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 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 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 ResearchCloning and characterization of mouse brush border myosin‐I in adult and embryonic intestine
Skowron J, Mooseker M. Cloning and characterization of mouse brush border myosin‐I in adult and embryonic intestine. Journal Of Experimental Zoology 1999, 283: 242-257. PMID: 9933937, DOI: 10.1002/(sici)1097-010x(19990215)283:3<242::aid-jez3>3.0.co;2-f.Peer-Reviewed Original ResearchConceptsBrush border myosinMicrovillar actin bundlesEmbryonic intestineSubcellular localization profileBasolateral membrane domainsGenomic clonesCalmodulin light chainsVertebrate speciesMembrane domainsActin corePlasma membraneKnockout strategiesActin bundlesImmunolocalization studiesIntestinal epithelial cellsGolgi apparatusNorthern analysisPrimary structureNorthern blotSitu localizationLocalization profilesRNA expressionEmbryosDirect targetingEmbryogenesis
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 surface
1996
Enzymatic Characterization and Functional Domain Mapping of Brain Myosin-V*
Nascimento A, Cheney R, Tauhata S, Larson R, Mooseker M. Enzymatic Characterization and Functional Domain Mapping of Brain Myosin-V*. Journal Of Biological Chemistry 1996, 271: 17561-17569. PMID: 8663447, DOI: 10.1074/jbc.271.29.17561.Peer-Reviewed Original Research
1994
Multiple unconventional myosin domains of the intestinal brush border cytoskeleton
Heintzelman M, Hasson T, Mooseker M. Multiple unconventional myosin domains of the intestinal brush border cytoskeleton. Journal Of Cell Science 1994, 107: 3535-3543. PMID: 7706404, DOI: 10.1242/jcs.107.12.3535.Peer-Reviewed Original Research
1993
Brain myosin-V is a two-headed unconventional myosin with motor activity
Cheney R, O'Shea M, Heuser J, Coelho M, Wolenski J, Espreafico E, Forscher P, Larson R, Mooseker M. Brain myosin-V is a two-headed unconventional myosin with motor activity. Cell 1993, 75: 13-23. PMID: 8402892, DOI: 10.1016/s0092-8674(05)80080-7.Peer-Reviewed Original ResearchIn vitro motilities of the unconventional myosins, brush border myosin‐I, and chick brain myosin‐V exhibit assay‐dependent differences in velocity
Wolenski J, Cheney R, Forscher P, Mooseker M. In vitro motilities of the unconventional myosins, brush border myosin‐I, and chick brain myosin‐V exhibit assay‐dependent differences in velocity. Journal Of Experimental Zoology 1993, 267: 33-39. PMID: 8376949, DOI: 10.1002/jez.1402670106.Peer-Reviewed Original ResearchCalcium-calmodulin and regulation of brush border myosin-I MgATPase and mechanochemistry
Wolenski J, Hayden S, Forscher P, Mooseker. Calcium-calmodulin and regulation of brush border myosin-I MgATPase and mechanochemistry. Journal Of Cell Biology 1993, 122: 613-621. PMID: 8335688, PMCID: PMC2119657, DOI: 10.1083/jcb.122.3.613.Peer-Reviewed Original Research
1992
Biochemical and immunological characterization of p190-calmodulin complex from vertebrate brain: a novel calmodulin-binding myosin.
Espindola F, Espreafico E, Coelho M, Martins A, Costa F, Mooseker M, Larson R. Biochemical and immunological characterization of p190-calmodulin complex from vertebrate brain: a novel calmodulin-binding myosin. Journal Of Cell Biology 1992, 118: 359-368. PMID: 1378447, PMCID: PMC2290054, DOI: 10.1083/jcb.118.2.359.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAnimalsAnimals, NewbornBrainCalmodulinCalmodulin-Binding ProteinsChickensCytoskeletal ProteinsElectrophoresis, Polyacrylamide GelEmbryonic and Fetal DevelopmentEpitopesFemaleImmunohistochemistryMaleMolecular WeightMyosinsNerve Tissue ProteinsOrgan SpecificityPurkinje CellsRabbitsRatsSpecies SpecificityConceptsCalmodulin-dependent kinase IIAdult forebrainMammalian brainPurkinje cellsImmunocytochemical studyDendritic extensionsRat tissuesImmunological characterizationImmunological evidencePost coitusImmunological recognitionCerebellumPolyclonal antibodiesBrainVertebrate brainMAbsEpitopesMg-ATPase activityKinase IIP190Brush border myosin IAction activationCa2Activity characteristicsForebrainLocalization of capping protein in chicken epithelial cells by immunofluorescence and biochemical fractionation.
