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 regionDomainEukaryotesClathrinYeastRegulatorProteinBinds
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-Phenylalanine
2005
Myosin-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 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 ResearchThe Yeast Class V Myosins, Myo2p and Myo4p, Are Nonprocessive Actin-Based Motors
Reck-Peterson S, Tyska M, Novick P, Mooseker M. The Yeast Class V Myosins, Myo2p and Myo4p, Are Nonprocessive Actin-Based Motors. Journal Of Cell Biology 2001, 153: 1121-1126. PMID: 11381095, PMCID: PMC2174330, DOI: 10.1083/jcb.153.5.1121.Peer-Reviewed Original ResearchActinsAdenosine TriphosphateAnimalsAntibodiesBrainCalciumCalmodulin-Binding ProteinsCarrier ProteinsChickensFungal ProteinsKineticsMicroscopy, VideoMolecular Motor ProteinsMovementMyosin Heavy ChainsMyosin Type IIMyosin Type VMyosinsNerve Tissue ProteinsProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsMyosin-VIIb, a Novel Unconventional Myosin, Is a Constituent of Microvilli in Transporting Epithelia
Chen Z, Hasson T, Zhang D, Schwender B, Derfler B, Mooseker M, Corey D. Myosin-VIIb, a Novel Unconventional Myosin, Is a Constituent of Microvilli in Transporting Epithelia. Genomics 2001, 72: 285-296. PMID: 11401444, DOI: 10.1006/geno.2000.6456.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsBase SequenceBiological TransportBlotting, NorthernBlotting, WesternChromosome MappingCloning, MolecularDNA, ComplementaryEpitheliumExonsFemaleGenesImmunohistochemistryIntestinesIntronsKidneyMiceMice, Inbred BALB CMicrovilliMolecular Sequence DataMyosinsPhylogenyProtein IsoformsRNA, MessengerSequence AlignmentSequence Analysis, DNASequence Homology, Amino AcidTissue Distribution
2000
The light chain composition of chicken brain myosin‐Va: Calmodulin, myosin‐II essential light chains, and 8‐kDa dynein light chain/PIN
Espindola F, Suter D, Partata L, Cao T, Wolenski J, Cheney R, King S, Mooseker M. The light chain composition of chicken brain myosin‐Va: Calmodulin, myosin‐II essential light chains, and 8‐kDa dynein light chain/PIN. Cytoskeleton 2000, 47: 269-281. PMID: 11093248, DOI: 10.1002/1097-0169(200012)47:4<269::aid-cm2>3.0.co;2-g.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsBrainCalmodulinCalpainCarrier ProteinsCells, CulturedChick EmbryoChickensDrosophila ProteinsDyneinsElectrophoresis, Polyacrylamide GelFlagellaGanglia, SpinalImmunoglobulin GIntermediate Filament ProteinsMiceMicroscopy, FluorescenceMolecular Sequence DataMyosin Heavy ChainsMyosin Light ChainsMyosin Type VMyosinsNeuronsProtein BindingProtein Structure, TertiarySequence Analysis, ProteinMyosin-V stepping kinetics: A molecular model for processivity
Rief M, Rock R, Mehta A, Mooseker M, Cheney R, Spudich J. Myosin-V stepping kinetics: A molecular model for processivity. Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 9482-9486. PMID: 10944217, PMCID: PMC16890, DOI: 10.1073/pnas.97.17.9482.Peer-Reviewed Original ResearchThe mouse neurological mutant flailer expresses a novel hybrid gene derived by exon shuffling between Gnb5 and Myo5a
Jones J, Huang J, Mermall V, Hamilton B, Mooseker M, Escayg A, Copeland N, Jenkins N, Meisler M. The mouse neurological mutant flailer expresses a novel hybrid gene derived by exon shuffling between Gnb5 and Myo5a. Human Molecular Genetics 2000, 9: 821-828. PMID: 10749990, DOI: 10.1093/hmg/9.5.821.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBrainDNA, ComplementaryExonsFungal ProteinsGene DosageGenes, RecessiveGTP-Binding Protein beta SubunitsIntronsMiceMice, Inbred C57BLMice, Mutant StrainsMicroscopy, ElectronMolecular Sequence DataMonomeric GTP-Binding ProteinsMyosin Type IMyosinsPurkinje CellsRNA, MessengerSaccharomyces cerevisiae ProteinsConceptsN-terminal 83 amino acidsAmino acidsWild-type proteinGlobular tail domainNon-homologous recombinationSmooth endoplasmic reticulum vesiclesNovel hybrid geneDominant-negative mechanismExon shufflingChromosomal arrangementsMammalian mutationsNew genesNovel genesUnrelated genesEndoplasmic reticulum vesiclesTail domainHybrid geneMutational mechanismsTerminal exonIntracellular transportGenetic studiesGenesExonsProteinGNB5Class V myosins
Reck-Peterson S, Provance D, Mooseker M, Mercer J. Class V myosins. Biochimica Et Biophysica Acta 2000, 1496: 36-51. PMID: 10722875, DOI: 10.1016/s0167-4889(00)00007-0.Peer-Reviewed Original ResearchLocalization of unconventional myosins V and VI in neuronal growth cones
Suter D, Espindola F, Lin C, Forscher P, Mooseker M. Localization of unconventional myosins V and VI in neuronal growth cones. Developmental Neurobiology 2000, 42: 370-382. PMID: 10645976, DOI: 10.1002/(sici)1097-4695(20000215)42:3<370::aid-neu8>3.0.co;2-v.Peer-Reviewed Original Research