2021
Phosphatidylserine binding directly regulates TIM-3 function
Smith CM, Li A, Krishnamurthy N, Lemmon MA. Phosphatidylserine binding directly regulates TIM-3 function. Biochemical Journal 2021, 478: 3331-3349. PMID: 34435619, PMCID: PMC8454703, DOI: 10.1042/bcj20210425.Peer-Reviewed Original ResearchConceptsTim-3T cell receptorTherapeutic targetCo-signaling receptorsTim-3 functionTim-3 ligandTim-3 signalingCo-inhibitory receptorsCo-stimulatory receptorsImmune modulation approachesIL-2 secretionPotential therapeutic targetNF-κB signalingImportant therapeutic targetPD-1Jurkat cellsCultured Jurkat cellsT cellsCell receptorTCR stimulationReceptorsImportance of phosphatidylserineDifferent studiesCellsSignaling
2006
Palmitoylation of the EGFR Ligand Spitz by Rasp Increases Spitz Activity by Restricting Its Diffusion
Miura GI, Buglino J, Alvarado D, Lemmon MA, Resh MD, Treisman JE. Palmitoylation of the EGFR Ligand Spitz by Rasp Increases Spitz Activity by Restricting Its Diffusion. Developmental Cell 2006, 10: 167-176. PMID: 16459296, DOI: 10.1016/j.devcel.2005.11.017.Peer-Reviewed Original ResearchMeSH KeywordsAcyltransferasesAnimalsBase SequenceBiological Transport, ActiveCell LineCell MembraneCysteineDNADrosophilaDrosophila ProteinsEpidermal Growth FactorErbB ReceptorsFemaleGenes, InsectIn Vitro TechniquesLigandsMaleMembrane ProteinsModels, BiologicalMutagenesis, Site-DirectedMutationOvaryPalmitic AcidRecombinant ProteinsTransfectionWings, AnimalConceptsEpidermal growth factor receptorDrosophila epidermal growth factor receptorEGFR ligand SpitzPlasma membrane associationN-terminal cysteine residueLigand SpitzMembrane associationWnt familyDevelopmental functionsGrowth factor receptorCysteine residuesBiological functionsLipid modificationPalmitoylationIntracellular proteinsCultured cellsCell membraneFactor receptorSpitzReduced activityVivoTransmembraneHedgehogProteinActivity
2004
Inhibition of nuclear import and cell-cycle progression by mutated forms of the dynamin-like GTPase MxB
King MC, Raposo G, Lemmon MA. Inhibition of nuclear import and cell-cycle progression by mutated forms of the dynamin-like GTPase MxB. Proceedings Of The National Academy Of Sciences Of The United States Of America 2004, 101: 8957-8962. PMID: 15184662, PMCID: PMC428454, DOI: 10.1073/pnas.0403167101.Peer-Reviewed Original ResearchMeSH KeywordsActive Transport, Cell NucleusAmino Acid SubstitutionCell CycleCell NucleusCytoplasmGene ExpressionGTP-Binding ProteinsGuanosine TriphosphateHeLa CellsHumansInterferon-alphaMicroscopy, FluorescenceMicroscopy, ImmunoelectronMyxovirus Resistance ProteinsNuclear PoreNuclear Pore Complex ProteinsRecombinant Fusion ProteinsRNA InterferenceTransfectionConceptsNuclear importCell cycle progressionRNA interferenceDynamin-like proteinCell cycle defectsDynamin-like GTPasesNormal cellular functionNucleocytoplasmic traffickingCellular functionsNuclear poresCytoplasmic faceMx proteinCellular traffickingUnexpected roleMxBType I IFNTraffickingProteinI IFNImportAntiviral activityGTPasesMutantsSubfamiliesRole
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