2007
Myosin 1E interacts with synaptojanin‐1 and dynamin and is involved in endocytosis
Krendel M, Osterweil EK, Mooseker MS. Myosin 1E interacts with synaptojanin‐1 and dynamin and is involved in endocytosis. FEBS Letters 2007, 581: 644-650. PMID: 17257598, PMCID: PMC1861834, DOI: 10.1016/j.febslet.2007.01.021.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAnimalsChlorocebus aethiopsClathrin-Coated VesiclesCOS CellsDynaminsEndocytosisHeLa CellsHumansImmunoprecipitationMiceMyosin Type INerve Tissue ProteinsPhosphoric Monoester HydrolasesProtein BindingProtein TransportRatsSrc Homology DomainsSynapsesTissue ExtractsTransferrinTwo-Hybrid System TechniquesConceptsSH3 domainMyosin 1eSynaptojanin 1Myosin IIntact SH3 domainDominant-negative mannerReceptor-mediated endocytosisHigher eukaryotesArp2/3 complexInhibits endocytosisPlasma membraneActin polymerizationImportant regulatorEndocytosisHuman class IProminent functionDynaminTail regionDomainEukaryotesClathrinYeastRegulatorProteinBinds
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
1999
Cloning 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
Human myosin-IXb is a mechanochemically active motor and a GAP for rho
Post P, Bokoch G, Mooseker M. Human myosin-IXb is a mechanochemically active motor and a GAP for rho. Journal Of Cell Science 1998, 111: 941-950. PMID: 9490638, DOI: 10.1242/jcs.111.7.941.Peer-Reviewed Original ResearchActinsAdenosine TriphosphateAlternative SplicingAmino Acid SequenceAnimalsCalciumCalmodulinGTP PhosphohydrolasesGTPase-Activating ProteinsGTP-Binding ProteinsHumansLeukocytesMolecular Sequence DataMuscle ContractionMyosinsProtein BindingProteinsRas GTPase-Activating ProteinsRas ProteinsRatsRho GTP-Binding Proteins
1997
An actin-related protein in Drosophila colocalizes with heterochromatin protein 1 in pericentric heterochromatin
Frankel S, Sigel E, Craig C, Elgin S, Mooseker M, Artavanis-Tsakonas S. An actin-related protein in Drosophila colocalizes with heterochromatin protein 1 in pericentric heterochromatin. Journal Of Cell Science 1997, 110: 1999-2012. PMID: 9378752, DOI: 10.1242/jcs.110.17.1999.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsAntibodiesBacterial ProteinsCarrier ProteinsCell NucleusChromatinChromobox Protein Homolog 5Chromosomal Proteins, Non-HistoneChromosomesDrosophila melanogasterEmbryo, NonmammalianEuchromatinGene Expression Regulation, DevelopmentalGenes, InsectHeterochromatinMutagenesisNuclear ProteinsRatsConceptsHeterochromatin protein 1Actin-related proteinsPolytene chromosome spreadsLocalization patternsCentric heterochromatinChromosome spreadsEuchromatic bandsProtein 1Heterochromatin-mediated geneNuclear localization patternPericentric heterochromatinHeterochromatin functionChromatin structureNuclear functionsFunctional diversitySequence similarityPolytene nucleiArp4Larval tissuesPrepupal developmentGenetic evidenceMutant formsGenetic dataHeterochromatinCell cycle
1995
Expression in cochlea and retina of myosin VIIa, the gene product defective in Usher syndrome type 1B.
