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
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 ResearchMeSH KeywordsAnimalsColonDuodenumEnterocytesIleumMiceMice, KnockoutMicroscopy, ElectronMicroscopy, Electron, ScanningMicrovilliMyosin Heavy ChainsPhenotypeConceptsMyosin-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
2001
High 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 Proteins
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, ProteinRole of Actin and Myo2p in Polarized Secretion and Growth ofSaccharomyces cerevisiae
Karpova T, Reck-Peterson S, Elkind N, Mooseker M, Novick P, Cooper J. Role of Actin and Myo2p in Polarized Secretion and Growth ofSaccharomyces cerevisiae. Molecular Biology Of The Cell 2000, 11: 1727-1737. PMID: 10793147, PMCID: PMC14879, DOI: 10.1091/mbc.11.5.1727.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActinsBridged Bicyclo Compounds, HeterocyclicCarrier ProteinsCell DivisionCell PolarityFungal ProteinsGreen Fluorescent ProteinsLuminescent ProteinsMicroscopy, VideoMutationMyosin Heavy ChainsMyosin Type IIMyosin Type VRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsThiazolesThiazolidinesConceptsActin patch polarizationCell surface growthPolarized secretionFilamentous actinCortical actin patchesClass V myosin Myo2pRole of actinTime-lapse video microscopyIndividual living cellsActin patchesPolarized growthActin cytoskeletonActin cablesMyo2-66Tail domainMyo2pSevere defectsLiving cellsOfSaccharomyces cerevisiaeMotor domainLatrunculinActinOverall growthVideo microscopyQuantitative assayCompartmentalization of the Cell Cortex by Septins Is Required for Maintenance of Cell Polarity in Yeast
Barral Y, Mermall V, Mooseker M, Snyder M. Compartmentalization of the Cell Cortex by Septins Is Required for Maintenance of Cell Polarity in Yeast. Molecular Cell 2000, 5: 841-851. PMID: 10882120, DOI: 10.1016/s1097-2765(00)80324-x.Peer-Reviewed Original ResearchMeSH KeywordsActinsCarrier ProteinsCell CompartmentationCell Cycle ProteinsCell DivisionCell MembraneCell PolarityCytoplasmCytoskeletal ProteinsExocytosisFungal ProteinsMorphogenesisMyosin Heavy ChainsMyosin Type IIMyosin Type VProtein-Tyrosine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsConceptsCell polaritySpecialized plasma membrane domainsIsotropic bud growthPlasma membrane domainsBud neckMembrane domainsMother cellsCell cortexCell peripheryGrowth polaritySeptinsProper regulationBud surfaceBiological processesBud growthCell polarizationIsotropic growthCortical domainsExocytosisPatch stabilityActive siteCellsMyo2Sec5SPA2Localization 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
1999
The Tail of a Yeast Class V Myosin, Myo2p, Functions as a Localization Domain
Reck-Peterson S, Novick P, Mooseker M. The Tail of a Yeast Class V Myosin, Myo2p, Functions as a Localization Domain. Molecular Biology Of The Cell 1999, 10: 1001-1017. PMID: 10198053, PMCID: PMC25227, DOI: 10.1091/mbc.10.4.1001.Peer-Reviewed Original ResearchActinsCarrier ProteinsCell FractionationCell PolarityFungal ProteinsKineticsMutagenesis, Site-DirectedMyosin Heavy ChainsMyosin Type IIMyosin Type VMyosinsPhenotypePolymerase Chain ReactionRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsSubcellular Fractions
1998
Human brush border myosin‐I and myosin‐Ic expression in human intestine and Caco‐2BBe cells
