2013
Role of Myosin1a in regulated exocytosis of CFTR in villus enterocytes
Hoekstra N, Kravtsov D, Mooseker M, Ameen N. Role of Myosin1a in regulated exocytosis of CFTR in villus enterocytes. The FASEB Journal 2013, 27: 913.11-913.11. DOI: 10.1096/fasebj.27.1_supplement.913.11.Peer-Reviewed Original ResearchSurface biotinylationRegulated exocytosisCFTR trafficSurface CFTRSubapical endosomesBrush border membraneMembrane traffickingCFTR deliveryKD cellsKnockdown cellsCFTR channelsCFTR distributionVillus enterocytesMolecular mechanismsEnterocyte brush border membraneCFTRBiotinylationConfocal microscopyEndosomesIntestinal brush border membraneMouse intestineExocytosisCGMP agonistMyo1aBorder membrane
2012
Mo1821 Normalization of CFTR Brush Border Membrane Trafficking Defects in the Intestines of Myosin 1A/6 Double Mutant Mice
Hoekstra N, Mooseker M, Ameen N. Mo1821 Normalization of CFTR Brush Border Membrane Trafficking Defects in the Intestines of Myosin 1A/6 Double Mutant Mice. Gastroenterology 2012, 142: s-692-s-693. DOI: 10.1016/s0016-5085(12)62674-2.Peer-Reviewed Original Research
2008
Myo2p, a class V myosin in budding yeast, associates with a large ribonucleic acid–protein complex that contains mRNAs and subunits of the RNA-processing body
Chang W, Zaarour RF, Reck-Peterson S, Rinn J, Singer RH, Snyder M, Novick P, Mooseker MS. Myo2p, a class V myosin in budding yeast, associates with a large ribonucleic acid–protein complex that contains mRNAs and subunits of the RNA-processing body. RNA 2008, 14: 491-502. PMID: 18218704, PMCID: PMC2248268, DOI: 10.1261/rna.665008.Peer-Reviewed Original ResearchMeSH KeywordsActinsAdenosine TriphosphatasesBase SequenceDNA PrimersMacromolecular SubstancesMyosin Heavy ChainsMyosin Type VOligonucleotide Array Sequence AnalysisOrganellesPolyribosomesRibonucleoproteinsRNA Processing, Post-TranscriptionalRNA, FungalRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSecretory VesiclesVacuolesConceptsRNA processing bodiesClass V myosinsP-bodiesRelease of mRNAProcessing bodiesOrganelle traffickingSpindle orientationMotor mutantsMyo2-66Ribosomal subunitMyo2pProtein subunitsPartial colocalizationMicroarray analysisSubunitsSedimentation analysisYeastMRNAComplexesMyosinMutantsPolysomesTraffickingRNAColocalization
2007
Roles for Drosophila melanogaster Myosin IB in Maintenance of Enterocyte Brush-Border Structure and Resistance to the Bacterial Pathogen Pseudomonas entomophila
Hegan PS, Mermall V, Tilney LG, Mooseker MS. Roles for Drosophila melanogaster Myosin IB in Maintenance of Enterocyte Brush-Border Structure and Resistance to the Bacterial Pathogen Pseudomonas entomophila. Molecular Biology Of The Cell 2007, 18: 4625-4636. PMID: 17855510, PMCID: PMC2043548, DOI: 10.1091/mbc.e07-02-0191.Peer-Reviewed Original ResearchConceptsMutant larvaePseudomonas entomophilaTail domainMyosin IBMidgut epithelial cellsActin filament coreDrosophila genomeApical brush borderMidgut enterocytesBrush borderCytoskeletal defectsLarval gutResponse pathwaysApical localizationMV membraneBrush border structureDeletion mutationsFood uptakeGram-negative bacterial infectionsInnate immune responseMyo1bGut physiologyEntomophilaEpithelial cellsMidgutAssessment of myosin II, Va, VI and VIIa loss of function on endocytosis and endocytic vesicle motility in bone marrow‐derived dendritic cells
