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
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, Protein
1997
Actin-binding membrane proteins identified by F-actin blot overlays.
Luna E, Pestonjamasp K, Cheney R, Strassel C, Lu T, Chia C, Hitt A, Fechheimer M, Furthmayr H, Mooseker M. Actin-binding membrane proteins identified by F-actin blot overlays. Society Of General Physiologists Series 1997, 52: 3-18. PMID: 9210216.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsActinsAmino Acid SequenceAnimalsBlotting, WesternBrainBreast NeoplasmsCattleChick EmbryoDictyosteliumElectrophoresis, Polyacrylamide GelHeLa CellsHumansIodine RadioisotopesMammalsMembrane ProteinsMiceMicrofilament ProteinsNeuroblastomaNeuropeptidesNeutrophilsSodium Dodecyl SulfateTumor Cells, CulturedConceptsBlot overlayApparent molecular massMembrane proteinsF-actinF-actin binding proteinMolecular massControl cell shapePeripheral membrane proteinsSpecialized membrane domainsCell-cell adhesionPlasma membrane-enriched fractionActin-binding proteinsMammalian cell linesCell surface extensionsMembrane-enriched fractionMembrane rufflesProtein 4.1Membrane domainsMammalian cellsDictyostelium discoideumSoil amoebaPseudopod dynamicsCell shapeEfficient chemotaxisMembrane bilayer
1995
Characterization of Myosin-IA and Myosin-IB, Two Unconventional Myosins Associated with theDrosophilaBrush Border Cytoskeleton
Morgan N, Heintzelman M, Mooseker M. Characterization of Myosin-IA and Myosin-IB, Two Unconventional Myosins Associated with theDrosophilaBrush Border Cytoskeleton. Developmental Biology 1995, 172: 51-71. PMID: 7589814, DOI: 10.1006/dbio.1995.0005.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell DifferentiationCloning, MolecularCytoskeletonDrosophila melanogasterElectrophoresis, Polyacrylamide GelEmbryo, NonmammalianFemaleGene Expression RegulationImmunoblottingImmunohistochemistryLarvaMicroscopy, ElectronMicroscopy, ImmunoelectronMicrovilliMyosinsOogenesisOvumPupaRecombinant ProteinsConceptsMyosin IBAdult gutATP-dependent extractionMyosin IASomatic follicle cellsExogenous F-actinBrush border cytoskeletonNovel unconventional myosinDrosophila melanogasterMicrovillus assemblyEgg chambersApical domainMicrovillar componentsMicrovillar domainApical microvillar domainBasolateral domainExpression patternsUnconventional myosinF-actinSubcellular distributionFollicle cellsFunctional myosinDifferentiated enterocytesBiochemical propertiesBrush border
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 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
1988
Characterization of ZO-1, a protein component of the tight junction from mouse liver and Madin-Darby canine kidney cells.
Anderson J, Stevenson B, Jesaitis L, Goodenough D, Mooseker M. Characterization of ZO-1, a protein component of the tight junction from mouse liver and Madin-Darby canine kidney cells. Journal Of Cell Biology 1988, 106: 1141-1149. PMID: 2452168, PMCID: PMC2115004, DOI: 10.1083/jcb.106.4.1141.Peer-Reviewed Original Research
1986
Reevaluation of the hydrophobic nature of the 110‐kD calmodulin‐, actin‐, and membrane‐binding protein of the intestinal microvillus
Conzelman K, Mooseker M. Reevaluation of the hydrophobic nature of the 110‐kD calmodulin‐, actin‐, and membrane‐binding protein of the intestinal microvillus. Journal Of Cellular Biochemistry 1986, 30: 271-279. PMID: 3700495, DOI: 10.1002/jcb.240300308.Peer-Reviewed Original Research
1980
Brush-border calmodulin. A major component of the isolated microvillus core.
Howe C, Mooseker M, Graves T. Brush-border calmodulin. A major component of the isolated microvillus core. Journal Of Cell Biology 1980, 85: 916-923. PMID: 6893051, PMCID: PMC2111444, DOI: 10.1083/jcb.85.3.916.Peer-Reviewed Original ResearchActinsAnimalsCalciumCalcium-Binding ProteinsCalmodulinCell MembraneChickensCytoskeletonElectrophoresis, Polyacrylamide GelMicrovilliProtein Binding
1976
Studies of muscle proteins in embryonic myocardial cells of cardiac lethal mutant mexican axolotls (Ambystoma mexicanum) by use of heavy meromyosin binding and sodium dodecyl sulfate polyacrylamide gel electrophoresis.
Lemanski L, Mooseker M, Peachey L, Iyengar M. Studies of muscle proteins in embryonic myocardial cells of cardiac lethal mutant mexican axolotls (Ambystoma mexicanum) by use of heavy meromyosin binding and sodium dodecyl sulfate polyacrylamide gel electrophoresis. Journal Of Cell Biology 1976, 68: 375-388. PMID: 1107335, PMCID: PMC2109630, DOI: 10.1083/jcb.68.2.375.Peer-Reviewed Original ResearchMeSH KeywordsActinsAmbystomaAnimalsCell DifferentiationElectrophoresis, Polyacrylamide GelGenes, RecessiveHeartMuscle ProteinsMutationMyocardiumMyosin SubfragmentsMyosinsTropomyosinConceptsMutant heartsRecessive mutant gene cMutant siblingsGene CHeart muscle differentiationMutant heart cellsHeavy meromyosin treatmentDalton bandMuscle proteinsGel electrophoresisSingle gene mutationsMutant embryonic heartsDifferent muscle proteinsEmbryonic myocardial cellsEarly developmental stagesSkeletal muscleSodium dodecyl sulfate gel electrophoresisDodecyl sulfate gel electrophoresisEmbryonic heart functionSodium dodecyl sulfate-polyacrylamide gel electrophoresisDodecyl sulfate-polyacrylamide gel electrophoresisSulfate-polyacrylamide gel electrophoresisHeavy meromyosin bindingMuscle differentiationMexican axolotl
1973
THE POLYMERIZATION OF ACTIN: ITS ROLE IN THE GENERATION OF THE ACROSOMAL PROCESS OF CERTAIN ECHINODERM SPERM
Tilney L, Hatano S, Ishikawa H, Mooseker M. THE POLYMERIZATION OF ACTIN: ITS ROLE IN THE GENERATION OF THE ACROSOMAL PROCESS OF CERTAIN ECHINODERM SPERM. Journal Of Cell Biology 1973, 59: 109-126. PMID: 4356568, PMCID: PMC2110911, DOI: 10.1083/jcb.59.1.109.Peer-Reviewed Original ResearchConceptsSperm actinAcrosomal processGel electrophoresisUnreacted spermSodium dodecyl sulfate gel electrophoresisDodecyl sulfate gel electrophoresisMuscle myosinMuscle F-actinPolymerization of actinHeavy meromyosin bindingSulfate gel electrophoresisEchinoderm spermF-actinSDS gel electrophoresisMonomeric stateDetergent Triton XSkeletal muscle myosinActinAcrosomal regionBundles of microfilamentsAcrosomal capMicrofilamentsSame molecular weightSperm extractsEgg jellyISOLATION AND REACTIVATION OF THE AXOSTYLE
Mooseker M, Tilney L. ISOLATION AND REACTIVATION OF THE AXOSTYLE. Journal Of Cell Biology 1973, 56: 13-26. PMID: 4345162, PMCID: PMC2108841, DOI: 10.1083/jcb.56.1.13.Peer-Reviewed Original Research