2008
Myo2p, a class V myosin in budding yeast, associates with a large ribonucleic acid–protein complex that contains mRNAs and subunits of the RNA-processing body
Chang W, Zaarour RF, Reck-Peterson S, Rinn J, Singer RH, Snyder M, Novick P, Mooseker MS. Myo2p, a class V myosin in budding yeast, associates with a large ribonucleic acid–protein complex that contains mRNAs and subunits of the RNA-processing body. RNA 2008, 14: 491-502. PMID: 18218704, PMCID: PMC2248268, DOI: 10.1261/rna.665008.Peer-Reviewed Original ResearchMeSH KeywordsActinsAdenosine TriphosphatasesBase SequenceDNA PrimersMacromolecular SubstancesMyosin Heavy ChainsMyosin Type VOligonucleotide Array Sequence AnalysisOrganellesPolyribosomesRibonucleoproteinsRNA Processing, Post-TranscriptionalRNA, FungalRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSecretory VesiclesVacuolesConceptsRNA processing bodiesClass V myosinsP-bodiesRelease of mRNAProcessing bodiesOrganelle traffickingSpindle orientationMotor mutantsMyo2-66Ribosomal subunitMyo2pProtein subunitsPartial colocalizationMicroarray analysisSubunitsSedimentation analysisYeastMRNAComplexesMyosinMutantsPolysomesTraffickingRNAColocalization
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
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
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 brush border myosin‐I and myosin‐Ic expression in human intestine and Caco‐2BBe cells
Skowron J, Bement W, Mooseker M. Human brush border myosin‐I and myosin‐Ic expression in human intestine and Caco‐2BBe cells. Cytoskeleton 1998, 41: 308-324. PMID: 9858156, DOI: 10.1002/(sici)1097-0169(1998)41:4<308::aid-cm4>3.0.co;2-j.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
Human myosin-IXb, an unconventional myosin with a chimerin-like rho/rac GTPase-activating protein domain in its tail
Wirth J, Jensen K, Post P, Bement W, Mooseker M. Human myosin-IXb, an unconventional myosin with a chimerin-like rho/rac GTPase-activating protein domain in its tail. Journal Of Cell Science 1996, 109: 653-661. PMID: 8907710, DOI: 10.1242/jcs.109.3.653.Peer-Reviewed Original ResearchConceptsProtein domainsHL-60 cellsRho/Rac familyNovel N-terminal domainGTPase-activating protein (GAP) domainUnconventional myosin heavy chainRas-like G proteinsPrimary structurePutative actin-binding siteAmino acidsFull-length primary structureSkeletal muscle myosin IIN-terminal domainAmino acid extensionActin-binding siteProtein kinase CNorthern blot analysisMuscle myosin IIRac familyDifferent human tissuesUndifferentiated HL-60 cellsRegulatory domainPutative zincRac GTPaseCell periphery
1995
The mouse Snell's waltzer deafness gene encodes an unconventional myosin required for structural integrity of inner ear hair cells
Avraham K, Hasson T, Steel K, Kingsley D, Russell L, Mooseker M, Copeland N, Jenkins N. The mouse Snell's waltzer deafness gene encodes an unconventional myosin required for structural integrity of inner ear hair cells. Nature Genetics 1995, 11: 369-375. PMID: 7493015, DOI: 10.1038/ng1295-369.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceChromosome InversionCloning, MolecularDeafnessDNA Mutational AnalysisGenes, RecessiveHair Cells, Auditory, InnerHumansMiceMice, Inbred C57BLMice, Mutant StrainsMolecular Sequence DataMyosin Heavy ChainsOrgan of CortiRestriction MappingRNA, MessengerSequence DeletionConceptsMyosin VIUnconventional myosin heavy chainPositional cloning approachInner ear hair cellsHuman deafness disordersExcellent model systemEar hair cellsSensory hair cellsHair cellsDeafness disordersCloning approachUnconventional myosinDeafness mutationsDeafness mutantsDeafness genesMyosin heavy chainGenesGenetic deafnessModel systemHeavy chainStructural integrityWaltzerInner earCellsMutants
1994
Identification and overlapping expression of multiple unconventional myosin genes in vertebrate cell types.
Bement W, Hasson T, Wirth J, Cheney R, Mooseker M. Identification and overlapping expression of multiple unconventional myosin genes in vertebrate cell types. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 11767. PMID: 7972138, PMCID: PMC55655, DOI: 10.1073/pnas.91.24.11767-c.Peer-Reviewed Original ResearchPorcine myosin-VI: characterization of a new mammalian unconventional myosin.