Holt JP, Bottomly K, Mooseker MS. Assessment of myosin II, Va, VI and VIIa loss of function on endocytosis and endocytic vesicle motility in bone marrow‐derived dendritic cells. Cytoskeleton 2007, 64: 756-766. PMID: 17615572, DOI: 10.1002/cm.20220.Peer-Reviewed Original ResearchConceptsDendritic cellsBone marrow-derived dendritic cellsMarrow-derived dendritic cellsShaker-1Immune surveillanceDendritic cell endocytosisCytometric analysisMouse linesBlebbistatin-treated cellsMyosin mutationsDextran uptakeVesicle movementEndosomal acidificationMyosin IIPhagocytosisWaltzerCell rateCellsFluorescent dextranMyosin II functionFluid-phase uptakeUptakeMyosin Va.Vesicle motilityMyosin familyMyosin 1E interacts with synaptojanin‐1 and dynamin and is involved in endocytosis
Krendel M, Osterweil EK, Mooseker MS. Myosin 1E interacts with synaptojanin‐1 and dynamin and is involved in endocytosis. FEBS Letters 2007, 581: 644-650. PMID: 17257598, PMCID: PMC1861834, DOI: 10.1016/j.febslet.2007.01.021.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAnimalsChlorocebus aethiopsClathrin-Coated VesiclesCOS CellsDynaminsEndocytosisHeLa CellsHumansImmunoprecipitationMiceMyosin Type INerve Tissue ProteinsPhosphoric Monoester HydrolasesProtein BindingProtein TransportRatsSrc Homology DomainsSynapsesTissue ExtractsTransferrinTwo-Hybrid System TechniquesConceptsSH3 domainMyosin 1eSynaptojanin 1Myosin IIntact SH3 domainDominant-negative mannerReceptor-mediated endocytosisHigher eukaryotesArp2/3 complexInhibits endocytosisPlasma membraneActin polymerizationImportant regulatorEndocytosisHuman class IProminent functionDynaminTail regionDomainEukaryotesClathrinYeastRegulatorProteinBindsThe Structural And Functional Diversity Of The Myosin Family Of Actin-Based Molecular Motors
Mooseker M, Foth B. The Structural And Functional Diversity Of The Myosin Family Of Actin-Based Molecular Motors. Proteins And Cell Regulation 2007, 7: 1-34. DOI: 10.1007/978-1-4020-6519-4_1.Peer-Reviewed Original Research
2006
Modulation of Cell Adhesion and Motility in the Immune System by Myo1f
Kim SV, Mehal WZ, Dong X, Heinrich V, Pypaert M, Mellman I, Dembo M, Mooseker MS, Wu D, Flavell RA. Modulation of Cell Adhesion and Motility in the Immune System by Myo1f. Science 2006, 314: 136-139. PMID: 17023661, DOI: 10.1126/science.1131920.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsCD18 AntigensCell AdhesionCell DegranulationCell MovementChemotaxis, LeukocyteColony Count, MicrobialCytoplasmic GranulesExocytosisImmunity, InnateLigandsListeria monocytogenesListeriosisMiceMice, KnockoutMyosin Type INeutrophil ActivationNeutrophilsN-Formylmethionine Leucyl-PhenylalanineThe Tail Domain of Myosin Va Modulates Actin Binding to One Head*
Olivares A, Chang W, Mooseker M, Hackney D, De La Cruz E. The Tail Domain of Myosin Va Modulates Actin Binding to One Head*. Journal Of Biological Chemistry 2006, 281: 31326-31336. DOI: 10.1016/s0021-9258(19)84045-0.Peer-Reviewed Original Research
2005
Cell Polarity Protein Spa2P Associates With Proteins Involved In Actin Function In Saccharomyces Cerevisiae
