2009
A possible effector role for the pleckstrin homology (PH) domain of dynamin
Bethoney KA, King MC, Hinshaw JE, Ostap EM, Lemmon MA. A possible effector role for the pleckstrin homology (PH) domain of dynamin. Proceedings Of The National Academy Of Sciences Of The United States Of America 2009, 106: 13359-13364. PMID: 19666604, PMCID: PMC2720410, DOI: 10.1073/pnas.0906945106.Peer-Reviewed Original ResearchConceptsPleckstrin homology domainHomology domainPH domainAbility of dynaminLarge GTPase dynaminPH domain mutationsPhosphoinositide-containing membranesGTPase dynaminDynamin functionVesicle scissionMembrane scissionDynamin helixDynamin assemblyTargeting roleDynamin oligomersDynamin 1Possible effector roleAnimal cellsBisphosphate moleculesActin polymerizationDynaminClathrinDomain mutationsPhosphoinositideEndocytosis
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
2003
Loss of Phosphatidylinositol 3-Phosphate Binding by the C-terminal Tiam-1 Pleckstrin Homology Domain Prevents in Vivo Rac1 Activation without Affecting Membrane Targeting*
Baumeister MA, Martinu L, Rossman KL, Sondek J, Lemmon MA, Chou MM. Loss of Phosphatidylinositol 3-Phosphate Binding by the C-terminal Tiam-1 Pleckstrin Homology Domain Prevents in Vivo Rac1 Activation without Affecting Membrane Targeting*. Journal Of Biological Chemistry 2003, 278: 11457-11464. PMID: 12525493, DOI: 10.1074/jbc.m211901200.Peer-Reviewed Original Research
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