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
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
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