Schafer D, Mooseker M, Cooper J. Localization of capping protein in chicken epithelial cells by immunofluorescence and biochemical fractionation. Journal Of Cell Biology 1992, 118: 335-346. PMID: 1629237, PMCID: PMC2290044, DOI: 10.1083/jcb.118.2.335.Peer-Reviewed Original ResearchMeSH KeywordsActin Depolymerizing FactorsActinsAnimalsAntibodiesCells, CulturedChick EmbryoChickensCochleaDestrinElectrophoresis, Polyacrylamide GelEpithelial CellsEpitheliumFluorescent Antibody TechniqueIntestinesKidneyMacromolecular SubstancesMicrofilament ProteinsMicrovilliMusclesPigment Epithelium of EyeSubcellular FractionsConceptsIntestinal epithelial cellsNuclei of cellsBiochemical fractionationJunctional complexesActin filamentsCell-cell junctional complexesSingle intestinal epithelial cellsBarbed endsEpithelial cellsSensory epitheliumCell-cell contactIntact intestinal epithelial cellsAffinity-purified polyclonal antibodiesProtein bindsCapping proteinIntestinal epitheliumZonula adherensCell junctionsChick embryo kidney cellsPattern coincidentEmbryo kidney cellsProteinConfocal microscopyKidney cellsIsolated intestinal epithelial cells
1990
Binding of brush border myosin I to phospholipid vesicles.
Hayden S, Wolenski J, Mooseker M. Binding of brush border myosin I to phospholipid vesicles. Journal Of Cell Biology 1990, 111: 443-451. PMID: 2143194, PMCID: PMC2116197, DOI: 10.1083/jcb.111.2.443.Peer-Reviewed Original ResearchConceptsBB myosin IMyosin IBrush border myosin IMyosin I heavy chainMembrane-binding domainActin filament corePhospholipid vesiclesATP-sensitive mannerPlasma membraneIntestinal epithelial cellsF-actinMembrane interactionsPhosphatidylglycerol vesiclesFree proteinCOOH-terminalAnionic phospholipidsImmunoblot analysisVesiclesEpithelial cellsImmunoblot stainingM. SimilarHeavy chainActinStructural informationNeutral phospholipidsAssembly of the brush border cytoskeleton: Changes in the distribution of microvillar core proteins during enterocyte differentiation in adult chicken intestine
Heintzelman M, Mooseker M. Assembly of the brush border cytoskeleton: Changes in the distribution of microvillar core proteins during enterocyte differentiation in adult chicken intestine. Cytoskeleton 1990, 15: 12-22. PMID: 2403846, DOI: 10.1002/cm.970150104.Peer-Reviewed Original Research
1989
Partial deduced sequence of the 110-kD-calmodulin complex of the avian intestinal microvillus shows that this mechanoenzyme is a member of the myosin I family.
Garcia A, Coudrier E, Carboni J, Anderson J, Vandekerkhove J, Mooseker M, Louvard D, Arpin M. Partial deduced sequence of the 110-kD-calmodulin complex of the avian intestinal microvillus shows that this mechanoenzyme is a member of the myosin I family. Journal Of Cell Biology 1989, 109: 2895-2903. PMID: 2687288, PMCID: PMC2115973, DOI: 10.1083/jcb.109.6.2895.Peer-Reviewed Original ResearchZO-1 and cingulin: tight junction proteins with distinct identities and localizations
Stevenson B, Heintzelman M, Anderson J, Citi S, Mooseker M. ZO-1 and cingulin: tight junction proteins with distinct identities and localizations. American Journal Of Physiology 1989, 257: c621-c628. PMID: 2679124, DOI: 10.1152/ajpcell.1989.257.4.c621.Peer-Reviewed Original ResearchConceptsCell-cell contactPlasma membraneHepatoma tissue cultureZO-1MDCK cellsMadin-Darby canine kidney cellsCanine kidney cellsSubconfluent MDCK cellsSingle polypeptideCingulinHepatoma cell lineMolecular massChicken small intestineDistinct localizationImmunoblot analysisJunctional membranesImmunofluorescent localizationCell linesKidney cellsJunction proteinsKidney distalTight junctionsChicken intestineConfluent monolayersProteinCharacterization of intestinal microvillar membrane disks: detergent-resistant membrane sheets enriched in associated brush border myosin I (110K-calmodulin).
Mooseker M, Conzelman K, Coleman T, Heuser J, Sheetz M. Characterization of intestinal microvillar membrane disks: detergent-resistant membrane sheets enriched in associated brush border myosin I (110K-calmodulin). Journal Of Cell Biology 1989, 109: 1153-1161. PMID: 2527857, PMCID: PMC2115773, DOI: 10.1083/jcb.109.3.1153.Peer-Reviewed Original Research