the cell membrane by pleckstrinhomology domains. Trends In Cell Biology 1997, 7: 237-242. PMID: 17708952, DOI: 10.1016/s0962-8924(97)01065-9.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsCell membraneSmall protein modulesPleckstrin homology domainPH domainProtein modulesBiological functionsDiverse processesCertain proteinsSpecific membraneProtein synthesisCell adhesionDNA synthesisProteinMembraneRecent studiesRecruitmentDomainPhosphoinositideEfficient mechanismRegulationPathwayCellsFunctionAdhesion