Hasson T, Mooseker M. Porcine myosin-VI: characterization of a new mammalian unconventional myosin. Journal Of Cell Biology 1994, 127: 425-440. PMID: 7929586, PMCID: PMC2120210, DOI: 10.1083/jcb.127.2.425.Peer-Reviewed Original ResearchCloning and mRNA Expression of Human Unconventional Myosin-IC A Homologue of Amoeboid Myosins-I With a Single IQ Motif and an SH3 Domain
Bement W, Wirth J, Mooseker M. Cloning and mRNA Expression of Human Unconventional Myosin-IC A Homologue of Amoeboid Myosins-I With a Single IQ Motif and an SH3 Domain. Journal Of Molecular Biology 1994, 243: 356-363. PMID: 7932763, DOI: 10.1006/jmbi.1994.1662.Peer-Reviewed Original ResearchConceptsSrc homology 3 domainSingle IQ motifIQ motifComplete deduced amino acid sequenceDeduced amino acid sequenceSingle open reading frameC-terminal tailOpen reading frameATP-binding siteAmino acid sequenceMembrane-binding sitesMultiple sequence alignmentNorthern blot analysisSH3 domainCDNA clonesReading frameAcid sequenceSequence alignmentMyosin ICIdentification and overlapping expression of multiple unconventional myosin genes in vertebrate cell types.
Bement W, Hasson T, Wirth J, Cheney R, Mooseker M. Identification and overlapping expression of multiple unconventional myosin genes in vertebrate cell types. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 6549-6553. PMID: 8022818, PMCID: PMC44240, DOI: 10.1073/pnas.91.14.6549.Peer-Reviewed Original ResearchThe Molecular Cloning and Characterization of Drosophila melanogaster Myosin-IA and Myosin-IB
Morgan N, Skovronsky D, Artavanis-Tsakonas S, Mooseker M. The Molecular Cloning and Characterization of Drosophila melanogaster Myosin-IA and Myosin-IB. Journal Of Molecular Biology 1994, 239: 347-356. PMID: 8201616, DOI: 10.1006/jmbi.1994.1376.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCloning, MolecularConsensus SequenceConserved SequenceDrosophila melanogasterGenes, InsectLarvaMolecular Sequence DataMyosinsProtein Structure, TertiaryRNA, MessengerSequence AlignmentSequence Analysis, DNASequence Homology, Amino AcidTranscription, GeneticConceptsDeduced amino acid sequenceKilobase cDNA cloneAmino acid sequenceMyosin IBCDNA clonesIQ motifGene productsAcid sequenceMyosin I familyDrosophila cDNA libraryPrimary sequence analysisMyosin IANorthern blot analysisVertebrate homologsEmbryonic libraryDrosophila melanogasterMolecular cloningSequence comparisonNovel myosinCDNA libraryTail domainHead libraryUnique tailDegenerate primersUnconventional myosinIdentification of a Divergent Actin-related Protein in Drosophila
Frankel S, Heintzelman M, Artavanis-Tsakonas S, Mooseker M. Identification of a Divergent Actin-related Protein in Drosophila. Journal Of Molecular Biology 1994, 235: 1351-1356. PMID: 8308899, DOI: 10.1006/jmbi.1994.1090.Peer-Reviewed Original ResearchConceptsActin-related proteinsAmino acid identityPrimary sequence homologyDivergent actinConventional actinPolytene chromosomesEarly embryogenesisAcid identityX chromosomeSequence homologyGenomic DNAOverall divergenceSequence insertionNew isotypeActinDrosophilaProteinEmbryogenesisChromosomesHomologyGenesStages of developmentTranscriptsUnique locationLater stages
1993
Cloning of a Secretory Gelsolin from Drosophila melanogaster
Heintzelman M, Frankel S, Artavanis-Tsakonas S, Mooseker M. Cloning of a Secretory Gelsolin from Drosophila melanogaster. Journal Of Molecular Biology 1993, 230: 709-716. PMID: 8386771, DOI: 10.1006/jmbi.1993.1191.Peer-Reviewed Original ResearchConceptsSecretory gelsolinAcid sequenceThird instar Drosophila larvaeDeduced amino acid sequenceFull-length complementary DNAInstar Drosophila larvaeClass of proteinsActin-binding proteinsAmino acid sequenceAmino acid residuesGelsolin sequenceThird chromosomeDrosophila melanogasterGelsolin familyCytoplasmic proteinsSignal peptideSingle geneDrosophila larvaeRepeat structureActin filamentsMonomeric actinAcid residuesBarbed endsPrimary structureNorthern blot
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 Research