2009
Role of Inn1 and its interactions with Hof1 and Cyk3 in promoting cleavage furrow and septum formation in S. cerevisiae
Nishihama R, Schreiter JH, Onishi M, Vallen EA, Hanna J, Moravcevic K, Lippincott MF, Han H, Lemmon MA, Pringle JR, Bi E. Role of Inn1 and its interactions with Hof1 and Cyk3 in promoting cleavage furrow and septum formation in S. cerevisiae. Journal Of Cell Biology 2009, 185: 995-1012. PMID: 19528296, PMCID: PMC2711614, DOI: 10.1083/jcb.200903125.Peer-Reviewed Original ResearchConceptsCleavage furrowChitin synthase Chs2C-terminal regionActomyosin ring contractionCytokinesis proteinsDivision siteMitotic exitPXXP motifSH3 domainSeptum formationC2 domainS. cerevisiaePlasma membraneBind phospholipidsAMR contractionN-terminusCyk3Inn1Extracellular matrixChs2ProteinImportant interactionsHof1MembraneCytokinesis
2007
Investigation of Novel Molecular Targets for Pleckstrin Homology (PH) Domains Found in Oncogenes Implicated in Breast Cancer
Keleti D, Lemmon M. Investigation of Novel Molecular Targets for Pleckstrin Homology (PH) Domains Found in Oncogenes Implicated in Breast Cancer. 2007 DOI: 10.21236/ada469536.Peer-Reviewed Original ResearchHomology domainPH domainHuman PH domainsOSBP PH domainHost adaptor proteinsMembrane-targeting modulesPleckstrin homology domainGTPase Arf1Adaptor proteinNovel molecular targetsS. cerevisiaePlasma membraneMembrane lipidsSpecific membraneHigh affinityPPInsDirect interactionComparable affinityDomain classesMolecular targetsGolgiBinding propertiesMembraneRecent studiesAffinity
2006
Specificity of the Myotubularin Family of Phosphatidylinositol-3-phosphatase Is Determined by the PH/GRAM Domain*
Choudhury P, Srivastava S, Li Z, Ko K, Albaqumi M, Narayan K, Coetzee W, Lemmon M, Skolnik E. Specificity of the Myotubularin Family of Phosphatidylinositol-3-phosphatase Is Determined by the PH/GRAM Domain*. Journal Of Biological Chemistry 2006, 281: 31762-31769. DOI: 10.1016/s0021-9258(19)84091-7.Peer-Reviewed Original Research
2004
The 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
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 acidsPhosphoinositideThe 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
1999
Dominant-negative inhibition of receptor-mediated endocytosis by a dynamin-1 mutant with a defective pleckstrin homology domain
Lee A, Frank D, Marks M, Lemmon M. Dominant-negative inhibition of receptor-mediated endocytosis by a dynamin-1 mutant with a defective pleckstrin homology domain. Current Biology 1999, 9: 261-265. PMID: 10074457, DOI: 10.1016/s0960-9822(99)80115-8.Peer-Reviewed Original ResearchConceptsPleckstrin homology domainPH domainReceptor-mediated endocytosisDynamin 1Homology domainEndocytic vesiclesPH domain bindsDynamin PH domainDominant negative inhibitorHigher-order oligomersDominant-negative inhibitionDynamin functionDomain bindsDynamin oligomersGTP bindingGTP hydrolysisGTPase activityPlasma membraneDynaminEndocytosisVesiclesPhosphoinositideBindsDomainMembrane
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