Skowron J, Bement W, Mooseker M. Human brush border myosin‐I and myosin‐Ic expression in human intestine and Caco‐2BBe cells. Cytoskeleton 1998, 41: 308-324. PMID: 9858156, DOI: 10.1002/(sici)1097-0169(1998)41:4<308::aid-cm4>3.0.co;2-j.Peer-Reviewed Original ResearchMolecular Genetic Dissection of Mouse Unconventional Myosin-VA: Head Region Mutations
Huang J, Cope M, Mermall V, Strobel M, Kendrick-Jones J, Russell L, Mooseker M, Copeland N, Jenkins N. Molecular Genetic Dissection of Mouse Unconventional Myosin-VA: Head Region Mutations. Genetics 1998, 148: 1951-1961. PMID: 9560408, PMCID: PMC1460099, DOI: 10.1093/genetics/148.4.1951.Peer-Reviewed Original ResearchMolecular Genetic Dissection of Mouse Unconventional Myosin-VA: Tail Region Mutations
Huang J, Mermall V, Strobel M, Russell L, Mooseker M, Copeland N, Jenkins N. Molecular Genetic Dissection of Mouse Unconventional Myosin-VA: Tail Region Mutations. Genetics 1998, 148: 1963-1972. PMID: 9560409, PMCID: PMC1460104, DOI: 10.1093/genetics/148.4.1963.Peer-Reviewed Original ResearchConceptsMyosin VaMolecular genetic dissectionMammalian myosinGenetic dissectionProper foldingTail mutationsAlternative splicingColor locusDilute allelesSequencing approachSpecific functionsMutationsTail functionRegion mutationsFirst extensive collectionRT-PCRExtensive collectionSplicingLociTailFoldingIsoformsAllelesCargoSequence
1997
Unconventional Myosins in Inner-Ear Sensory Epithelia
Hasson T, Gillespie P, Garcia J, MacDonald R, Zhao Y, Yee A, Mooseker M, Corey D. Unconventional Myosins in Inner-Ear Sensory Epithelia. Journal Of Cell Biology 1997, 137: 1287-1307. PMID: 9182663, PMCID: PMC2132524, DOI: 10.1083/jcb.137.6.1287.Peer-Reviewed Original ResearchEffects of shaker‐1 mutations on myosin‐VIIa protein and mRNA expression
Hasson T, Walsh J, Cable J, Mooseker M, Brown S, Steel K. Effects of shaker‐1 mutations on myosin‐VIIa protein and mRNA expression. Cytoskeleton 1997, 37: 127-138. PMID: 9186010, DOI: 10.1002/(sici)1097-0169(1997)37:2<127::aid-cm5>3.0.co;2-5.Peer-Reviewed Original ResearchConceptsShaker-1 mutationsWild-type levelsNorthern blot analysisMammalian diseasesActin cytoskeletonMyosin VIIaShaker-1 miceGene expressionUnconventional myosinMRNA expressionProteinMyosin-VIIa mutationsImmunoblot analysisMotor domainRange of expressionMutationsBlot analysisAllelesProtein expressionTissue functionExpressionLife spanSH1Inner earLight microscopic level
1996
Human myosin-IXb, an unconventional myosin with a chimerin-like rho/rac GTPase-activating protein domain in its tail
Wirth J, Jensen K, Post P, Bement W, Mooseker M. Human myosin-IXb, an unconventional myosin with a chimerin-like rho/rac GTPase-activating protein domain in its tail. Journal Of Cell Science 1996, 109: 653-661. PMID: 8907710, DOI: 10.1242/jcs.109.3.653.Peer-Reviewed Original ResearchConceptsProtein domainsHL-60 cellsRho/Rac familyNovel N-terminal domainGTPase-activating protein (GAP) domainUnconventional myosin heavy chainRas-like G proteinsPrimary structurePutative actin-binding siteAmino acidsFull-length primary structureSkeletal muscle myosin IIN-terminal domainAmino acid extensionActin-binding siteProtein kinase CNorthern blot analysisMuscle myosin IIRac familyDifferent human tissuesUndifferentiated HL-60 cellsRegulatory domainPutative zincRac GTPaseCell periphery