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
Assessment 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 family
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 interactionsProtein
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
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, 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 ResearchRole 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 siteCellsMyo2Sec5SPA2Class 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
1999
Myosin-V is a processive actin-based motor
Mehta A, Rock R, Rief M, Spudich J, Mooseker M, Cheney R. Myosin-V is a processive actin-based motor. Nature 1999, 400: 590-593. PMID: 10448864, DOI: 10.1038/23072.Peer-Reviewed Original ResearchThe 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
Vesicle-associated brain myosin-V can be activated to catalyze actin-based transport
Evans L, Lee A, Bridgman P, Mooseker M. Vesicle-associated brain myosin-V can be activated to catalyze actin-based transport. Journal Of Cell Science 1998, 111: 2055-2066. PMID: 9645952, DOI: 10.1242/jcs.111.14.2055.Peer-Reviewed Original ResearchConceptsMyosin VVesicle proteinsTotal vesicle proteinSynaptic vesicle proteinsInitial fractionation stepSynaptic vesicle marker proteinActin transportBrain myosin-VOrganelle transportActin filament motilityOrganelle motorFunctional analysisVesicle fractionFunction-blocking antibodiesLocalization studiesMarker proteinsImmunoelectron microscopyMotility assaysMotor domainProteinVesiclesFilament motilityVesicle integrityActinVesicle surfaceMolecular 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
1996
Function of Myosin-V in Filopodial Extension of Neuronal Growth Cones
Wang F, Wolenski J, Cheney R, Mooseker M, Jay D. Function of Myosin-V in Filopodial Extension of Neuronal Growth Cones. Science 1996, 273: 660-663. PMID: 8662560, DOI: 10.1126/science.273.5275.660.Peer-Reviewed Original Research