2005
A 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
2001
Myosin-VIIb, a Novel Unconventional Myosin, Is a Constituent of Microvilli in Transporting Epithelia
Chen Z, Hasson T, Zhang D, Schwender B, Derfler B, Mooseker M, Corey D. Myosin-VIIb, a Novel Unconventional Myosin, Is a Constituent of Microvilli in Transporting Epithelia. Genomics 2001, 72: 285-296. PMID: 11401444, DOI: 10.1006/geno.2000.6456.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsBase SequenceBiological TransportBlotting, NorthernBlotting, WesternChromosome MappingCloning, MolecularDNA, ComplementaryEpitheliumExonsFemaleGenesImmunohistochemistryIntestinesIntronsKidneyMiceMice, Inbred BALB CMicrovilliMolecular Sequence DataMyosinsPhylogenyProtein IsoformsRNA, MessengerSequence AlignmentSequence Analysis, DNASequence Homology, Amino AcidTissue Distribution
1998
Molecular 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
Myosin VIIA mutation screening in 189 Usher syndrome type 1 patients.
Weston M, Kelley P, Overbeck L, Wagenaar M, Orten D, Hasson T, Chen Z, Corey D, Mooseker M, Sumegi J, Cremers C, Moller C, Jacobson S, Gorin M, Kimberling W. Myosin VIIA mutation screening in 189 Usher syndrome type 1 patients. American Journal Of Human Genetics 1996, 59: 1074-83. PMID: 8900236, PMCID: PMC1914835.Peer-Reviewed Original ResearchConceptsCongenital profound hearing lossMyosin-VIIa mutationsType 1 patientsProfound hearing lossUsher syndrome type 1BUnique mutationsPresence of mutationsAutosomal recessive disorderVestibular abnormalitiesMyosin VIIA geneHearing lossRetinitis pigmentosaPatientsType 1bI casesRecessive disorderSingle caseCompound heterozygotesPremature stop codonSimple heterozygotesGreater percentageUnrelated control samplesDisordersMutant allelesCurrent studyMapping of Unconventional Myosins in Mouse and Human
Hasson T, Skowron J, Gilbert D, Avraham K, Perry W, Bement W, Anderson B, Sherr E, Chen Z, Greene L, Ward D, Corey D, Mooseker M, Copeland N, Jenkins N. Mapping of Unconventional Myosins in Mouse and Human. Genomics 1996, 36: 431-439. PMID: 8884266, DOI: 10.1006/geno.1996.0488.Peer-Reviewed Original Research
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
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 characteristicsForebrain
1988
Localization of villin, a cytoskeletal protein specific to microvilli, in human ileum and colon and in colonic neoplasms
West A, Isaac C, Carboni J, Morrow J, Mooseker M, Barwick K. Localization of villin, a cytoskeletal protein specific to microvilli, in human ileum and colon and in colonic neoplasms. Gastroenterology 1988, 94: 343-352. PMID: 3335311, DOI: 10.1016/0016-5085(88)90421-0.Peer-Reviewed Original Research