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 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
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
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 ResearchMeSH Keywords3T3 CellsActinsAnimalsMiceMicroscopy, ElectronProtein BindingProtein-Tyrosine KinasesRecombinant Fusion ProteinsConceptsF-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 cooperativityArg
2000
The 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 studiesGenesExonsProteinGNB5
1999
An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin
Zhou D, Mooseker M, Galán J. An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 10176-10181. PMID: 10468582, PMCID: PMC17862, DOI: 10.1073/pnas.96.18.10176.Peer-Reviewed Original ResearchConceptsActin-bundling activityT-plastinBacterial-host cell contactHost cell signal transduction pathwaysHost cellsType III secretion systemBacterial effector proteinsActin-binding proteinsSignal transduction pathwaysBacterial effectorsMembrane rufflesEffector proteinsActin cytoskeletonMembrane rufflingSecretion systemSalmonella proteinsBacterial entryBacterial internalizationSalmonella entrySignaling processesActin filamentsF-actinNonphagocytic cellsProteinCell contact
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 ResearchAn in vitro model for the analysis of intestinal brush border assembly I. Ultrastructural analysis of cell contact-induced brush border assembly in Caco-2BBe cells
Peterson M, Mooseker M. An in vitro model for the analysis of intestinal brush border assembly I. Ultrastructural analysis of cell contact-induced brush border assembly in Caco-2BBe cells. Journal Of Cell Science 1993, 105: 445-460. PMID: 8408276, DOI: 10.1242/jcs.105.2.445.Peer-Reviewed Original Research
1990
Structural and compositional analysis of early stages in microvillus assembly in the enterocyte of the chick embryo
Heintzelman M, Mooseker M. Structural and compositional analysis of early stages in microvillus assembly in the enterocyte of the chick embryo. Differentiation 1990, 43: 175-182. PMID: 2387484, DOI: 10.1111/j.1432-0436.1990.tb00444.x.Peer-Reviewed Original ResearchAssembly 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
ZO-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 ResearchContributions of the β‐subunit to spectrin structure and function
Coleman T, Fishkind D, Mooseker M, Morrow J. Contributions of the β‐subunit to spectrin structure and function. Cytoskeleton 1989, 12: 248-263. PMID: 2524283, DOI: 10.1002/cm.970120406.Peer-Reviewed Original Research
1988
Tight junction structure and ZO-1 content are identical in two strains of Madin-Darby canine kidney cells which differ in transepithelial resistance.
Stevenson B, Anderson J, Goodenough D, Mooseker M. Tight junction structure and ZO-1 content are identical in two strains of Madin-Darby canine kidney cells which differ in transepithelial resistance. Journal Of Cell Biology 1988, 107: 2401-2408. PMID: 3058723, PMCID: PMC2115690, DOI: 10.1083/jcb.107.6.2401.Peer-Reviewed Original Research
1986
Cytoskeletal proteins of the rat kidney proximal tubule brush border.
Rodman J, Mooseker M, Farquhar M. Cytoskeletal proteins of the rat kidney proximal tubule brush border. European Journal Of Cell Biology 1986, 42: 319-27. PMID: 3545840.Peer-Reviewed Original ResearchConceptsProximal tubule cellsBrush borderIntestinal brush borderTubule cellsProximal tubule brush borderKidney proximal tubule cellsTubule brush borderRat kidney proximal tubule cellsTerminal web regionKidney brush borderTerminal webImmunogold labeling procedureKidneyCell typesImmunoelectron microscopyBasolateral membraneCytoskeletal componentsVillinCytoskeletal proteinsMicrovilli
1985
Effects of actin filament cross-linking and filament length on actin-myosin interaction.
Coleman T, Mooseker M. Effects of actin filament cross-linking and filament length on actin-myosin interaction. Journal Of Cell Biology 1985, 101: 1850-1857. PMID: 2932451, PMCID: PMC2113970, DOI: 10.1083/jcb.101.5.1850.Peer-Reviewed Original Research
1984
Brush border cytoskeleton and integration of cellular functions.
Mooseker M, Bonder E, Conzelman K, Fishkind D, Howe C, Keller T. Brush border cytoskeleton and integration of cellular functions. Journal Of Cell Biology 1984, 99: 104s-112s. PMID: 6378918, PMCID: PMC2275581, DOI: 10.1083/jcb.99.1.104s.Peer-Reviewed Original Research
1983
Direct measurement of critical concentrations and assembly rate constants at the two ends of an actin filament
Bonder E, Fishkind D, Mooseker M. Direct measurement of critical concentrations and assembly rate constants at the two ends of an actin filament. Cell 1983, 34: 491-501. PMID: 6684506, DOI: 10.1016/0092-8674(83)90382-3.Peer-Reviewed Original Research
1973
MICROTUBULES: EVIDENCE FOR 13 PROTOFILAMENTS
Tilney L, Bryan J, Bush D, Fujiwara K, Mooseker M, Murphy D, Snyder D. MICROTUBULES: EVIDENCE FOR 13 PROTOFILAMENTS. Journal Of Cell Biology 1973, 59: 267-275. PMID: 4805001, PMCID: PMC2109099, DOI: 10.1083/jcb.59.2.267.Peer-Reviewed Original Research