Shih J, Reck-Peterson S, Newitt R, Mooseker M, Aebersold R, Herskowitz I. Cell Polarity Protein Spa2P Associates With Proteins Involved In Actin Function In Saccharomyces Cerevisiae. Molecular Biology Of The Cell 2005, 16: 4595-4608. PMID: 16030260, PMCID: PMC1237067, DOI: 10.1091/mbc.e05-02-0108.Peer-Reviewed Original ResearchConceptsCell polarityPolarity proteinsActin functionCell wall morphogenesisCell polarity proteinsYeast cell polarityPresumptive bud siteCell separation defectATP-sensitive mannerTandem mass spectrometry analysisNonessential proteinsWall morphogenesisMolecular functionsBud sitePolarized localizationSpa2pMass spectrometry analysisSite of growthSaccharomyces cerevisiaeMyo2pCoimmunoprecipitation strategyCell cycleF-actinIndirect interactionsProteinMyosin-1a Is Critical for Normal Brush Border Structure and Composition
Tyska M, Mackey A, Huang J, Copeland N, Jenkins N, Mooseker M. Myosin-1a Is Critical for Normal Brush Border Structure and Composition. Molecular Biology Of The Cell 2005, 16: 2443-2457. PMID: 15758024, PMCID: PMC1087248, DOI: 10.1091/mbc.e04-12-1116.Peer-Reviewed Original ResearchConceptsMyosin-1aWhole animal phenotypesWhole animal levelIntermediate filament proteinsEctopic recruitmentFunctional redundancyAnimal phenotypesBrush borderMyosin 1cOvert phenotypeBrush border structureFilament proteinsMembrane componentsCellular levelVertebrate myosinsPhenotypeSigns of stressAnimal levelKnockout miceSignificant perturbationsEnterocytesMultifunctional componentsGenesDistinct changesProteinA role for myosin VI in postsynaptic structure and glutamate receptor endocytosis
Osterweil E, Wells D, Mooseker M. A role for myosin VI in postsynaptic structure and glutamate receptor endocytosis. Journal Of Cell Biology 2005, 168: 329-338. PMID: 15657400, PMCID: PMC2171578, DOI: 10.1083/jcb.200410091.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex 2Adaptor Proteins, Signal TransducingAdenosine TriphosphateAlpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic AcidAnimalsAstrocytesBrainBrain ChemistryDendritesDendritic SpinesDiscs Large Homolog 1 ProteinDyneinsEndocytosisFemaleGlial Fibrillary Acidic ProteinGuanylate KinasesInsulinMaleMembrane ProteinsMiceMice, Inbred C57BLMice, Mutant StrainsMicrofilament ProteinsMicroscopy, ElectronMyosin Heavy ChainsMyosin VIIaMyosinsNerve Tissue ProteinsNeuronsReceptors, AMPAReceptors, GlutamateSucroseSynapsesSynaptic MembranesSynaptosomesTransferrinConceptsHippocampal neuronsDendritic spinesIsoxazole propionic acid-type glutamate receptorsWild-type hippocampal neuronsShort dendritic spinesNumber of synapsesSynapse lossNeurons displaySynapse numberGlutamate receptorsNervous systemNonneuronal cellsPostsynaptic structuresSynaptic structurePostsynaptic densityDominant negative disruptionSignificant deficitsAstrogliosisNeuronsBrainMYO6SpineSynapsesReceptor endocytosisMyosin VI
2004
A role for myosin-1A in the localization of a brush border disaccharidase
Tyska M, Mooseker M. A role for myosin-1A in the localization of a brush border disaccharidase. Journal Of Cell Biology 2004, 165: 395-405. PMID: 15138292, PMCID: PMC2172191, DOI: 10.1083/jcb.200310031.Peer-Reviewed Original Research
2003
Myosin-Va Binds to and Mechanochemically Couples Microtubules to Actin Filaments
Cao T, Chang W, Masters S, Mooseker M. Myosin-Va Binds to and Mechanochemically Couples Microtubules to Actin Filaments. Molecular Biology Of The Cell 2003, 15: 151-161. PMID: 14565972, PMCID: PMC307536, DOI: 10.1091/mbc.e03-07-0504.Peer-Reviewed Original ResearchMyosin-V motility: these levers were made for walking