Hasson T, Heintzelman M, Santos-Sacchi J, Corey D, Mooseker M. Expression in cochlea and retina of myosin VIIa, the gene product defective in Usher syndrome type 1B. Proceedings Of The National Academy Of Sciences Of The United States Of America 1995, 92: 9815-9819. PMID: 7568224, PMCID: PMC40893, DOI: 10.1073/pnas.92.21.9815.Peer-Reviewed Original ResearchMeSH KeywordsAbnormalities, MultipleAmino Acid SequenceAnimalsAntibody SpecificityBlindnessCochleaDeafnessDyneinsFluorescent Antibody TechniqueGuinea PigsHearing Loss, SensorineuralHumansImmunoblottingMolecular Sequence DataMyosin VIIaMyosinsRatsRetinaRetinitis PigmentosaSequence Homology, Amino AcidSwineSyndromeTissue DistributionConceptsHair cellsMyosin VIIa expressionEpithelial cellsMyosin VIIaCochlear hair cellsMyosin VIIa functionOuter hair cellsUsher syndrome type 1BMyosin VIIA geneVestibular dysfunctionCell-specific localizationCongenital deafnessRetinitis pigmentosaUsher syndromeType 1bType 1B.Normal functionApical stereociliaVIIaDeafnessDisease phenotypeCochleaInherited diseaseRetinaShaker-1
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 characteristicsForebrain6 Assembly of the Intestinal Brush Border Cytoskeleton
Heintzelman M, Mooseker M. 6 Assembly of the Intestinal Brush Border Cytoskeleton. Current Topics In Developmental Biology 1992, 26: 93-122. PMID: 1563281, DOI: 10.1016/s0070-2153(08)60442-1.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 monolayersProteinZO-1 mRNA and protein expression during tight junction assembly in Caco-2 cells.
Anderson J, Van Itallie C, Peterson M, Stevenson B, Carew E, Mooseker M. ZO-1 mRNA and protein expression during tight junction assembly in Caco-2 cells. Journal Of Cell Biology 1989, 109: 1047-1056. PMID: 2670954, PMCID: PMC2115763, DOI: 10.1083/jcb.109.3.1047.Peer-Reviewed Original ResearchHepatic immunohistochemical localization of the tight junction protein ZO-1 in rat models of cholestasis.
Anderson J, Glade J, Stevenson B, Boyer J, Mooseker M. Hepatic immunohistochemical localization of the tight junction protein ZO-1 in rat models of cholestasis. American Journal Of Pathology 1989, 134: 1055-62. PMID: 2719075, PMCID: PMC1879891.Peer-Reviewed Original ResearchConceptsZO-1 proteinZO-1Tight junctionsConsecutive daily subcutaneous injectionsFrozen sectionsReflux of bileDaily subcutaneous injectionsBile duct obstructionCommon bile ductMale Sprague-DawleyHepatocyte tight junctionsBile duct ligation resultsTight junction protein ZO-1Cholestatic modelsDuct obstructionBile ductSubcutaneous injectionCholestatic liverRat modelEthinyl estradiolSprague-DawleyProtein ZO-1Immunoperoxidase stainingZO-1 stainingImmunohistochemical localization
1988
Characterization of villin from the intestinal brush border of the rat, and comparative analysis with avian villin
Alicea H, Mooseker M. Characterization of villin from the intestinal brush border of the rat, and comparative analysis with avian villin. Cytoskeleton 1988, 9: 60-72. PMID: 3356045, DOI: 10.1002/cm.970090107.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 proteinsMicrovilliIdentification of ZO-1: a high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia.
Stevenson B, Siliciano J, Mooseker M, Goodenough D. Identification of ZO-1: a high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia. Journal Of Cell Biology 1986, 103: 755-766. PMID: 3528172, PMCID: PMC2114282, DOI: 10.1083/jcb.103.3.755.Peer-Reviewed Original Research
1976
Brush border motility. Microvillar contraction in triton-treated brush borders isolated from intestinal epithelium.
Mooseker M. Brush border motility. Microvillar contraction in triton-treated brush borders isolated from intestinal epithelium. Journal Of Cell Biology 1976, 71: 417-433. PMID: 11222, PMCID: PMC2109748, DOI: 10.1083/jcb.71.2.417.Peer-Reviewed Original Research