Tyska M, Mooseker M. Myosin-V motility: these levers were made for walking. Trends In Cell Biology 2003, 13: 447-451. PMID: 12946621, DOI: 10.1016/s0962-8924(03)00172-7.Peer-Reviewed Original ResearchNative Myosin-IXb is a plus-, not a minus-end-directed motor
O'Connell C, Mooseker M. Native Myosin-IXb is a plus-, not a minus-end-directed motor. Nature Cell Biology 2003, 5: 171-172. PMID: 12563277, DOI: 10.1038/ncb924.Peer-Reviewed Original Research
2002
MYO1A (Brush Border Myosin I) Dynamics in the Brush Border of LLC-PK1-CL4 Cells
Tyska M, Mooseker M. MYO1A (Brush Border Myosin I) Dynamics in the Brush Border of LLC-PK1-CL4 Cells. Biophysical Journal 2002, 82: 1869-1883. PMID: 11916846, PMCID: PMC1301984, DOI: 10.1016/s0006-3495(02)75537-9.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsBiophysical PhenomenaBiophysicsCloning, MolecularCytoskeletonElectrophoresis, Polyacrylamide GelGreen Fluorescent ProteinsHumansKidneyKineticsLLC-PK1 CellsLuminescent ProteinsMicroscopy, ConfocalMicroscopy, FluorescenceMicrovilliMyosin Type IPrecipitin TestsProtein Structure, TertiaryRecombinant Fusion ProteinsSubcellular FractionsSwineTime FactorsTransfectionConceptsTail domainLLC-PK1Actin core bundleKidney epithelial cell lineApical targetingActin dynamicsBrush borderActin turnoverGFP-actinBB populationsEpithelial cell lineActin domainsFluorescence recoveryCl4 cellsRapid turnoverApical surfaceMotor domainCore bundleATP depletionCell linesActinTurnoverCellsDomain
2001
The Abl-related gene (Arg) nonreceptor tyrosine kinase uses two F-actin-binding domains to bundle F-actin
Wang Y, Miller A, Mooseker M, Koleske A. The Abl-related gene (Arg) nonreceptor tyrosine kinase uses two F-actin-binding domains to bundle F-actin. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 14865-14870. PMID: 11752434, PMCID: PMC64950, DOI: 10.1073/pnas.251249298.Peer-Reviewed Original ResearchConceptsF-actin-binding domainActin-rich structuresAbl family kinasesNonreceptor tyrosine kinaseF-actinActin cytoskeletonFamily kinasesFluorescent protein fusion proteinTyrosine kinaseActin-bundling activityProtein fusion proteinActin cytoskeletal structuresCellular morphogenesisSwiss 3T3 fibroblastsBundling activityDeletion mutantsCytoskeletal structuresC-terminusFusion proteinFunctional interactionKinaseActin moleculesCytoskeletonPositive cooperativityArgMyosin-I nomenclature
Gillespie P, Albanesi J, Bähler M, Bement W, Berg J, Burgess D, Burnside B, Cheney R, Corey D, Coudrier E, de Lanerolle P, Hammer J, Hasson T, Holt J, Hudspeth AJ, Ikebe M, Kendrick-Jones J, Korn E, Li R, Mercer J, Milligan R, Mooseker M, Ostap E, Petit C, Pollard T, Sellers J, Soldati T, Titus M. Myosin-I nomenclature. Journal Of Cell Biology 2001, 155: 703-704. PMID: 11724811, PMCID: PMC2150864, DOI: 10.1083/jcb.200110032.Peer-Reviewed Original ResearchHigh Affinity Binding of Brain Myosin-Va to F-actin Induced by Calcium in the Presence of ATP*
Tauhata S, dos Santos D, Taylor E, Mooseker M, Larson R. High Affinity Binding of Brain Myosin-Va to F-actin Induced by Calcium in the Presence of ATP*. Journal Of Biological Chemistry 2001, 276: 39812-39818. PMID: 11517216, DOI: 10.1074/jbc.m102583200.Peer-Reviewed Original Research